Hydrogen exchange reveals a stable and expandable core within the aspartate receptor cytoplasmic domain.
about
Mapping out regions on the surface of the aspartate receptor that are essential for kinase activationFlexibility of the cytoplasmic domain of the phototaxis transducer II from Natronomonas pharaonis.Evidence that the adaptation region of the aspartate receptor is a dynamic four-helix bundle: cysteine and disulfide scanning studies.Hydrogen exchange differences between chemoreceptor signaling complexes localize to functionally important subdomainsDynaFace: Discrimination between Obligatory and Non-obligatory Protein-Protein Interactions Based on the Complex's Dynamics.Crosslinking snapshots of bacterial chemoreceptor squads.Hydrogen exchange mass spectrometry of functional membrane-bound chemotaxis receptor complexesBacterial Chemoreceptor Dynamics: Helical Stability in the Cytoplasmic Domain Varies with Functional Segment and Adaptational Modification.Conserved glycine residues in the cytoplasmic domain of the aspartate receptor play essential roles in kinase coupling and on-off switching.Differential backbone dynamics of companion helices in the extended helical coiled-coil domain of a bacterial chemoreceptor.Quantitative analysis of aspartate receptor signaling complex reveals that the homogeneous two-state model is inadequate: development of a heterogeneous two-state model.Adaptation mechanism of the aspartate receptor: electrostatics of the adaptation subdomain play a key role in modulating kinase activity.
P2860
Q30894653-811752A3-1554-4717-9DA2-6C5CB7BC25D5Q33602520-BCA00581-62AC-4EA6-AFDD-EA152F2F2092Q33988261-0E5229A1-6564-407F-AF46-3DE6F18E015CQ34731661-0041AF0A-D4B5-486D-A881-DF75EC8C5B29Q35822949-EDFDB853-2F5A-4DFD-92D8-C7432018287FQ36604915-14A8503E-732D-4322-90C8-1C1421531A93Q37580824-A2A49B04-168C-4897-856E-7FF448D55E1FQ41692902-710982FC-C18C-41C1-9456-0416ACACB5F1Q42176500-77B74999-5AEE-427D-8977-9D91B99C8D97Q42600628-C3F07D8F-828F-414E-9C71-1BC2D431D64BQ42728101-6F029BC9-8481-46A9-8B12-6B57A988990CQ42738440-E4FC1205-312D-4F6B-AE7B-D48D52024F6D
P2860
Hydrogen exchange reveals a stable and expandable core within the aspartate receptor cytoplasmic domain.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
2001年學術文章
@zh
2001年學術文章
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name
Hydrogen exchange reveals a st ...... e receptor cytoplasmic domain.
@en
Hydrogen exchange reveals a st ...... e receptor cytoplasmic domain.
@nl
type
label
Hydrogen exchange reveals a st ...... e receptor cytoplasmic domain.
@en
Hydrogen exchange reveals a st ...... e receptor cytoplasmic domain.
@nl
prefLabel
Hydrogen exchange reveals a st ...... e receptor cytoplasmic domain.
@en
Hydrogen exchange reveals a st ...... e receptor cytoplasmic domain.
@nl
P2093
P2860
P356
P1476
Hydrogen exchange reveals a st ...... e receptor cytoplasmic domain.
@en
P2093
P2860
P304
43262-43269
P356
10.1074/JBC.M105585200
P407
P577
2001-09-11T00:00:00Z