Takuo Osawa1, Nobuo N Noda1. 1. Institute of Microbial Chemistry (BIKAKEN), Tokyo 141-0021, Japan.
Abstract
The degradation of cytoplasmic components via autophagy is crucial for intracellular homeostasis. In the process of autophagy, a newly synthesized isolation membrane (IM) is developed to sequester degradation targets and eventually the IM seals, forming an autophagosome. One of the most poorly understood autophagy-related proteins is Atg2, which is known to localize to a contact site between the edge of the expanding IM and the exit site of the endoplasmic reticulum (ERES). Recent advances in structural and biochemical analyses have been applied to Atg2 and have revealed it to be a novel multifunctional protein that tethers membranes and transfers phospholipids between them. Considering that Atg2 is essential for the expansion of the IM that requires phospholipids as building blocks, it is suggested that Atg2 transfers phospholipids from the ERES to the IM during the process of autophagosome formation, suggesting that lipid transfer proteins can mediate de novo organelle biogenesis.
The degradation of cytoplasmic components via autophagy is crucial for intracellular homeostasis. In the process of autophagy, a newly synthesized isolation membrane (IM) is developed to sequester degradation targets and eventually the IM seals, forming an autophagosome. One of the most poorly understood autophagy-related proteins is Atg2, which is known to localize to a contact site between the edge of the expanding IM and the exit site of the endoplasmic reticulum (ERES). Recent advances in structural and biochemical analyses have been applied to Atg2 and have revealed it to be a novel multifunctional protein that tethers membranes and transfers phospholipids between them. Considering that Atg2 is essential for the expansion of the IM that requires phospholipids as building blocks, it is suggested that Atg2 transfers phospholipids from the ERES to the IM during the process of autophagosome formation, suggesting that lipid transfer proteins can mediate de novo organelle biogenesis.
Autophagy is a highly conserved catabolic pathway in eukaryotes and occurs by a process of de novo organelle biogenesis.1, 2 In the budding yeast, Saccharomyces cerevisiae, this process starts with the nucleation of an isolation membrane (IM) in the vicinity of a vacuole. The cup‐shaped IM expands and encapsulates various cellular components, including biomolecules such as proteins and nucleic acids, and organelles such as mitochondria, endoplasmic reticulum (ER), and nucleus.3, 4, 5, 6 Finally, the IM becomes a double‐membrane organelle, termed an autophagosome, following the closure of its open mouth. The autophagosome fuses with the vacuole (known as a lysosome in mammals) and releases its inner membrane structure (the autophagic body) into the lumen of the vacuole, whereby the autophagic body together with its inner contents is degraded by vacuolar hydrolases for recycling the components. Autophagosome formation is an extremely important event in autophagy because the autophagy degradation targets are determined during this step. Autophagosome formation has attracted broad interest among researchers specialized in the field of autophagy as well as among cell biologists because this process is rare in the biogenesis of de novo double‐membrane organelles.In budding yeast, dozens of autophagy‐related (Atg) proteins regulate the steps of autophagy through interaction with membranes.7 Of these proteins, 18 are essential for autophagosome formation during starvation‐induced autophagy.1 These essential proteins, termed core Atg proteins, are classified into the following six functional groups: the Atg1–protein kinase complex, Atg2–Atg18 complex, sole transmembrane protein Atg9, autophagy‐specific phosphatidylinositol 3‐kinase (PI3K) complex, Atg12–Atg5 conjugation system, and Atg8–phosphatidylethanolamine (PE) conjugation system.8 The current model of autophagosome formation mediated by these six groups is as follows (Fig. 1): upon autophagy induction, the Atg1 complex functions as a scaffold for constructing the autophagosome formation site, known as the preautophagosomal structure in yeast, and at the same time phosphorylates proteins, including Atg2 and Atg9.9, 10, 11 The Atg9‐containing vesicle, in collaboration with the Atg1 complex, generates an IM precursor, in which the PI3K complex produces phosphatidylinositol 3‐phosphate (PI3P), which then recruits the Atg2–Atg18 complex and two ubiquitin‐like conjugation systems for the expansion and closure of the IM into an autophagosome.1, 12, 13, 14 The conservation of the six functional groups among eukaryotes from yeasts to mammals suggests that the basic mechanism of autophagosome formation is evolutionarily conserved.
Figure 1
Proposed model of autophagosome formation in yeast. Upon autophagy induction, the Atg1 complex consisting of Atg1, Atg13, Atg17, Atg29, and Atg31 forms a higher‐order assemblage that functions as a scaffold for the preautophagosomal structure (PAS), the site of autophagosome formation.10, 11 Atg9 vesicles, which are 30–60 nm in size and contain a transmembrane protein Atg9, are generated from the Golgi apparatus and target to the PAS to become the IM precursor.12 The PI3K complex is then recruited to the PAS and produces PI3P in the IM precursor, which further recruits the Atg2–Atg18 complex and two ubiquitin‐like conjugation systems (Atg8–PE conjugate and Atg12–Atg5–Atg16 complex),14 leading to the expansion and closure of the IM into the autophagosome.
Proposed model of autophagosome formation in yeast. Upon autophagy induction, the Atg1 complex consisting of Atg1, Atg13, Atg17, Atg29, and Atg31 forms a higher‐order assemblage that functions as a scaffold for the preautophagosomal structure (PAS), the site of autophagosome formation.10, 11 Atg9 vesicles, which are 30–60 nm in size and contain a transmembrane protein Atg9, are generated from the Golgi apparatus and target to the PAS to become the IM precursor.12 The PI3K complex is then recruited to the PAS and produces PI3P in the IM precursor, which further recruits the Atg2–Atg18 complex and two ubiquitin‐like conjugation systems (Atg8–PE conjugate and Atg12–Atg5–Atg16 complex),14 leading to the expansion and closure of the IM into the autophagosome.During the expansion of the IM, the Atg2–Atg18 complex localizes to the edge of the IM in a process dependent on PI3P and Atg9. The PROPPIN (β‐propellers that bind polyphosphoinositides) protein Atg18 recognizes PI3P for the recruitment of the Atg2–Atg18 complex to the IM,15 whereas the interaction of Atg9 with Atg2 restricts the localization of the Atg2–Atg18 complex to the edge of the IM.16 At the edge of the IM, the Atg2–Atg18 complex contacts the ER exit site (ERES) by an unknown mechanism, forming a contact site between the IM and ERES.17, 18 Although the physiological implications of the IM–ERES contact and the molecular functions of Atg2 had not been understood, recent advances in the structural and biochemical studies of Atg2 shed light on the critical function of Atg2 in autophagosome formation. This short review focuses on the recent advances in structural and biochemical studies of Atg2 and discusses the molecular mechanisms of the expansion of the IM, one of the biggest mysteries in the field of autophagy.
A Brief History of Atg2 Analysis in the Prestructural Era
In 1993, the screening of S. cerevisiae autophagy‐defective mutants led to the identification of 13 apg genes required for autophagy, including apg2, later renamed to atg2.19 Eight years later, the atg2 gene was cloned, and the essential role of the gene product, Atg2 protein, in autophagosome formation was established.20, 21 At that time, the affinity of Atg2 to the membranes was already implicit in its behavior as a peripheral membrane protein. However, the molecular functions of Atg2 were not elucidated for another 10 years. In 2012, studies on a mammalianAtg2 homolog, ATG2A, revealed that the C‐terminal portion of ATG2A is required for the localization of this protein to lipid droplets,22 and the lipid droplet localization was later confirmed by another group.23 These findings suggested that Atg2 has some affinity to lipids, but its significance in autophagy remains unclear. In 2013, Atg2 was shown to localize to the IM–ERES contact site,17, 18 an observation which indicated a critical role of Atg2 in autophagosomal membrane expansion. In 2017, the movement of the ER‐staining dye R18 from the ER to IM precursors was shown to be completely blocked by the deletion of Atg2,24 further suggesting a critical role of Atg2 in supplying lipids to the IM, although the molecular mechanisms involved remained unknown.
Shape of the Atg2–Atg18 Complex
Although structural studies on the core Atg proteins have significantly progressed in the last 15 years,25, 26, 27 the structure of Atg2 remained unsolved until 2017 due to its large size, 180 kDa in budding yeast, and the tendency of proteins to aggregate, making crystallization and NMR analysis difficult. However, recent advances in electron microscopy (EM) enabled the imaging of the mammalianAtg2–Atg18 complex at a low resolution.28, 29 Mammals have two Atg2 homologs (ATG2A and 2B) and four Atg18 homologs, known as WD repeat domain phosphoinositide‐interacting proteins (WIPI) 1–4.22, 30 Negative‐staining EM analysis of the ATG2A–WIPI4 complex (WIPI4 is also known as WDR45) and the ATG2B–WIPI4 complex revealed the overall shape of this protein complex (Fig. 2, left).28, 29 ATG2 has a rod‐like structure with a length of approximately 20 nm. The N terminus of ATG2 corresponds to one end of the rod, and the middle region of ATG2 forms the other end of the rod, binding to WIPI4 using an aromatic Y/HF motif.29 The C‐terminal half appears to go back to the N terminus, thereby producing an antiparallel topology, although the precise location of the C terminus of ATG2 in the rod structure is unclear due to its flexible conformation. Atg18 homologs belong to the PROPPIN family, which has a seven‐bladed β‐propeller fold with two phosphoinositide‐binding pockets that have been clearly characterized using high‐resolution crystal structures of Atg18 homologs.31, 32, 33, 34, 35 The β‐propeller ring of WIPI4 binds to one end of the ATG2 rod. Thus, the overall shape of the ATG2–WIPI4 complex looks like a golf club.28, 29 This architecture is roughly similar to a multiple‐subunit tethering complex, such as homotypic fusion and vacuole protein sorting,36 but the lack of high‐resolution structural information for Atg2 hampers further elucidation of the molecular functions of this complex family during autophagosome formation.
Figure 2
Structure of Atg2. Left, shape of the ATG2A–WIPI4 complex revealed by negative‐staining EM (EMDB ID 8899).28 Ribbon model represents the crystal structure of WIPI3 (PDB ID 6IYY)35 manually fitted into the EM image. Atg2‐family proteins have a rod‐like shape with ~20 nm in length and bind to ERES using one end and to IM using the opposite end, thereby tethering ERES to IM. Right, crystal structure of SpAtg2NR (ribbon model) complexed with PE (stick model) (PDB ID 6A9J).41 PE is bound to the hydrophobic cavity of SpAtg2NR using the acyl chains. The side‐chain of the arginine residue that interacts with the phosphoryl group of PE is shown with a stick model. Nitrogen and oxygen atoms are colored blue and red, respectively. N represents the N terminus.
Structure of Atg2. Left, shape of the ATG2A–WIPI4 complex revealed by negative‐staining EM (EMDB ID 8899).28 Ribbon model represents the crystal structure of WIPI3 (PDB ID 6IYY)35 manually fitted into the EM image. Atg2‐family proteins have a rod‐like shape with ~20 nm in length and bind to ERES using one end and to IM using the opposite end, thereby tethering ERES to IM. Right, crystal structure of SpAtg2NR (ribbon model) complexed with PE (stick model) (PDB ID 6A9J).41 PE is bound to the hydrophobic cavity of SpAtg2NR using the acyl chains. The side‐chain of the arginine residue that interacts with the phosphoryl group of PE is shown with a stick model. Nitrogen and oxygen atoms are colored blue and red, respectively. N represents the N terminus.
Establishment of the Membrane‐Tethering Activity of Atg2
In parallel with the structural studies, the biochemical studies of Atg2 using purified proteins began to unveil the specific functions of Atg2. Purified ATG2B was found to bind to liposomes in a PI3P‐independent manner, in contrast to purified WIPI4 that requires a relatively large amount (∼15%) of PI3P for liposome binding.29 In these experiments, the membrane curvature of the liposomes did not affect the interaction. In addition, purified ATG2A was shown to bind to liposomes in a PI3P‐independent manner.28 In contrast to ATG2B, however, the size of liposomes markedly affected their affinity to ATG2A. ATG2A was strongly bound to small unilamellar vesicles (SUVs) but less strongly to large unilamellar vesicles (LUVs). Importantly, the size of SUVs was increased in the presence of ATG2A, but not when proteinase K was added, suggesting that ATG2A exhibits membrane‐tethering (MT) activity.28 Moreover, the ATG2A–WIPI4 complex could mediate the tethering of LUVs containing PI3P. EM analysis of the ATG2A–WIPI4 complex with SUVs revealed that one ATG2A binds to two liposomes using both the ends, thereby bridging them,28 further confirming that ATG2A alone exhibits MT activity. The MT activity was observed for S. cerevisiaeAtg2 as well.37 Purified Atg2 showed binding to SUVs but not to LUVs in a PI3P‐independent manner. Moreover, purified Atg2 showed an MT activity for SUVs. All these activities are consistent with those observed for ATG2A. Truncation analysis identified two membrane‐binding regions in Atg2, one at the N terminus, involving residues 2–21, and the other at the C terminus, involving residues 1347–1592.37 Although each binding site alone was sufficient for binding to SUVs, both sites were required for tethering SUVs, indicating that Atg2 tethers SUVs using these two binding regions. Both binding regions were shown to be important for autophagy.37 Furthermore, the existence of two membrane‐binding regions in ATG2A was suggested by truncational analysis in vivo.38 The IM edge and ERES assume a high curvature39 and PI3P is enriched in the IM.40 Moreover, the N‐terminal portion of Atg2 was shown to be sufficient for targeting green fluorescent protein (GFP) to the ER.37 These observations suggest that the Atg2–Atg18 complex binds to both IM and ERES, thereby tethering them to each other.
Atomic Resolution Structure of the N‐Terminal Region of Atg2
To date, although the full‐length Atg2 has not been crystallized, the N‐terminal region of Schizosaccharomyces pombeAtg2 (SpAtg2NR), which contains an evolutionarily conserved region termed Chorein_N, was recently crystallized and its crystal structure was determined.41 SpAtg2NR comprises a helical region and a twisted β‐sheet, which fold into a globular structure with a large hydrophobic cavity. Mixing SpAtg2NR and PE resulted in the formation of a SpAtg2NR–PE complex, whose structure was determined at 2.7 Å resolution (Fig. 2, right).41 A single PE molecule binds to SpAtg2NR with its acyl chains buried within the hydrophobic cavity of SpAtg2NR, whereas the head group of the PE is exposed to the solvent. The phosphoryl group of the PE specifically interacts with the arginine residue of SpAtg2NR although this electrostatic interaction is not required for autophagy. The phospholipid‐binding mode of SpAtg2NR resembles that of synaptotagmin‐like mitochondrial lipid‐binding protein (SMP) domains, despite little topological similarity between them. The SMP domain is found in proteins, such as the ER–mitochondria encounter structure (ERMES) complex and extended synaptotagmins, both of which are localized at membrane contact sites and appear to transfer phospholipids between organelles.42 Moreover, SpAtg2NR showed high structural similarity to the N‐terminal region of Vps13, which also contains Chorein_N.43 Vps13 is a multifunctional protein that has been suggested to mediate lipid transfer (LT) at various organelle contact sites.44 These observations strongly suggest that Atg2 is an LT protein that functions at the IM–ERES contact site.
Discovery of the Phospholipid Transfer Activity of Atg2
LT assays using liposomes that contain fluorescently labeled phospholipids have demonstrated that Atg2 transfers phospholipids.41 The size of liposomes is important for the LT activity, and Atg2 shows strong LT activity only among SUVs. Considering that the tethering activity of Atg2 is restricted to SUVs, it appears that Atg2 transfers phospholipids between liposomes that are tethered to each other by the same Atg2 molecule. Most of the known LT proteins, such as those with SMP domains, have been experimentally shown to transfer lipids without tethering membranes. In terms of the close relationship between MT and LT activities, Atg2 is a novel type of LT protein. Atg18 itself showed no LT activity, but promoted the LT activity of Atg2, and in the presence of Atg18, PI3P further enhanced the LT activity of Atg2.41 Because the LT activity of Atg2 is proportional to its MT activity, Atg18 may promote the LT activity of Atg2 by enhancing its MT activity. Considering that Atg2 localizes to the IM–ERES contact site, it is proposed that Atg2 mediates tethering of the IM to ERES and simultaneously transfers phospholipids between them.In vitro LT activity was also confirmed for humanATG2A45, 46 and ATG2B (Osawa and Noda, unpublished observation). ATG2A bridges SUVs and transfers phospholipids between them, which is accelerated by the addition of PI3P together with WIPI proteins.45 Moreover, ATG2A was shown to localize to autophagosome–ER contact sites in mammalian cells.46 These observations are consistent with those observed for yeastAtg2, suggesting that the LT and MT activities of Atg2 and their role in autophagy are evolutionarily conserved.
Role of Atg2NR in Phospholipid Transfer
Atg2NR binds to a variety of phospholipids, including PE, phosphatidylcholine, and phosphatidylserine with low specificity.41 Conversely, the LT activity of Atg2NR is much lower than that of the full‐length Atg2, implying that a region other than Atg2NR is required for efficient phospholipid transfer. Together with the observation that Atg2NR is located at the one end of the rod‐like architecture and Atg2 tethers two membranes using both ends, it is proposed that Atg2NR functions as an extractor of phospholipids from one membrane. The substitution of the conserved basic residues at the surface of Atg2NR with acidic residues caused significant reduction in the MT and LT activities of Atg2.41 Although the basic residues of Atg2NR are not conserved in Vps13, a chimeric Atg2 involving the Chorein_N of Vps13, instead of the intrinsic Chorein_N, exhibited the same autophagic activity as wild‐type Atg2.41 The Chorein_N regions of Atg2 and Vps13 possess high structural similarity to each other and conserve a hydrophobic cavity despite the low sequence similarity.41, 43 Chorein_N may function to extract phospholipids from membranes as a prerequisite to LT. In humans, the dysfunction of VPS13A causes a neurodegenerative disorder, Chorea‐acanthocytosis.47 Some of the missense mutations in VPS13A, which are found in Chorea‐acanthocytosis patients, are located in the Chorein_N region,48 suggesting that a defect of phospholipid transfer at organelle contact sites may be one of the causes of some neurodegenerative disorders.
Proposed Mechanism of Phospholipid Transfer Mediated by Atg2
How does Atg2 transfer phospholipids from ERES to the IM? Because the MT activity is indispensable for the LT activity of Atg2, a well‐known LT system, in which LT proteins shuttle between organelles,49 does not appear to apply to Atg2. As described above, Atg2‐mediated LT requires the region downstream of Atg2NR, which has been predicted to contain five repeated structures.41 These repeated structures are formed mainly by β‐strands rich in hydrophobic residues, suggesting that they might have a fold similar to the β‐jellyroll that harbors a hydrophobic groove. Among the five repeats, the most C‐terminal repeat contains a conserved ATG2_CAD region, which appears, from EM analyses, to form the IM‐binding surface together with Atg18.28 An attractive model is that Atg2NR and the five repeated structures constitute a successive hydrophobic groove that functions as a pathway for phospholipids; phospholipids move from ERES to the IM by sliding the hydrophobic acyl chains along the hydrophobic groove while exposing the hydrophilic head groups to the cytosol (Fig. 3, right). Indeed, recent Cryo‐EM analysis of ATG2A at 15 Å resolution proposed the existence of hydrophobic grooves or cavities throughout the rod structure although their consecutiveness remained elusive.46 A long hydrophobic groove has been observed in other LT protein complexes. The Lpt complex comprises seven components, named LptA–G, and it transfers lipopolysaccharides (LPSs) across the periplasm in bacteria.50 In the Lpt complex, LptA, LptC, and LptD are equipped with β‐jellyroll domains, which stack upon each other to form a hydrophobic pathway, that enable LPS molecules to cross the periplasm. The ERMES complex comprises four subunits (Mdm12, Mdm35, Mdm10, and Mmm1) and mediates phospholipid transfer between mitochondria and the ER.51 Mdm12 and Mmm1, both of which possess SMP domains, form a tubular tetramer in a 2:2 manner, which produce a successive hydrophobic cleft through the four molecules although the significance of the long cleft remains to be established.52 These examples suggest that a long hydrophobic groove within a protein or protein complex could function as a pathway for LT. It is necessary to experimentally validate whether Atg2 has a similar long hydrophobic groove and the groove, if it exists, mediates phospholipid transfer between membranes that are bridged by Atg2.
Figure 3
Distinct models of supplying phospholipids for autophagosome formation. Left, direct connection model. Phospholipids in the ER move to the IM through direct connection. Middle, vesicle‐mediated model. Fusion of vesicles derived from ER or other membrane source organelles with the IM provides phospholipids. Right, Atg2‐mediated model. Phospholipids in the ER move to the IM through Atg2. Among these models, the Atg2‐mediated model seems to be suitable for transferring phospholipids while excluding the influx of membrane proteins, which are abundant in ER and other membrane source organelles, to the IM.
Distinct models of supplying phospholipids for autophagosome formation. Left, direct connection model. Phospholipids in the ER move to the IM through direct connection. Middle, vesicle‐mediated model. Fusion of vesicles derived from ER or other membrane source organelles with the IM provides phospholipids. Right, Atg2‐mediated model. Phospholipids in the ER move to the IM through Atg2. Among these models, the Atg2‐mediated model seems to be suitable for transferring phospholipids while excluding the influx of membrane proteins, which are abundant in ER and other membrane source organelles, to the IM.To expand the IM, Atg2 must mediate a unidirectional transfer of phospholipids from ERES to IM. Atg18 and Atg9 might determine the flow direction of the phospholipids by fixing the orientation of Atg2: Atg18 binds to one end of Atg2, which is opposite to Atg2NR, and recognizes PI3P existing in the IM.15, 28, 29 Atg9 localizes to the edge of the IM and interacts with Atg2 at the edge.16 These interactions localize the Atg2–Atg18–Atg9 complex at the edge of the IM and, at the same time, orient Atg2NR toward ERES, possibly allowing Atg2NR to interact with ERES but not with IM and extract phospholipids only from ERES.
Proposed Mechanism of De Novo Autophagosome Biogenesis
Autophagosomes, 0.3–0.9 μm in size, are formed within 10 min in yeast.53, 54, 55 Compared with other organelle membranes, autophagosomal membranes contain few membrane proteins.56 Because the role of autophagosomes is restricted to deliver substrates to lysosomes/vacuoles for degradation, a minimum number of membrane proteins would be sufficient for the functioning of autophagosomes. Several mechanisms have been proposed for membrane supply during autophagosome formation, including direct connections between the IM and ER, and vesicular transport (Fig. 3).57, 58, 59, 60 One of the biggest shortcomings of these models is that it would be difficult to supply lipids while excluding membrane proteins that are abundant in membrane source organelles, including the ER. An Atg2‐mediated lipid supply appears more likely because Atg2 could transfer lipids while blocking the influx of membrane proteins to the IM. To construct the autophagosomal membranes, significant amounts of phospholipid molecules (more than a million) are required as building blocks. Currently, it is unclear what percentage of phospholipids in an autophagosome is provided by the LT activity of Atg2. If most phospholipids are provided by the LT activity of Atg2, Atg2 must mediate a fairly rapid transfer of phospholipids from the ER and other membrane source organelles to the IM. Because Atg2 itself does not use energy for LT, mechanisms including other unknown proteins would be required for ensuring the unidirectional, highly efficient phospholipid transfer that is needed for de novo autophagosome biogenesis.
Conclusions
Recent advances in structural biology and biochemical studies have shed light on the molecular functions of Atg2, one of the most poorly understood proteins in the field of autophagy. Thus, the finding that Atg2 is a novel type of phospholipid transfer protein, bridging two membranes and at the same time transferring phospholipids between them, is unexpected and provides a novel model of autophagosome formation: LT proteins supply phospholipids from membrane source organelles as building blocks for autophagosome formation. Although technically difficult, in vivo visualization of phospholipid movement from the ER to IM via Atg2 and atomic resolution structural determination of the full‐length Atg2 will provide further mechanistic insights into Atg2 function solving one of the biggest questions in autophagy: the mechanism of de novo autophagosome biogenesis.
Authors: Yi Xin Iris Tu; Andrew M Sydor; Etienne Coyaud; Estelle M N Laurent; Diana Dyer; Nora Mellouk; Jonathan St-Germain; Robert M Vernon; Julie D Forman-Kay; Taoyingnan Li; Rong Hua; Kexin Zhao; Neale D Ridgway; Peter K Kim; Brian Raught; John H Brumell Journal: Autophagy Date: 2021-09-15 Impact factor: 13.391
Authors: Daniel J Klionsky; Amal Kamal Abdel-Aziz; Sara Abdelfatah; Mahmoud Abdellatif; Asghar Abdoli; Steffen Abel; Hagai Abeliovich; Marie H Abildgaard; Yakubu Princely Abudu; Abraham Acevedo-Arozena; Iannis E Adamopoulos; Khosrow Adeli; Timon E Adolph; Annagrazia Adornetto; Elma Aflaki; Galila Agam; Anupam Agarwal; Bharat B Aggarwal; Maria Agnello; Patrizia Agostinis; Javed N Agrewala; Alexander Agrotis; Patricia V Aguilar; S Tariq Ahmad; Zubair M Ahmed; Ulises Ahumada-Castro; Sonja Aits; Shu Aizawa; Yunus Akkoc; Tonia Akoumianaki; Hafize Aysin Akpinar; Ahmed M Al-Abd; Lina Al-Akra; Abeer Al-Gharaibeh; Moulay A Alaoui-Jamali; Simon Alberti; Elísabet Alcocer-Gómez; Cristiano Alessandri; Muhammad Ali; M Abdul Alim Al-Bari; Saeb Aliwaini; Javad Alizadeh; Eugènia Almacellas; Alexandru Almasan; Alicia Alonso; Guillermo D Alonso; Nihal Altan-Bonnet; Dario C Altieri; Élida M C Álvarez; Sara Alves; Cristine Alves da Costa; Mazen M Alzaharna; Marialaura Amadio; Consuelo Amantini; Cristina Amaral; Susanna Ambrosio; Amal O Amer; Veena Ammanathan; Zhenyi An; Stig U Andersen; Shaida A Andrabi; Magaiver Andrade-Silva; Allen M Andres; Sabrina Angelini; David Ann; Uche C Anozie; Mohammad Y Ansari; Pedro Antas; Adam Antebi; Zuriñe Antón; Tahira Anwar; Lionel Apetoh; Nadezda Apostolova; Toshiyuki Araki; Yasuhiro Araki; Kohei Arasaki; Wagner L Araújo; Jun Araya; Catherine Arden; Maria-Angeles Arévalo; Sandro Arguelles; Esperanza Arias; Jyothi Arikkath; Hirokazu Arimoto; Aileen R Ariosa; Darius Armstrong-James; Laetitia Arnauné-Pelloquin; Angeles Aroca; Daniela S Arroyo; Ivica Arsov; Rubén Artero; Dalia Maria Lucia Asaro; Michael Aschner; Milad Ashrafizadeh; Osnat Ashur-Fabian; Atanas G Atanasov; Alicia K Au; Patrick Auberger; Holger W Auner; Laure Aurelian; Riccardo Autelli; Laura Avagliano; Yenniffer Ávalos; Sanja Aveic; Célia Alexandra Aveleira; Tamar Avin-Wittenberg; Yucel Aydin; Scott Ayton; Srinivas Ayyadevara; Maria Azzopardi; Misuzu Baba; Jonathan M Backer; Steven K Backues; Dong-Hun Bae; Ok-Nam Bae; Soo Han Bae; Eric H Baehrecke; Ahruem Baek; Seung-Hoon Baek; Sung Hee Baek; Giacinto Bagetta; Agnieszka Bagniewska-Zadworna; Hua Bai; Jie Bai; Xiyuan Bai; Yidong Bai; Nandadulal Bairagi; Shounak Baksi; Teresa Balbi; Cosima T Baldari; Walter Balduini; Andrea Ballabio; Maria Ballester; Salma Balazadeh; Rena Balzan; Rina Bandopadhyay; Sreeparna Banerjee; Sulagna Banerjee; Ágnes Bánréti; Yan Bao; Mauricio S Baptista; Alessandra Baracca; Cristiana Barbati; Ariadna Bargiela; Daniela Barilà; Peter G Barlow; Sami J Barmada; Esther Barreiro; George E Barreto; Jiri Bartek; Bonnie Bartel; Alberto Bartolome; Gaurav R Barve; Suresh H Basagoudanavar; Diane C Bassham; Robert C Bast; Alakananda Basu; Henri Batoko; Isabella Batten; Etienne E Baulieu; Bradley L Baumgarner; Jagadeesh Bayry; Rupert Beale; Isabelle Beau; Florian Beaumatin; Luiz R G Bechara; George R Beck; Michael F Beers; Jakob Begun; Christian Behrends; Georg M N Behrens; Roberto Bei; Eloy Bejarano; Shai Bel; Christian Behl; Amine Belaid; Naïma Belgareh-Touzé; Cristina Bellarosa; Francesca Belleudi; Melissa Belló Pérez; Raquel Bello-Morales; Jackeline Soares de Oliveira Beltran; Sebastián Beltran; Doris Mangiaracina Benbrook; Mykolas Bendorius; Bruno A Benitez; Irene Benito-Cuesta; Julien Bensalem; Martin W Berchtold; Sabina Berezowska; Daniele Bergamaschi; Matteo Bergami; Andreas Bergmann; Laura Berliocchi; Clarisse Berlioz-Torrent; Amélie Bernard; Lionel Berthoux; Cagri G Besirli; Sebastien Besteiro; Virginie M Betin; Rudi Beyaert; Jelena S Bezbradica; Kiran Bhaskar; Ingrid Bhatia-Kissova; Resham Bhattacharya; Sujoy Bhattacharya; Shalmoli Bhattacharyya; Md Shenuarin Bhuiyan; Sujit Kumar Bhutia; Lanrong Bi; Xiaolin Bi; Trevor J Biden; Krikor Bijian; Viktor A Billes; Nadine Binart; Claudia Bincoletto; Asa B Birgisdottir; Geir Bjorkoy; Gonzalo Blanco; Ana Blas-Garcia; Janusz Blasiak; Robert Blomgran; Klas Blomgren; Janice S Blum; Emilio Boada-Romero; Mirta Boban; Kathleen Boesze-Battaglia; Philippe Boeuf; Barry Boland; Pascale Bomont; Paolo Bonaldo; Srinivasa Reddy Bonam; Laura Bonfili; Juan S Bonifacino; Brian A Boone; Martin D Bootman; Matteo Bordi; Christoph Borner; Beat C Bornhauser; Gautam Borthakur; Jürgen Bosch; Santanu Bose; Luis M Botana; Juan Botas; Chantal M Boulanger; Michael E Boulton; Mathieu Bourdenx; Benjamin Bourgeois; Nollaig M Bourke; Guilhem Bousquet; Patricia Boya; Peter V Bozhkov; Luiz H M Bozi; Tolga O Bozkurt; Doug E Brackney; Christian H Brandts; Ralf J Braun; Gerhard H Braus; Roberto Bravo-Sagua; José M Bravo-San Pedro; Patrick Brest; Marie-Agnès Bringer; Alfredo Briones-Herrera; V Courtney Broaddus; Peter Brodersen; Jeffrey L Brodsky; Steven L Brody; Paola G Bronson; Jeff M Bronstein; Carolyn N Brown; Rhoderick E Brown; Patricia C Brum; John H Brumell; Nicola Brunetti-Pierri; Daniele Bruno; Robert J Bryson-Richardson; Cecilia Bucci; Carmen Buchrieser; Marta Bueno; Laura Elisa Buitrago-Molina; Simone Buraschi; Shilpa Buch; J Ross Buchan; Erin M Buckingham; Hikmet Budak; Mauricio Budini; Geert Bultynck; Florin Burada; Joseph R Burgoyne; M Isabel Burón; Victor Bustos; Sabrina Büttner; Elena Butturini; Aaron Byrd; Isabel Cabas; Sandra Cabrera-Benitez; Ken Cadwell; Jingjing Cai; Lu Cai; Qian Cai; Montserrat Cairó; Jose A Calbet; Guy A Caldwell; Kim A Caldwell; Jarrod A Call; Riccardo Calvani; Ana C Calvo; Miguel Calvo-Rubio Barrera; Niels Os Camara; Jacques H Camonis; Nadine Camougrand; Michelangelo Campanella; Edward M Campbell; François-Xavier Campbell-Valois; Silvia Campello; Ilaria Campesi; Juliane C Campos; Olivier Camuzard; Jorge Cancino; Danilo Candido de Almeida; Laura Canesi; Isabella Caniggia; Barbara Canonico; Carles Cantí; Bin Cao; Michele Caraglia; Beatriz Caramés; Evie H Carchman; Elena Cardenal-Muñoz; Cesar Cardenas; Luis Cardenas; Sandra M Cardoso; Jennifer S Carew; Georges F Carle; Gillian Carleton; Silvia Carloni; Didac Carmona-Gutierrez; Leticia A Carneiro; Oliana Carnevali; Julian M Carosi; Serena Carra; Alice Carrier; Lucie Carrier; Bernadette Carroll; A Brent Carter; Andreia Neves Carvalho; Magali Casanova; Caty Casas; Josefina Casas; Chiara Cassioli; Eliseo F Castillo; Karen Castillo; Sonia Castillo-Lluva; Francesca Castoldi; Marco Castori; Ariel F Castro; Margarida Castro-Caldas; Javier Castro-Hernandez; Susana Castro-Obregon; Sergio D Catz; Claudia Cavadas; Federica Cavaliere; Gabriella Cavallini; Maria Cavinato; Maria L Cayuela; Paula Cebollada Rica; Valentina Cecarini; Francesco Cecconi; Marzanna Cechowska-Pasko; Simone Cenci; Victòria Ceperuelo-Mallafré; João J Cerqueira; Janete M Cerutti; Davide Cervia; Vildan Bozok Cetintas; Silvia Cetrullo; Han-Jung Chae; Andrei S Chagin; Chee-Yin Chai; Gopal Chakrabarti; Oishee Chakrabarti; Tapas Chakraborty; Trinad Chakraborty; Mounia Chami; Georgios Chamilos; David W Chan; Edmond Y W Chan; Edward D Chan; H Y Edwin Chan; Helen H Chan; Hung Chan; Matthew T V Chan; Yau Sang Chan; Partha K Chandra; Chih-Peng Chang; Chunmei Chang; Hao-Chun Chang; Kai Chang; Jie Chao; Tracey Chapman; Nicolas Charlet-Berguerand; Samrat Chatterjee; Shail K Chaube; Anu Chaudhary; Santosh Chauhan; Edward Chaum; Frédéric Checler; Michael E Cheetham; Chang-Shi Chen; Guang-Chao Chen; Jian-Fu Chen; Liam L Chen; Leilei Chen; Lin Chen; Mingliang Chen; Mu-Kuan Chen; Ning Chen; Quan Chen; Ruey-Hwa Chen; Shi Chen; Wei Chen; Weiqiang Chen; Xin-Ming Chen; Xiong-Wen Chen; Xu Chen; Yan Chen; Ye-Guang Chen; Yingyu Chen; Yongqiang Chen; Yu-Jen Chen; Yue-Qin Chen; Zhefan Stephen Chen; Zhi Chen; Zhi-Hua Chen; Zhijian J Chen; Zhixiang Chen; Hanhua Cheng; Jun Cheng; Shi-Yuan Cheng; Wei Cheng; Xiaodong Cheng; Xiu-Tang Cheng; Yiyun Cheng; Zhiyong Cheng; Zhong Chen; Heesun Cheong; Jit Kong Cheong; Boris V Chernyak; Sara Cherry; Chi Fai Randy Cheung; Chun Hei Antonio Cheung; King-Ho Cheung; Eric Chevet; Richard J Chi; Alan Kwok Shing Chiang; Ferdinando Chiaradonna; Roberto Chiarelli; Mario Chiariello; Nathalia Chica; Susanna Chiocca; Mario Chiong; Shih-Hwa Chiou; Abhilash I Chiramel; Valerio Chiurchiù; Dong-Hyung Cho; Seong-Kyu Choe; Augustine M K Choi; Mary E Choi; Kamalika Roy Choudhury; Norman S Chow; Charleen T Chu; Jason P Chua; John Jia En Chua; Hyewon Chung; Kin Pan Chung; Seockhoon Chung; So-Hyang Chung; Yuen-Li Chung; Valentina Cianfanelli; Iwona A Ciechomska; Mariana Cifuentes; Laura Cinque; Sebahattin Cirak; Mara Cirone; Michael J Clague; Robert Clarke; Emilio Clementi; Eliana M Coccia; Patrice Codogno; Ehud Cohen; Mickael M Cohen; Tania Colasanti; Fiorella Colasuonno; Robert A Colbert; Anna Colell; Miodrag Čolić; Nuria S Coll; Mark O Collins; María I Colombo; Daniel A Colón-Ramos; Lydie Combaret; Sergio Comincini; Márcia R Cominetti; Antonella Consiglio; Andrea Conte; Fabrizio Conti; Viorica Raluca Contu; Mark R Cookson; Kevin M Coombs; Isabelle Coppens; Maria Tiziana Corasaniti; Dale P Corkery; Nils Cordes; Katia Cortese; Maria do Carmo Costa; Sarah Costantino; Paola Costelli; Ana Coto-Montes; Peter J Crack; Jose L Crespo; Alfredo Criollo; Valeria Crippa; Riccardo Cristofani; Tamas Csizmadia; Antonio Cuadrado; Bing Cui; Jun Cui; Yixian Cui; Yong Cui; Emmanuel Culetto; Andrea C Cumino; Andrey V Cybulsky; Mark J Czaja; Stanislaw J Czuczwar; Stefania D'Adamo; Marcello D'Amelio; Daniela D'Arcangelo; Andrew C D'Lugos; Gabriella D'Orazi; James A da Silva; Hormos Salimi Dafsari; Ruben K Dagda; Yasin Dagdas; Maria Daglia; Xiaoxia Dai; Yun Dai; Yuyuan Dai; Jessica Dal Col; Paul Dalhaimer; Luisa Dalla Valle; Tobias Dallenga; Guillaume Dalmasso; Markus Damme; Ilaria Dando; Nico P Dantuma; April L Darling; Hiranmoy Das; Srinivasan Dasarathy; Santosh K Dasari; Srikanta Dash; Oliver Daumke; Adrian N Dauphinee; Jeffrey S Davies; Valeria A Dávila; Roger J Davis; Tanja Davis; Sharadha Dayalan Naidu; Francesca De Amicis; Karolien De Bosscher; Francesca De Felice; Lucia De Franceschi; Chiara De Leonibus; Mayara G de Mattos Barbosa; Guido R Y De Meyer; Angelo De Milito; Cosimo De Nunzio; Clara De Palma; Mauro De Santi; Claudio De Virgilio; Daniela De Zio; Jayanta Debnath; Brian J DeBosch; Jean-Paul Decuypere; Mark A Deehan; Gianluca Deflorian; James DeGregori; Benjamin Dehay; Gabriel Del Rio; Joe R Delaney; Lea M D Delbridge; Elizabeth Delorme-Axford; M Victoria Delpino; Francesca Demarchi; Vilma Dembitz; Nicholas D Demers; Hongbin Deng; Zhiqiang Deng; Joern Dengjel; Paul Dent; Donna Denton; Melvin L DePamphilis; Channing J Der; Vojo Deretic; Albert Descoteaux; Laura Devis; Sushil Devkota; Olivier Devuyst; Grant Dewson; Mahendiran Dharmasivam; Rohan Dhiman; Diego di Bernardo; Manlio Di Cristina; Fabio Di Domenico; Pietro Di Fazio; Alessio Di Fonzo; Giovanni Di Guardo; Gianni M Di Guglielmo; Luca Di Leo; Chiara Di Malta; Alessia Di Nardo; Martina Di Rienzo; Federica Di Sano; George Diallinas; Jiajie Diao; Guillermo Diaz-Araya; Inés Díaz-Laviada; Jared M Dickinson; Marc Diederich; Mélanie Dieudé; Ivan Dikic; Shiping Ding; Wen-Xing Ding; Luciana Dini; Jelena Dinić; Miroslav Dinic; Albena T Dinkova-Kostova; Marc S Dionne; Jörg H W Distler; Abhinav Diwan; Ian M C Dixon; Mojgan Djavaheri-Mergny; Ina Dobrinski; Oxana Dobrovinskaya; Radek Dobrowolski; Renwick C J Dobson; Jelena Đokić; Serap Dokmeci Emre; Massimo Donadelli; Bo Dong; Xiaonan Dong; Zhiwu Dong; Gerald W Dorn Ii; Volker Dotsch; Huan Dou; Juan Dou; Moataz Dowaidar; Sami Dridi; Liat Drucker; Ailian Du; Caigan Du; Guangwei Du; Hai-Ning Du; Li-Lin Du; André du Toit; Shao-Bin Duan; Xiaoqiong Duan; Sónia P Duarte; Anna Dubrovska; Elaine A Dunlop; Nicolas Dupont; Raúl V Durán; Bilikere S Dwarakanath; Sergey A Dyshlovoy; Darius Ebrahimi-Fakhari; Leopold Eckhart; Charles L Edelstein; Thomas Efferth; Eftekhar Eftekharpour; Ludwig Eichinger; Nabil Eid; Tobias Eisenberg; N Tony Eissa; Sanaa Eissa; Miriam Ejarque; Abdeljabar El Andaloussi; Nazira El-Hage; Shahenda El-Naggar; Anna Maria Eleuteri; Eman S El-Shafey; Mohamed Elgendy; Aristides G Eliopoulos; María M Elizalde; Philip M Elks; Hans-Peter Elsasser; Eslam S Elsherbiny; Brooke M Emerling; N C Tolga Emre; Christina H Eng; Nikolai Engedal; Anna-Mart Engelbrecht; Agnete S T Engelsen; Jorrit M Enserink; Ricardo Escalante; Audrey Esclatine; Mafalda Escobar-Henriques; Eeva-Liisa Eskelinen; Lucile Espert; Makandjou-Ola Eusebio; Gemma Fabrias; Cinzia Fabrizi; Antonio Facchiano; Francesco Facchiano; Bengt Fadeel; Claudio Fader; Alex C Faesen; W Douglas Fairlie; Alberto Falcó; Bjorn H Falkenburger; Daping Fan; Jie Fan; Yanbo Fan; Evandro F Fang; Yanshan Fang; Yognqi Fang; Manolis Fanto; Tamar Farfel-Becker; Mathias Faure; Gholamreza Fazeli; Anthony O Fedele; Arthur M Feldman; Du Feng; Jiachun Feng; Lifeng Feng; Yibin Feng; Yuchen Feng; Wei Feng; Thais Fenz Araujo; Thomas A Ferguson; Álvaro F Fernández; Jose C Fernandez-Checa; Sonia Fernández-Veledo; Alisdair R Fernie; Anthony W Ferrante; Alessandra Ferraresi; Merari F Ferrari; Julio C B Ferreira; Susan Ferro-Novick; Antonio Figueras; Riccardo Filadi; Nicoletta Filigheddu; Eduardo Filippi-Chiela; Giuseppe Filomeni; Gian Maria Fimia; Vittorio Fineschi; Francesca Finetti; Steven Finkbeiner; Edward A Fisher; Paul B Fisher; Flavio Flamigni; Steven J Fliesler; Trude H Flo; Ida Florance; Oliver Florey; Tullio Florio; Erika Fodor; Carlo Follo; Edward A Fon; Antonella Forlino; Francesco Fornai; Paola Fortini; Anna Fracassi; Alessandro Fraldi; Brunella Franco; Rodrigo Franco; Flavia Franconi; Lisa B Frankel; Scott L Friedman; Leopold F Fröhlich; Gema Frühbeck; Jose M Fuentes; Yukio Fujiki; Naonobu Fujita; Yuuki Fujiwara; Mitsunori Fukuda; Simone Fulda; Luc Furic; Norihiko Furuya; Carmela Fusco; Michaela U Gack; Lidia Gaffke; Sehamuddin Galadari; Alessia Galasso; Maria F Galindo; Sachith Gallolu Kankanamalage; Lorenzo Galluzzi; Vincent Galy; Noor Gammoh; Boyi Gan; Ian G Ganley; Feng Gao; Hui Gao; Minghui Gao; Ping Gao; Shou-Jiang Gao; Wentao Gao; Xiaobo Gao; Ana Garcera; Maria Noé Garcia; Verónica E Garcia; Francisco García-Del Portillo; Vega Garcia-Escudero; Aracely Garcia-Garcia; Marina Garcia-Macia; Diana García-Moreno; Carmen Garcia-Ruiz; Patricia García-Sanz; Abhishek D Garg; Ricardo Gargini; Tina Garofalo; Robert F Garry; Nils C Gassen; Damian Gatica; Liang Ge; Wanzhong Ge; Ruth Geiss-Friedlander; Cecilia Gelfi; Pascal Genschik; Ian E Gentle; Valeria Gerbino; Christoph Gerhardt; Kyla Germain; Marc Germain; David A Gewirtz; Elham Ghasemipour Afshar; Saeid Ghavami; Alessandra Ghigo; Manosij Ghosh; Georgios Giamas; Claudia Giampietri; Alexandra Giatromanolaki; Gary E Gibson; Spencer B Gibson; Vanessa Ginet; Edward Giniger; Carlotta Giorgi; Henrique Girao; Stephen E Girardin; Mridhula Giridharan; Sandy Giuliano; Cecilia Giulivi; Sylvie Giuriato; Julien Giustiniani; Alexander Gluschko; Veit Goder; Alexander Goginashvili; Jakub Golab; David C Goldstone; Anna Golebiewska; Luciana R Gomes; Rodrigo Gomez; Rubén Gómez-Sánchez; Maria Catalina Gomez-Puerto; Raquel Gomez-Sintes; Qingqiu Gong; Felix M Goni; Javier González-Gallego; Tomas Gonzalez-Hernandez; Rosa A Gonzalez-Polo; Jose A Gonzalez-Reyes; Patricia González-Rodríguez; Ing Swie Goping; Marina S Gorbatyuk; Nikolai V Gorbunov; Kıvanç Görgülü; Roxana M Gorojod; Sharon M Gorski; Sandro Goruppi; Cecilia Gotor; Roberta A Gottlieb; Illana Gozes; Devrim Gozuacik; Martin Graef; Markus H Gräler; Veronica Granatiero; Daniel Grasso; Joshua P Gray; Douglas R Green; Alexander Greenhough; Stephen L Gregory; Edward F Griffin; Mark W Grinstaff; Frederic Gros; Charles Grose; Angelina S Gross; Florian Gruber; Paolo Grumati; Tilman Grune; Xueyan Gu; Jun-Lin Guan; Carlos M Guardia; Kishore Guda; Flora Guerra; Consuelo Guerri; Prasun Guha; Carlos Guillén; Shashi Gujar; Anna Gukovskaya; Ilya Gukovsky; Jan Gunst; Andreas Günther; Anyonya R Guntur; Chuanyong Guo; Chun Guo; Hongqing Guo; Lian-Wang Guo; Ming Guo; Pawan Gupta; Shashi Kumar Gupta; Swapnil Gupta; Veer Bala Gupta; Vivek Gupta; Asa B Gustafsson; David D Gutterman; Ranjitha H B; Annakaisa Haapasalo; James E Haber; Aleksandra Hać; Shinji Hadano; Anders J Hafrén; Mansour Haidar; Belinda S Hall; Gunnel Halldén; Anne Hamacher-Brady; Andrea Hamann; Maho Hamasaki; Weidong Han; Malene Hansen; Phyllis I Hanson; Zijian Hao; Masaru Harada; Ljubica Harhaji-Trajkovic; Nirmala Hariharan; Nigil Haroon; James Harris; Takafumi Hasegawa; Noor Hasima Nagoor; Jeffrey A Haspel; Volker Haucke; Wayne D Hawkins; Bruce A Hay; Cole M Haynes; Soren B Hayrabedyan; Thomas S Hays; Congcong He; Qin He; Rong-Rong He; You-Wen He; Yu-Ying He; Yasser Heakal; Alexander M Heberle; J Fielding Hejtmancik; Gudmundur Vignir Helgason; Vanessa Henkel; Marc Herb; Alexander Hergovich; Anna Herman-Antosiewicz; Agustín Hernández; Carlos Hernandez; Sergio Hernandez-Diaz; Virginia Hernandez-Gea; Amaury Herpin; Judit Herreros; Javier H Hervás; Daniel Hesselson; Claudio Hetz; Volker T Heussler; Yujiro Higuchi; Sabine Hilfiker; Joseph A Hill; William S Hlavacek; Emmanuel A Ho; Idy H T Ho; Philip Wing-Lok Ho; Shu-Leong Ho; Wan Yun Ho; G Aaron Hobbs; Mark Hochstrasser; Peter H M Hoet; Daniel Hofius; Paul Hofman; Annika Höhn; Carina I Holmberg; Jose R Hombrebueno; Chang-Won Hong Yi-Ren Hong; Lora V Hooper; Thorsten Hoppe; Rastislav Horos; Yujin Hoshida; I-Lun Hsin; Hsin-Yun Hsu; Bing Hu; Dong Hu; Li-Fang Hu; Ming Chang Hu; Ronggui Hu; Wei Hu; Yu-Chen Hu; Zhuo-Wei Hu; Fang Hua; Jinlian Hua; Yingqi Hua; Chongmin Huan; Canhua Huang; Chuanshu Huang; Chuanxin Huang; Chunling Huang; Haishan Huang; Kun Huang; Michael L H Huang; Rui Huang; Shan Huang; Tianzhi Huang; Xing Huang; Yuxiang Jack Huang; Tobias B Huber; Virginie Hubert; Christian A Hubner; Stephanie M Hughes; William E Hughes; Magali Humbert; Gerhard Hummer; James H Hurley; Sabah Hussain; Salik Hussain; Patrick J Hussey; Martina Hutabarat; Hui-Yun Hwang; Seungmin Hwang; Antonio Ieni; Fumiyo Ikeda; Yusuke Imagawa; Yuzuru Imai; Carol Imbriano; Masaya Imoto; Denise M Inman; Ken Inoki; Juan Iovanna; Renato V Iozzo; Giuseppe Ippolito; Javier E Irazoqui; Pablo Iribarren; Mohd Ishaq; Makoto Ishikawa; Nestor Ishimwe; Ciro Isidoro; Nahed Ismail; Shohreh Issazadeh-Navikas; Eisuke Itakura; Daisuke Ito; Davor Ivankovic; Saška Ivanova; Anand Krishnan V Iyer; José M Izquierdo; Masanori Izumi; Marja Jäättelä; Majid Sakhi Jabir; William T Jackson; Nadia Jacobo-Herrera; Anne-Claire Jacomin; Elise Jacquin; Pooja Jadiya; Hartmut Jaeschke; Chinnaswamy Jagannath; Arjen J Jakobi; Johan Jakobsson; Bassam Janji; Pidder Jansen-Dürr; Patric J Jansson; Jonathan Jantsch; Sławomir Januszewski; Alagie Jassey; Steve Jean; Hélène Jeltsch-David; Pavla Jendelova; Andreas Jenny; Thomas E Jensen; Niels Jessen; Jenna L Jewell; Jing Ji; Lijun Jia; Rui Jia; Liwen Jiang; Qing Jiang; Richeng Jiang; Teng Jiang; Xuejun Jiang; Yu Jiang; Maria Jimenez-Sanchez; Eun-Jung Jin; Fengyan Jin; Hongchuan Jin; Li Jin; Luqi Jin; Meiyan Jin; Si Jin; Eun-Kyeong Jo; Carine Joffre; Terje Johansen; Gail V W Johnson; Simon A Johnston; Eija Jokitalo; Mohit Kumar Jolly; Leo A B Joosten; Joaquin Jordan; Bertrand Joseph; Dianwen Ju; Jeong-Sun Ju; Jingfang Ju; Esmeralda Juárez; Delphine Judith; Gábor Juhász; Youngsoo Jun; Chang Hwa Jung; Sung-Chul Jung; Yong Keun Jung; Heinz Jungbluth; Johannes Jungverdorben; Steffen Just; Kai Kaarniranta; Allen Kaasik; Tomohiro Kabuta; Daniel Kaganovich; Alon Kahana; Renate Kain; Shinjo Kajimura; Maria Kalamvoki; Manjula Kalia; Danuta S Kalinowski; Nina Kaludercic; Ioanna Kalvari; Joanna Kaminska; Vitaliy O Kaminskyy; Hiromitsu Kanamori; Keizo Kanasaki; Chanhee Kang; Rui Kang; Sang Sun Kang; Senthilvelrajan Kaniyappan; Tomotake Kanki; Thirumala-Devi Kanneganti; Anumantha G Kanthasamy; Arthi Kanthasamy; Marc Kantorow; Orsolya Kapuy; Michalis V Karamouzis; Md Razaul Karim; Parimal Karmakar; Rajesh G Katare; Masaru Kato; Stefan H E Kaufmann; Anu Kauppinen; Gur P Kaushal; Susmita Kaushik; Kiyoshi Kawasaki; Kemal Kazan; Po-Yuan Ke; Damien J Keating; Ursula Keber; John H Kehrl; Kate E Keller; Christian W Keller; Jongsook Kim Kemper; Candia M Kenific; Oliver Kepp; Stephanie Kermorgant; Andreas Kern; Robin Ketteler; Tom G Keulers; Boris Khalfin; Hany Khalil; Bilon Khambu; Shahid Y Khan; Vinoth Kumar Megraj Khandelwal; Rekha Khandia; Widuri Kho; Noopur V Khobrekar; Sataree Khuansuwan; Mukhran Khundadze; Samuel A Killackey; Dasol Kim; Deok Ryong Kim; Do-Hyung Kim; Dong-Eun Kim; Eun Young Kim; Eun-Kyoung Kim; Hak-Rim Kim; Hee-Sik Kim; Jeong Hun Kim; Jin Kyung Kim; Jin-Hoi Kim; Joungmok Kim; Ju Hwan Kim; Keun Il Kim; Peter K Kim; Seong-Jun Kim; Scot R Kimball; Adi Kimchi; Alec C Kimmelman; Tomonori Kimura; Matthew A King; Kerri J Kinghorn; Conan G Kinsey; Vladimir Kirkin; Lorrie A Kirshenbaum; Sergey L Kiselev; Shuji Kishi; Katsuhiko Kitamoto; Yasushi Kitaoka; Kaio Kitazato; Richard N Kitsis; Josef T Kittler; Ole Kjaerulff; Peter S Klein; Thomas Klopstock; Jochen Klucken; Helene Knævelsrud; Roland L Knorr; Ben C B Ko; Fred Ko; Jiunn-Liang Ko; Hotaka Kobayashi; Satoru Kobayashi; Ina Koch; Jan C Koch; Ulrich Koenig; Donat Kögel; Young Ho Koh; Masato Koike; Sepp D Kohlwein; Nur M Kocaturk; Masaaki Komatsu; Jeannette König; Toru Kono; Benjamin T Kopp; Tamas Korcsmaros; Gözde Korkmaz; Viktor I Korolchuk; Mónica Suárez Korsnes; Ali Koskela; Janaiah Kota; Yaichiro Kotake; Monica L Kotler; Yanjun Kou; Michael I Koukourakis; Evangelos Koustas; Attila L Kovacs; Tibor Kovács; Daisuke Koya; Tomohiro Kozako; Claudine Kraft; Dimitri Krainc; Helmut Krämer; Anna D Krasnodembskaya; Carole Kretz-Remy; Guido Kroemer; Nicholas T Ktistakis; Kazuyuki Kuchitsu; Sabine Kuenen; Lars Kuerschner; Thomas Kukar; Ajay Kumar; Ashok Kumar; Deepak Kumar; Dhiraj Kumar; Sharad Kumar; Shinji Kume; Caroline Kumsta; Chanakya N Kundu; Mondira Kundu; Ajaikumar B Kunnumakkara; Lukasz Kurgan; Tatiana G Kutateladze; Ozlem Kutlu; SeongAe Kwak; Ho Jeong Kwon; Taeg Kyu Kwon; Yong Tae Kwon; Irene Kyrmizi; Albert La Spada; Patrick Labonté; Sylvain Ladoire; Ilaria Laface; Frank Lafont; Diane C Lagace; Vikramjit Lahiri; Zhibing Lai; Angela S Laird; Aparna Lakkaraju; Trond Lamark; Sheng-Hui Lan; Ane Landajuela; Darius J R Lane; Jon D Lane; Charles H Lang; Carsten Lange; Ülo Langel; Rupert Langer; Pierre Lapaquette; Jocelyn Laporte; Nicholas F LaRusso; Isabel Lastres-Becker; Wilson Chun Yu Lau; Gordon W Laurie; Sergio Lavandero; Betty Yuen Kwan Law; Helen Ka-Wai Law; Rob Layfield; Weidong Le; Herve Le Stunff; Alexandre Y Leary; Jean-Jacques Lebrun; Lionel Y W Leck; Jean-Philippe Leduc-Gaudet; Changwook Lee; Chung-Pei Lee; Da-Hye Lee; Edward B Lee; Erinna F Lee; Gyun Min Lee; He-Jin Lee; Heung Kyu Lee; Jae Man Lee; Jason S Lee; Jin-A Lee; Joo-Yong Lee; Jun Hee Lee; Michael Lee; Min Goo Lee; Min Jae Lee; Myung-Shik Lee; Sang Yoon Lee; Seung-Jae Lee; Stella Y Lee; Sung Bae Lee; Won Hee Lee; Ying-Ray Lee; Yong-Ho Lee; Youngil Lee; Christophe Lefebvre; Renaud Legouis; Yu L Lei; Yuchen Lei; Sergey Leikin; Gerd Leitinger; Leticia Lemus; Shuilong Leng; Olivia Lenoir; Guido Lenz; Heinz Josef Lenz; Paola Lenzi; Yolanda León; Andréia M Leopoldino; Christoph Leschczyk; Stina Leskelä; Elisabeth Letellier; Chi-Ting Leung; Po Sing Leung; Jeremy S Leventhal; Beth Levine; Patrick A Lewis; Klaus Ley; Bin Li; Da-Qiang Li; Jianming Li; Jing Li; Jiong Li; Ke Li; Liwu Li; Mei Li; Min Li; Min Li; Ming Li; Mingchuan Li; Pin-Lan Li; Ming-Qing Li; Qing Li; Sheng Li; Tiangang Li; Wei Li; Wenming Li; Xue Li; Yi-Ping Li; Yuan Li; Zhiqiang Li; Zhiyong Li; Zhiyuan Li; Jiqin Lian; Chengyu Liang; Qiangrong Liang; Weicheng Liang; Yongheng Liang; YongTian Liang; Guanghong Liao; Lujian Liao; Mingzhi Liao; Yung-Feng Liao; Mariangela Librizzi; Pearl P Y Lie; Mary A Lilly; Hyunjung J Lim; Thania R R Lima; Federica Limana; Chao Lin; Chih-Wen Lin; Dar-Shong Lin; Fu-Cheng Lin; Jiandie D Lin; Kurt M Lin; Kwang-Huei Lin; Liang-Tzung Lin; Pei-Hui Lin; Qiong Lin; Shaofeng Lin; Su-Ju Lin; Wenyu Lin; Xueying Lin; Yao-Xin Lin; Yee-Shin Lin; Rafael Linden; Paula Lindner; Shuo-Chien Ling; Paul Lingor; Amelia K Linnemann; Yih-Cherng Liou; Marta M Lipinski; Saška Lipovšek; Vitor A Lira; Natalia Lisiak; Paloma B Liton; Chao Liu; Ching-Hsuan Liu; Chun-Feng Liu; Cui Hua Liu; Fang Liu; Hao Liu; Hsiao-Sheng Liu; Hua-Feng Liu; Huifang Liu; Jia Liu; Jing Liu; Julia Liu; Leyuan Liu; Longhua Liu; Meilian Liu; Qin Liu; Wei Liu; Wende Liu; Xiao-Hong Liu; Xiaodong Liu; Xingguo Liu; Xu Liu; Xuedong Liu; Yanfen Liu; Yang Liu; Yang Liu; Yueyang Liu; Yule Liu; J Andrew Livingston; Gerard Lizard; Jose M Lizcano; Senka Ljubojevic-Holzer; Matilde E LLeonart; David Llobet-Navàs; Alicia Llorente; Chih Hung Lo; Damián Lobato-Márquez; Qi Long; Yun Chau Long; Ben Loos; Julia A Loos; Manuela G López; Guillermo López-Doménech; José Antonio López-Guerrero; Ana T López-Jiménez; Óscar López-Pérez; Israel López-Valero; Magdalena J Lorenowicz; Mar Lorente; Peter Lorincz; Laura Lossi; Sophie Lotersztajn; Penny E Lovat; Jonathan F Lovell; Alenka Lovy; Péter Lőw; Guang Lu; Haocheng Lu; Jia-Hong Lu; Jin-Jian Lu; Mengji Lu; Shuyan Lu; Alessandro Luciani; John M Lucocq; Paula Ludovico; Micah A Luftig; Morten Luhr; Diego Luis-Ravelo; Julian J Lum; Liany Luna-Dulcey; Anders H Lund; Viktor K Lund; Jan D Lünemann; Patrick Lüningschrör; Honglin Luo; Rongcan Luo; Shouqing Luo; Zhi Luo; Claudio Luparello; Bernhard Lüscher; Luan Luu; Alex Lyakhovich; Konstantin G Lyamzaev; Alf Håkon Lystad; Lyubomyr Lytvynchuk; Alvin C Ma; Changle Ma; Mengxiao Ma; Ning-Fang Ma; Quan-Hong Ma; Xinliang Ma; Yueyun Ma; Zhenyi Ma; Ormond A MacDougald; Fernando Macian; Gustavo C MacIntosh; Jeffrey P MacKeigan; Kay F Macleod; Sandra Maday; Frank Madeo; Muniswamy Madesh; Tobias Madl; Julio Madrigal-Matute; Akiko Maeda; Yasuhiro Maejima; Marta Magarinos; Poornima Mahavadi; Emiliano Maiani; Kenneth Maiese; Panchanan Maiti; Maria Chiara Maiuri; Barbara Majello; Michael B Major; Elena Makareeva; Fayaz Malik; Karthik Mallilankaraman; Walter Malorni; Alina Maloyan; Najiba Mammadova; Gene Chi Wai Man; Federico Manai; Joseph D Mancias; Eva-Maria Mandelkow; Michael A Mandell; Angelo A Manfredi; Masoud H Manjili; Ravi Manjithaya; Patricio Manque; Bella B Manshian; Raquel Manzano; Claudia Manzoni; Kai Mao; Cinzia Marchese; Sandrine Marchetti; Anna Maria Marconi; Fabrizio Marcucci; Stefania Mardente; Olga A Mareninova; Marta Margeta; Muriel Mari; Sara Marinelli; Oliviero Marinelli; Guillermo Mariño; Sofia Mariotto; Richard S Marshall; Mark R Marten; Sascha Martens; Alexandre P J Martin; Katie R Martin; Sara Martin; Shaun Martin; Adrián Martín-Segura; Miguel A Martín-Acebes; Inmaculada Martin-Burriel; Marcos Martin-Rincon; Paloma Martin-Sanz; José A Martina; Wim Martinet; Aitor Martinez; Ana Martinez; Jennifer Martinez; Moises Martinez Velazquez; Nuria Martinez-Lopez; Marta Martinez-Vicente; Daniel O Martins; Joilson O Martins; Waleska K Martins; Tania Martins-Marques; Emanuele Marzetti; Shashank Masaldan; Celine Masclaux-Daubresse; Douglas G Mashek; Valentina Massa; Lourdes Massieu; Glenn R Masson; Laura Masuelli; Anatoliy I Masyuk; Tetyana V Masyuk; Paola Matarrese; Ander Matheu; Satoaki Matoba; Sachiko Matsuzaki; Pamela Mattar; Alessandro Matte; Domenico Mattoscio; José L Mauriz; Mario Mauthe; Caroline Mauvezin; Emanual Maverakis; Paola Maycotte; Johanna Mayer; Gianluigi Mazzoccoli; Cristina Mazzoni; Joseph R Mazzulli; Nami McCarty; Christine McDonald; Mitchell R McGill; Sharon L McKenna; BethAnn McLaughlin; Fionn McLoughlin; Mark A McNiven; Thomas G McWilliams; Fatima Mechta-Grigoriou; Tania Catarina Medeiros; Diego L Medina; Lynn A Megeney; Klara Megyeri; Maryam Mehrpour; Jawahar L Mehta; Alfred J Meijer; Annemarie H Meijer; Jakob Mejlvang; Alicia Meléndez; Annette Melk; Gonen Memisoglu; Alexandrina F Mendes; Delong Meng; Fei Meng; Tian Meng; Rubem Menna-Barreto; Manoj B Menon; Carol Mercer; Anne E Mercier; Jean-Louis Mergny; Adalberto Merighi; Seth D Merkley; Giuseppe Merla; Volker Meske; Ana Cecilia Mestre; Shree Padma Metur; Christian Meyer; Hemmo Meyer; Wenyi Mi; Jeanne Mialet-Perez; Junying Miao; Lucia Micale; Yasuo Miki; Enrico Milan; Małgorzata Milczarek; Dana L Miller; Samuel I Miller; Silke Miller; Steven W Millward; Ira Milosevic; Elena A Minina; Hamed Mirzaei; Hamid Reza Mirzaei; Mehdi Mirzaei; Amit Mishra; Nandita Mishra; Paras Kumar Mishra; Maja Misirkic Marjanovic; Roberta Misasi; Amit Misra; Gabriella Misso; Claire Mitchell; Geraldine Mitou; Tetsuji Miura; Shigeki Miyamoto; Makoto Miyazaki; Mitsunori Miyazaki; Taiga Miyazaki; Keisuke Miyazawa; Noboru Mizushima; Trine H Mogensen; Baharia Mograbi; Reza Mohammadinejad; Yasir Mohamud; Abhishek Mohanty; Sipra Mohapatra; Torsten Möhlmann; Asif Mohmmed; Anna Moles; Kelle H Moley; Maurizio Molinari; Vincenzo Mollace; Andreas Buch Møller; Bertrand Mollereau; Faustino Mollinedo; Costanza Montagna; Mervyn J Monteiro; Andrea Montella; L Ruth Montes; Barbara Montico; Vinod K Mony; Giacomo Monzio Compagnoni; Michael N Moore; Mohammad A Moosavi; Ana L Mora; Marina Mora; David Morales-Alamo; Rosario Moratalla; Paula I Moreira; Elena Morelli; Sandra Moreno; Daniel Moreno-Blas; Viviana Moresi; Benjamin Morga; Alwena H Morgan; Fabrice Morin; Hideaki Morishita; Orson L Moritz; Mariko Moriyama; Yuji Moriyasu; Manuela Morleo; Eugenia Morselli; Jose F Moruno-Manchon; Jorge Moscat; Serge Mostowy; Elisa Motori; Andrea Felinto Moura; Naima Moustaid-Moussa; Maria Mrakovcic; Gabriel Muciño-Hernández; Anupam Mukherjee; Subhadip Mukhopadhyay; Jean M Mulcahy Levy; Victoriano Mulero; 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Siegfried Reipert; Rokeya Sultana Rekha; Hongmei Ren; Jun Ren; Weichao Ren; Tristan Renault; Giorgia Renga; Karen Reue; Kim Rewitz; Bruna Ribeiro de Andrade Ramos; S Amer Riazuddin; Teresa M Ribeiro-Rodrigues; Jean-Ehrland Ricci; Romeo Ricci; Victoria Riccio; Des R Richardson; Yasuko Rikihisa; Makarand V Risbud; Ruth M Risueño; Konstantinos Ritis; Salvatore Rizza; Rosario Rizzuto; Helen C Roberts; Luke D Roberts; Katherine J Robinson; Maria Carmela Roccheri; Stephane Rocchi; George G Rodney; Tiago Rodrigues; Vagner Ramon Rodrigues Silva; Amaia Rodriguez; Ruth Rodriguez-Barrueco; Nieves Rodriguez-Henche; Humberto Rodriguez-Rocha; Jeroen Roelofs; Robert S Rogers; Vladimir V Rogov; Ana I Rojo; Krzysztof Rolka; Vanina Romanello; Luigina Romani; Alessandra Romano; Patricia S Romano; David Romeo-Guitart; Luis C Romero; Montserrat Romero; Joseph C Roney; Christopher Rongo; Sante Roperto; Mathias T Rosenfeldt; Philip Rosenstiel; Anne G Rosenwald; Kevin A Roth; Lynn Roth; Steven Roth; Kasper M A Rouschop; 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Laura Segatori; Nava Segev; Per O Seglen; Iban Seiliez; Ekihiro Seki; Scott B Selleck; Frank W Sellke; Joshua T Selsby; Michael Sendtner; Serif Senturk; Elena Seranova; Consolato Sergi; Ruth Serra-Moreno; Hiromi Sesaki; Carmine Settembre; Subba Rao Gangi Setty; Gianluca Sgarbi; Ou Sha; John J Shacka; Javeed A Shah; Dantong Shang; Changshun Shao; Feng Shao; Soroush Sharbati; Lisa M Sharkey; Dipali Sharma; Gaurav Sharma; Kulbhushan Sharma; Pawan Sharma; Surendra Sharma; Han-Ming Shen; Hongtao Shen; Jiangang Shen; Ming Shen; Weili Shen; Zheni Shen; Rui Sheng; Zhi Sheng; Zu-Hang Sheng; Jianjian Shi; Xiaobing Shi; Ying-Hong Shi; Kahori Shiba-Fukushima; Jeng-Jer Shieh; Yohta Shimada; Shigeomi Shimizu; Makoto Shimozawa; Takahiro Shintani; Christopher J Shoemaker; Shahla Shojaei; Ikuo Shoji; Bhupendra V Shravage; Viji Shridhar; Chih-Wen Shu; Hong-Bing Shu; Ke Shui; Arvind K Shukla; Timothy E Shutt; Valentina Sica; Aleem Siddiqui; Amanda Sierra; Virginia Sierra-Torre; Santiago Signorelli; Payel Sil; 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Motomasa Tanaka; Daolin Tang; Jingfeng Tang; Tie-Shan Tang; Isei Tanida; Zhipeng Tao; Mohammed Taouis; Lars Tatenhorst; Nektarios Tavernarakis; Allen Taylor; Gregory A Taylor; Joan M Taylor; Elena Tchetina; Andrew R Tee; Irmgard Tegeder; David Teis; Natercia Teixeira; Fatima Teixeira-Clerc; Kumsal A Tekirdag; Tewin Tencomnao; Sandra Tenreiro; Alexei V Tepikin; Pilar S Testillano; Gianluca Tettamanti; Pierre-Louis Tharaux; Kathrin Thedieck; Arvind A Thekkinghat; Stefano Thellung; Josephine W Thinwa; V P Thirumalaikumar; Sufi Mary Thomas; Paul G Thomes; Andrew Thorburn; Lipi Thukral; Thomas Thum; Michael Thumm; Ling Tian; Ales Tichy; Andreas Till; Vincent Timmerman; Vladimir I Titorenko; Sokol V Todi; Krassimira Todorova; Janne M Toivonen; Luana Tomaipitinca; Dhanendra Tomar; Cristina Tomas-Zapico; Sergej Tomić; Benjamin Chun-Kit Tong; Chao Tong; Xin Tong; Sharon A Tooze; Maria L Torgersen; Satoru Torii; Liliana Torres-López; Alicia Torriglia; Christina G Towers; Roberto Towns; Shinya Toyokuni; 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