Literature DB >> 17496832

Sheddases and intramembrane-cleaving proteases: RIPpers of the membrane. Symposium on regulated intramembrane proteolysis.

Stefan F Lichtenthaler1, Harald Steiner.   

Abstract

Mesh：

Substances：

Year:  2007        PMID： 17496832      PMCID： PMC2002526          DOI： 10.1038/sj.embor.7400978

Source DB:  PubMed          Journal:  EMBO Rep        ISSN： 1469-221X            Impact factor:   8.807


× No keyword cloud information.
  18 in total

Review 1.  Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans.

Authors:  M S Brown; J Ye; R B Rawson; J L Goldstein
Journal:  Cell       Date:  2000-02-18       Impact factor: 41.582

2.  Electron microscopic structure of purified, active gamma-secretase reveals an aqueous intramembrane chamber and two pores.

Authors:  Vlado K Lazarov; Patrick C Fraering; Wenjuan Ye; Michael S Wolfe; Dennis J Selkoe; Huilin Li
Journal:  Proc Natl Acad Sci U S A       Date:  2006-04-24       Impact factor: 11.205

3.  Mechanism of intramembrane proteolysis investigated with purified rhomboid proteases.

Authors:  Marius K Lemberg; Javier Menendez; Angelika Misik; Maite Garcia; Christopher M Koth; Matthew Freeman
Journal:  EMBO J       Date:  2004-12-23       Impact factor: 11.598

4.  SPPL2a and SPPL2b promote intramembrane proteolysis of TNFalpha in activated dendritic cells to trigger IL-12 production.

Authors:  Elena Friedmann; Ehud Hauben; Kerstin Maylandt; Simone Schleeger; Sarah Vreugde; Stefan F Lichtenthaler; Peer-Hendrik Kuhn; Daniela Stauffer; Giorgio Rovelli; Bruno Martoglio
Journal:  Nat Cell Biol       Date:  2006-07-09       Impact factor: 28.824

5.  The GxGD motif of presenilin contributes to catalytic function and substrate identification of gamma-secretase.

Authors:  Aya Yamasaki; Stefan Eimer; Masayasu Okochi; Agata Smialowska; Christoph Kaether; Ralf Baumeister; Christian Haass; Harald Steiner
Journal:  J Neurosci       Date:  2006-04-05       Impact factor: 6.167

6.  Control of peripheral nerve myelination by the beta-secretase BACE1.

Authors:  Michael Willem; Alistair N Garratt; Bozidar Novak; Martin Citron; Steve Kaufmann; Andrea Rittger; Bart DeStrooper; Paul Saftig; Carmen Birchmeier; Christian Haass
Journal:  Science       Date:  2006-09-21       Impact factor: 47.728

7.  A gamma-secretase-like intramembrane cleavage of TNFalpha by the GxGD aspartyl protease SPPL2b.

Authors:  Regina Fluhrer; Gudula Grammer; Lars Israel; Margaret M Condron; Christof Haffner; Elena Friedmann; Claudia Böhland; Axel Imhof; Bruno Martoglio; David B Teplow; Christian Haass
Journal:  Nat Cell Biol       Date:  2006-07-09       Impact factor: 28.824

8.  Contribution of presenilin transmembrane domains 6 and 7 to a water-containing cavity in the gamma-secretase complex.

Authors:  Alexandra Tolia; Lucía Chávez-Gutiérrez; Bart De Strooper
Journal:  J Biol Chem       Date:  2006-07-14       Impact factor: 5.157

9.  Serine proteases from two cell types target different components of a complex that governs regulated intramembrane proteolysis of pro-sigmaK during Bacillus subtilis development.

Authors:  Ruanbao Zhou; Lee Kroos
Journal:  Mol Microbiol       Date:  2005-11       Impact factor: 3.501

10.  Enzymatic analysis of a rhomboid intramembrane protease implicates transmembrane helix 5 as the lateral substrate gate.

Authors:  Rosanna P Baker; Keith Young; Liang Feng; Yigong Shi; Sinisa Urban
Journal:  Proc Natl Acad Sci U S A       Date:  2007-04-26       Impact factor: 11.205
View more
  11 in total

Review 1.  Membrane proteases in the bacterial protein secretion and quality control pathway.

Authors:  Ross E Dalbey; Peng Wang; Jan Maarten van Dijl
Journal:  Microbiol Mol Biol Rev       Date:  2012-06       Impact factor: 11.056

Review 2.  Substrate specificity of gamma-secretase and other intramembrane proteases.

Authors:  A J Beel; C R Sanders
Journal:  Cell Mol Life Sci       Date:  2008-05       Impact factor: 9.261

Review 3.  A TAG on to the neurogenic functions of APP.

Authors:  Quan-Hong Ma; Dominique Bagnard; Zhi-Cheng Xiao; Gavin S Dawe
Journal:  Cell Adh Migr       Date:  2008-01-25       Impact factor: 3.405

Review 4.  Assembly, maturation, and trafficking of the gamma-secretase complex in Alzheimer's disease.

Authors:  Daniel R Dries; Gang Yu
Journal:  Curr Alzheimer Res       Date:  2008-04       Impact factor: 3.498

5.  Systematic proteomic analysis identifies β-site amyloid precursor protein cleaving enzyme 2 and 1 (BACE2 and BACE1) substrates in pancreatic β-cells.

Authors:  Ina Stützer; Nathalie Selevsek; Daria Esterházy; Alexander Schmidt; Ruedi Aebersold; Markus Stoffel
Journal:  J Biol Chem       Date:  2013-02-19       Impact factor: 5.157

Review 6.  Therapeutic Potential of Targeting Regulated Intramembrane Proteolysis Mechanisms of Voltage-Gated Ion Channel Subunits and Cell Adhesion Molecules.

Authors:  Samantha L Hodges; Alexandra A Bouza; Lori L Isom
Journal:  Pharmacol Rev       Date:  2022-10       Impact factor: 18.923

7.  Mechanism of intramembrane cleavage of alcadeins by γ-secretase.

Authors:  Yi Piao; Ayano Kimura; Satomi Urano; Yuhki Saito; Hidenori Taru; Tohru Yamamoto; Saori Hata; Toshiharu Suzuki
Journal:  PLoS One       Date:  2013-04-26       Impact factor: 3.240

8.  Determination of the proteolytic cleavage sites of the amyloid precursor-like protein 2 by the proteases ADAM10, BACE1 and γ-secretase.

Authors:  Sebastian Hogl; Peer-Hendrik Kuhn; Alessio Colombo; Stefan F Lichtenthaler
Journal:  PLoS One       Date:  2011-06-17       Impact factor: 3.240

Review 9.  MBTPS2, a membrane bound protease, underlying several distinct skin and bone disorders.

Authors:  Natarin Caengprasath; Thanakorn Theerapanon; Thantrira Porntaveetus; Vorasuk Shotelersuk
Journal:  J Transl Med       Date:  2021-03-20       Impact factor: 5.531

10.  Application of a Bioinformatics-Based Approach to Identify Novel Putative in vivo BACE1 Substrates.

Authors:  Joseph L Johnson; Emily Chambers; Keerthi Jayasundera
Journal:  Biomed Eng Comput Biol       Date:  2013-02-03
View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.