Biochemical and structural insights into intramembrane metalloprotease mechanisms.
about
The Leaderless Bacteriocin Enterocin K1 Is Highly Potent against Enterococcus faecium: A Study on Structure, Target Spectrum and Receptor.Copper economy in Chlamydomonas: prioritized allocation and reallocation of copper to respiration vs. photosynthesis.Roles of the membrane-reentrant β-hairpin-like loop of RseP protease in selective substrate cleavageNicastrin functions to sterically hinder γ-secretase-substrate interactions driven by substrate transmembrane domainComplex Formed between Intramembrane Metalloprotease SpoIVFB and Its Substrate, Pro-σKFeatures of Pro-σK important for cleavage by SpoIVFB, an intramembrane metalloprotease.An Intronic MBTPS2 Variant Results in a Splicing Defect in Horses with Brindle Coat TextureResidues in conserved loops of intramembrane metalloprotease SpoIVFB interact with residues near the cleavage site in pro-σKRegulated proteolysis in bacterial development.Why cells need intramembrane proteases - a mechanistic perspective.LsbB Bacteriocin Interacts with the Third Transmembrane Domain of the YvjB ReceptorInteraction of intramembrane metalloprotease SpoIVFB with substrate Pro-σK.Both positional and chemical variables control in vitro proteolytic cleavage of a presenilin ortholog.Involvement of a conserved GFG motif region in substrate binding by RseP, an Escherichia coli S2P protease.Regulated intramembrane proteolysis: emergent role in cell signalling pathways.Bacillus subtilis Intramembrane Protease RasP Activity in Escherichia coli and In Vitro.Transmembrane redox control and proteolysis of PdeC, a novel type of c-di-GMP phosphodiesterase.
P2860
Q33628014-00F90599-8665-466C-8E8D-350B381B9896Q35157092-FC6797AD-B1EC-4C89-83BE-65A272DEACF7Q36135739-17394CBF-B47B-4A06-B3E6-36A610C49112Q36563117-1B6868B4-2C7A-40BC-9098-3DEB835E9FE1Q36876249-1EFBAE20-DA2E-434F-B9C7-9099F3437654Q36969506-04181248-62DC-4782-ABE2-82A70B7527CBQ37242077-04C22D02-DD95-4F57-88FE-D2837842F1CAQ37253097-01AA5322-E31B-4DAB-8DA5-67D2E33F66B4Q37728640-34FA87FC-4BDB-459B-A95D-D27816AD8B5CQ38682929-66A61B3C-A19B-4C44-83E0-E19385871655Q41717546-68FC5480-8D93-4097-8022-FB6475371380Q47359023-98294606-4B3D-40BF-B486-D765DC04A378Q47695301-16714855-D5D1-4FB6-B827-A177DDEA12DDQ48167824-5B414396-F49C-4F56-966C-2982D7FD5902Q50100385-726BB49D-6557-46CD-A712-4AABCBCB22BEQ50909454-D69B93D7-F553-4926-9880-AA46A4031476Q52668709-A37BA252-91A8-4220-8765-E93ACD483ACE
P2860
Biochemical and structural insights into intramembrane metalloprotease mechanisms.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on December 2013
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Biochemical and structural insights into intramembrane metalloprotease mechanisms.
@en
Biochemical and structural insights into intramembrane metalloprotease mechanisms.
@nl
type
label
Biochemical and structural insights into intramembrane metalloprotease mechanisms.
@en
Biochemical and structural insights into intramembrane metalloprotease mechanisms.
@nl
prefLabel
Biochemical and structural insights into intramembrane metalloprotease mechanisms.
@en
Biochemical and structural insights into intramembrane metalloprotease mechanisms.
@nl
P2860
P1476
Biochemical and structural insights into intramembrane metalloprotease mechanisms.
@en
P2093
Yoshinori Akiyama
P2860
P304
P356
10.1016/J.BBAMEM.2013.03.032
P407
P577
2013-12-01T00:00:00Z