Enzymatic analysis of a rhomboid intramembrane protease implicates transmembrane helix 5 as the lateral substrate gate. - Wikidata - awgldk - TriplyDB

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

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

http://www.wikidata.org/entity/Q34623352

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Hydrogen bond dynamics in membrane protein function Toward the structure of presenilin/γ-secretase and presenilin homologs Making the cut: central roles of intramembrane proteolysis in pathogenic microorganisms The Role of L1 Loop in the Mechanism of Rhomboid Intramembrane Protease GlpG Structure of a site-2 protease family intramembrane metalloprotease The structural basis for catalysis and substrate specificity of a rhomboid protease Structure of Rhomboid Protease in a Lipid Environment Large Lateral Movement of Transmembrane Helix S5 Is Not Required for Substrate Access to the Active Site of Rhomboid Intramembrane Protease Conformational Change in Rhomboid Protease GlpG Induced by Inhibitor Binding to Its S′ Subsites Mechanism of farnesylated CAAX protein processing by the intramembrane protease Rce1 Proteolysis inside the Membrane Is a Rate-Governed Reaction Not Driven by Substrate Affinity Unconventional serine proteases: variations on the catalytic Ser/His/Asp triad configuration Allosteric regulation of rhomboid intramembrane proteolysis A Trichomonas vaginalis Rhomboid Protease and Its Substrate Modulate Parasite Attachment and Cytolysis of Host Cells Membrane Protein Structure, Function, and Dynamics: a Perspective from Experiments and Theory.Structure and mechanism of rhomboid protease An internal water-retention site in the rhomboid intramembrane protease GlpG ensures catalytic efficiency.Functional analysis of the transmembrane domains of presenilin 1: participation of transmembrane domains 2 and 6 in the formation of initial substrate-binding site of gamma-secretase.Sequence-specific intramembrane proteolysis: identification of a recognition motif in rhomboid substrates Substrate binding and specificity of rhomboid intramembrane protease revealed by substrate-peptide complex structures An Entamoeba histolytica rhomboid protease with atypical specificity cleaves a surface lectin involved in phagocytosis and immune evasion.Taking the plunge: integrating structural, enzymatic and computational insights into a unified model for membrane-immersed rhomboid proteolysis Derlin-1 is a rhomboid pseudoprotease required for the dislocation of mutant α-1 antitrypsin from the endoplasmic reticulum.Catalytic mechanism of rhomboid protease GlpG probed by 3,4-dichloroisocoumarin and diisopropyl fluorophosphonate.From rhomboid function to structure and back again Intramembrane proteolysis of Toxoplasma apical membrane antigen 1 facilitates host-cell invasion but is dispensable for replication.Membrane proteases in the bacterial protein secretion and quality control pathway.Holophytochrome-Interacting Proteins in Physcomitrella: Putative Actors in Phytochrome Cytoplasmic Signaling.Membrane immersion allows rhomboid proteases to achieve specificity by reading transmembrane segment dynamics.Topological constraints and modular structure in the folding and functional motions of GlpG, an intramembrane protease.Substrate specificity of gamma-secretase and other intramembrane proteases.Soluble oligomers of the intramembrane serine protease YqgP are catalytically active in the absence of detergents.Structural and Functional Determinants of gamma-Secretase, an Intramembrane Protease Implicated in Alzheimer's Disease.Core principles of intramembrane proteolysis: comparison of rhomboid and site-2 family proteases Intramembrane proteolysis Rhomboid protease dynamics and lipid interactions Presenilins: members of the gamma-secretase quartets, but part-time soloists too.Structure and mechanism of intramembrane protease.Intramembrane-cleaving proteases.The PARL family of mitochondrial rhomboid proteases.

P2860

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P2860

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

http://www.wikidata.org/entity/Q34623352

description

2007 nî lūn-bûn

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2007 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի ապրիլին հրատարակված գիտական հոդված

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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name

Enzymatic analysis of a rhombo ...... as the lateral substrate gate.

@ast

Enzymatic analysis of a rhombo ...... as the lateral substrate gate.

@en

Enzymatic analysis of a rhombo ...... as the lateral substrate gate.

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type

label

Enzymatic analysis of a rhombo ...... as the lateral substrate gate.

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Enzymatic analysis of a rhombo ...... as the lateral substrate gate.

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Enzymatic analysis of a rhombo ...... as the lateral substrate gate.

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prefLabel

Enzymatic analysis of a rhombo ...... as the lateral substrate gate.

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Enzymatic analysis of a rhombo ...... as the lateral substrate gate.

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Enzymatic analysis of a rhombo ...... as the lateral substrate gate.

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PNAS.0700814104

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Enzymatic analysis of a rhombo ...... as the lateral substrate gate.

@en

P2093

Keith Young

http://www.w3.org/2001/XMLSchema#string

Liang Feng

http://www.w3.org/2001/XMLSchema#string

Rosanna P Baker

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Sinisa Urban

http://www.w3.org/2001/XMLSchema#string

Yigong Shi

http://www.w3.org/2001/XMLSchema#string

P2860

Presenilin 1 is linked with gamma-secretase activity in the detergent solubilized state

Purification and characterization of the human gamma-secretase complex

TMP21 is a presenilin complex component that modulates gamma-secretase but not epsilon-secretase activity

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

The rhomboids: a nearly ubiquitous family of intramembrane serine proteases that probably evolved by multiple ancient horizontal gene transfers

Structural basis for intramembrane proteolysis by rhomboid serine proteases

The crystal structure of the rhomboid peptidase from Haemophilus influenzae provides insight into intramembrane proteolysis.

X-ray structure of a protein-conducting channel

Open-cap conformation of intramembrane protease GlpG

Complementation cloning of S2P, a gene encoding a putative metalloprotease required for intramembrane cleavage of SREBPs

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104

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6366391

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17463085

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P921

transmembrane protein

P932

1895938

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