Nucleotide-dependent substrate recognition by the AAA+ HslUV protease.
about
Glycine-alanine repeats impair proper substrate unfolding by the proteasomeEvolution of the ssrA degradation tag in Mycoplasma: specificity switch to a different proteaseFundamental Characteristics of AAA+ Protein Family Structure and FunctionPaddling mechanism for the substrate translocation by AAA+ motor revealed by multiscale molecular simulations.A novel plant E3 ligase stabilizes Escherichia coli heat shock factor σ32.Characterization of the Escherichia coli ClpY (HslU) substrate recognition site in the ClpYQ (HslUV) protease using the yeast two-hybrid system.Recognition of misfolded proteins by Lon, a AAA(+) proteaseStepwise activity of ClpY (HslU) mutants in the processive degradation of Escherichia coli ClpYQ (HslUV) protease substrates.Design principles of the proteolytic cascade governing the sigmaE-mediated envelope stress response in Escherichia coli: keys to graded, buffered, and rapid signal transduction.Visualizing the ATPase cycle in a protein disaggregating machine: structural basis for substrate binding by ClpBTransfer-messenger RNA-SmpB protein regulates ribonuclease R turnover by promoting binding of HslUV and Lon proteases.ATP-dependent proteases of bacteria: recognition logic and operating principlesATP-dependent proteases differ substantially in their ability to unfold globular proteinsHslVU ATP-dependent protease utilizes maximally six among twelve threonine active sites during proteolysisProteolysis in the Escherichia coli heat shock response: a player at many levels.Mechanistic insights into bacterial AAA+ proteases and protein-remodelling machines.Rethinking proteasome evolution: two novel bacterial proteasomes.Multiple sequence signals direct recognition and degradation of protein substrates by the AAA+ protease HslUV.Altered specificity of a AAA+ protease.Asymmetric nucleotide transactions of the HslUV protease.A Structurally Dynamic Region of the HslU Intermediate Domain Controls Protein Degradation and ATP Hydrolysis.The I domain of the AAA+ HslUV protease coordinates substrate binding, ATP hydrolysis, and protein degradationNblA, a key protein of phycobilisome degradation, interacts with ClpC, a HSP100 chaperone partner of a cyanobacterial Clp protease.Substrate recognition by AAA+ ATPases: distinct substrate binding modes in ATP-dependent protease Yme1 of the mitochondrial intermembrane spaceExamination of polypeptide substrate specificity for Escherichia coli ClpB.Cleavage mechanism of ATP-dependent Lon protease toward ribosomal S2 protein.Structure of the mitochondrial inner membrane AAA+ protease YME1 gives insight into substrate processing.Covalently linked HslU hexamers support a probabilistic mechanism that links ATP hydrolysis to protein unfolding and translocation.
P2860
Q24543904-147F0672-4E60-4DEB-A321-31AFA992E3C4Q24649663-6AF35AFA-B4C1-47D9-95DE-0C15A864645FQ28066287-F2C74F4F-F57C-4765-A4EA-1B8D27FE95C8Q30491561-C5DA2138-5764-4907-899D-440A07D4A1D1Q33826067-284FE575-6296-4AF6-B0A5-3C26B34B0EADQ34606942-4D9E37BD-1518-46FC-9107-78D8E2508DACQ34809787-FD444DA7-74FB-400E-A894-045AB399B832Q35274427-C513C3E0-84A6-4DCA-99BB-BC85101CA047Q35565304-DA52A0D3-F36E-47AC-8A45-3A56886D5D0BQ35757826-3A43DC0A-6892-4B8E-876E-FEE20E7CAB40Q36286137-BC423ABD-565C-4EF0-9833-BCE159442377Q36639201-2A5A30F1-041B-437B-B58F-11298230F6AAQ37254059-F196106C-7905-4B32-B905-58973C073A1DQ37446205-86010558-D943-4520-87D3-CFB7464E335BQ37847387-498B1A46-730C-44FC-9787-CACDC8274180Q38660358-9BD19373-9E75-43DE-8FE0-6C50FDAB597EQ39739226-9FA3D960-7455-4D58-BD5A-5A6CB0DB73A0Q41898305-DA2BD5CD-C740-4728-BE59-FD5533632AE5Q42255627-490C2C7D-0E87-4265-97D4-59ADD19AFE1BQ42262524-1E80C159-CFC3-46AC-8835-F16C4142E849Q42281706-E04E6A75-90A2-4592-B897-13509CAA7AF1Q42549116-F9D06128-4972-447F-888E-F65ACF1D149FQ42598626-B2D86AD0-824F-4327-A8F3-81A1F1C7FD63Q42738109-98CCF6E2-2435-4F0A-BEAF-056F8563450EQ44631073-6BEE9E4B-E323-4C2E-950E-529645EC4252Q46842184-12C565D3-A841-4533-9EF4-84D68EFB1479Q48373223-91B212D0-1792-48AC-8B16-01483B3D40CDQ50995389-FE8BE8E1-2539-40BA-A700-740003F2BD5A
P2860
Nucleotide-dependent substrate recognition by the AAA+ HslUV protease.
description
2005 nî lūn-bûn
@nan
2005 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Nucleotide-dependent substrate recognition by the AAA+ HslUV protease.
@ast
Nucleotide-dependent substrate recognition by the AAA+ HslUV protease.
@en
Nucleotide-dependent substrate recognition by the AAA+ HslUV protease.
@nl
type
label
Nucleotide-dependent substrate recognition by the AAA+ HslUV protease.
@ast
Nucleotide-dependent substrate recognition by the AAA+ HslUV protease.
@en
Nucleotide-dependent substrate recognition by the AAA+ HslUV protease.
@nl
prefLabel
Nucleotide-dependent substrate recognition by the AAA+ HslUV protease.
@ast
Nucleotide-dependent substrate recognition by the AAA+ HslUV protease.
@en
Nucleotide-dependent substrate recognition by the AAA+ HslUV protease.
@nl
P2860
P356
P1476
Nucleotide-dependent substrate recognition by the AAA+ HslUV protease
@en
P2093
Randall E Burton
Tania A Baker
P2860
P2888
P304
P356
10.1038/NSMB898
P50
P577
2005-02-06T00:00:00Z