Literature DB >> 17412596

Functional amyloid--from bacteria to humans.

Douglas M Fowler1, Atanas V Koulov, William E Balch, Jeffery W Kelly.   

Abstract

Amyloid--a fibrillar, cross beta-sheet quaternary structure--was first discovered in the context of human disease and tissue damage, and was thought to always be detrimental to the host. Recent studies have identified amyloid fibers in bacteria, fungi, insects, invertebrates and humans that are functional. For example, human Pmel17 has important roles in the biosynthesis of the pigment melanin, and the factor XII protein of the hemostatic system is activated by amyloid. Functional amyloidogenesis in these systems requires tight regulation to avoid toxicity. A greater understanding of the diverse physiological applications of this fold has the potential to provide a fresh perspective for the treatment of amyloid diseases.

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Year:  2007        PMID: 17412596     DOI: 10.1016/j.tibs.2007.03.003

Source DB:  PubMed          Journal:  Trends Biochem Sci        ISSN: 0968-0004            Impact factor:   13.807


  358 in total

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Journal:  Alzheimers Dement       Date:  2011-11-02       Impact factor: 21.566

2.  Self-assembly of functional, amphipathic amyloid monolayers by the fungal hydrophobin EAS.

Authors:  Ingrid Macindoe; Ann H Kwan; Qin Ren; Vanessa K Morris; Wenrong Yang; Joel P Mackay; Margaret Sunde
Journal:  Proc Natl Acad Sci U S A       Date:  2012-01-23       Impact factor: 11.205

3.  An amyloid organelle, solid-state NMR evidence for cross-β assembly of gas vesicles.

Authors:  Marvin J Bayro; Eugenio Daviso; Marina Belenky; Robert G Griffin; Judith Herzfeld
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4.  Perfecting precision of predicting prion propensity.

Authors:  Daniel C Masison
Journal:  Proc Natl Acad Sci U S A       Date:  2012-04-12       Impact factor: 11.205

5.  Microcin amyloid fibrils A are reservoir of toxic oligomeric species.

Authors:  Mohammad Shahnawaz; Claudio Soto
Journal:  J Biol Chem       Date:  2012-02-15       Impact factor: 5.157

6.  Inflammation protein SAA2.2 spontaneously forms marginally stable amyloid fibrils at physiological temperature.

Authors:  Zhuqiu Ye; Diane Bayron Poueymiroy; J Javier Aguilera; Saipraveen Srinivasan; Yun Wang; Louise C Serpell; Wilfredo Colón
Journal:  Biochemistry       Date:  2011-10-05       Impact factor: 3.162

7.  Chain collapse of an amyloidogenic intrinsically disordered protein.

Authors:  Neha Jain; Mily Bhattacharya; Samrat Mukhopadhyay
Journal:  Biophys J       Date:  2011-10-05       Impact factor: 4.033

Review 8.  Getting a grip on prions: oligomers, amyloids, and pathological membrane interactions.

Authors:  Byron Caughey; Gerald S Baron; Bruce Chesebro; Martin Jeffrey
Journal:  Annu Rev Biochem       Date:  2009       Impact factor: 23.643

9.  Gallibacterium elongation factor-Tu possesses amyloid-like protein characteristics, participates in cell adhesion, and is present in biofilms.

Authors:  Jaqueline López-Ochoa; J Fernando Montes-García; Candelario Vázquez; Patricia Sánchez-Alonso; Victor M Pérez-Márquez; Patrick J Blackall; Sergio Vaca; Erasmo Negrete-Abascal
Journal:  J Microbiol       Date:  2017-09-02       Impact factor: 3.422

10.  Exploring the aggregation propensity of γS-crystallin protein variants using two-dimensional spectroscopic tools.

Authors:  Jun Jiang; Kory J Golchert; Carolyn N Kingsley; William D Brubaker; Rachel W Martin; Shaul Mukamel
Journal:  J Phys Chem B       Date:  2013-11-12       Impact factor: 2.991

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