The betagamma-crystallin superfamily contains a universal motif for binding calcium
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A novel interdomain interface in crystallins: structural characterization of the βγ-crystallin from Geodia cydonium at 0.99 Å resolutionStructure and Substrate Specificity of a Eukaryotic Fucosidase from Fusarium graminearumBig domains are novel Ca²+-binding modules: evidences from big domains of Leptospira immunoglobulin-like (Lig) proteinsCa2+-binding motif of βγ-crystallins.Crybb2 coding for βB2-crystallin affects sensorimotor gating and hippocampal function.Guanidine-HCl dependent structural unfolding of M-crystallin: fluctuating native state like topologies and intermolecular association.Association properties and unfolding of a βγ-crystallin domain of a Vibrio-specific proteinγS-crystallin proteins from the Antarctic nototheniid toothfish: a model system for investigating differential resistance to chemical and thermal denaturation.L-type calcium channels play a critical role in maintaining lens transparency by regulating phosphorylation of aquaporin-0 and myosin light chain and expression of connexinsOn the accuracy of unit-cell parameters in protein crystallography.The glaucoma-associated olfactomedin domain of myocilin is a novel calcium binding protein.Solution structure of the Big domain from Streptococcus pneumoniae reveals a novel Ca2+-binding module.Evolution of crystallins for a role in the vertebrate eye lens.Expression of βA3/A1-crystallin in the developing and adult rat eye.Evolutionary remodeling of βγ-crystallins for domain stability at cost of Ca2+ binding.Primary sequence contribution to the optical function of the eye lens.Single-molecule Force Spectroscopy Reveals the Calcium Dependence of the Alternative Conformations in the Native State of a βγ-Crystallin Protein.Exploring the sequence-structure-function relationship for the intrinsically disordered βγ-crystallin Hahellin.Contributions of aromatic pairs to the folding and stability of long-lived human γD-crystallin.RapA2 is a calcium-binding lectin composed of two highly conserved cadherin-like domains that specifically recognize Rhizobium leguminosarum acidic exopolysaccharides.Backbone ¹H, ¹³C and ¹⁵N resonance assignments of an intrinsically unstructured βγ-crystallin from Hahella chejuensis.Identification of New Virulence Factors and Vaccine Candidates for Yersinia pestis.Complete backbone and DENQ side chain NMR assignments in proteins from a single experiment: implications to structure-function studies.
P2860
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P2860
The betagamma-crystallin superfamily contains a universal motif for binding calcium
description
2009 nî lūn-bûn
@nan
2009 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2009年の論文
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2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
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name
The betagamma-crystallin superfamily contains a universal motif for binding calcium
@ast
The betagamma-crystallin superfamily contains a universal motif for binding calcium
@en
The betagamma-crystallin superfamily contains a universal motif for binding calcium
@nl
type
label
The betagamma-crystallin superfamily contains a universal motif for binding calcium
@ast
The betagamma-crystallin superfamily contains a universal motif for binding calcium
@en
The betagamma-crystallin superfamily contains a universal motif for binding calcium
@nl
prefLabel
The betagamma-crystallin superfamily contains a universal motif for binding calcium
@ast
The betagamma-crystallin superfamily contains a universal motif for binding calcium
@en
The betagamma-crystallin superfamily contains a universal motif for binding calcium
@nl
P2093
P356
P1433
P1476
The betagamma-crystallin superfamily contains a universal motif for binding calcium
@en
P2093
Amita Mishra
Maroor K Jobby
Penmatsa Aravind
Rajan Sankaranarayanan
Shashi Kumar Suman
Yogendra Sharma
P304
P356
10.1021/BI9017076
P407
P577
2009-12-29T00:00:00Z