Pages that link to "Q56902968"

The following pages link to Structure and Function of the Conserved Domain in αA-Crystallin. Site-Directed Spin Labeling Identifies a β-Strand Located near a Subunit Interface (Q56902968):

Displaying 40 items.

• Cataract-linked γD-crystallin mutants have weak affinity to lens chaperones α-crystallins (Q24303942) (← links)
• Crystallin gene mutations in Indian families with inherited pediatric cataract (Q24336750) (← links)
• Crystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens function (Q27661297) (← links)
• Non-3D domain swapped crystal structure of truncated zebrafish alphaA crystallin (Q27663643) (← links)
• Crystal Structure of an Activated Variant of Small Heat Shock Protein Hsp16.5 (Q27679512) (← links)
• Effects of modifications of alpha-crystallin on its chaperone and other properties (Q28193145) (← links)
• Role of the C-terminal extensions of alpha-crystallins. Swapping the C-terminal extension of alpha-crystallin to alphaB-crystallin results in enhanced chaperone activity (Q28910389) (← links)
• Exploring protein solution structure: Second moments of fluorescent spectra report heterogeneity of tryptophan rotamers. (Q30376126) (← links)
• Algorithm for selection of optimized EPR distance restraints for de novo protein structure determination (Q30396233) (← links)
• Chaperone function of mutant versions of alpha A- and alpha B-crystallin prepared to pinpoint chaperone binding sites (Q31897258) (← links)
• Structural and functional changes in the alpha A-crystallin R116C mutant in hereditary cataracts (Q33989123) (← links)
• Mechanism of cataract formation in alphaA-crystallin Y118D mutation (Q34402815) (← links)
• Role of Subunit Exchange and Electrostatic Interactions on the Chaperone Activity of Mycobacterium leprae HSP18 (Q35670610) (← links)
• Sequence, structure, and dynamic determinants of Hsp27 (HspB1) equilibrium dissociation are encoded by the N-terminal domain (Q35801033) (← links)
• Spectral contribution of the individual tryptophan of alphaB-crystallin: a study by site-directed mutagenesis (Q36281400) (← links)
• Cryoelectron microscopy analysis of small heat shock protein 16.5 (Hsp16.5) complexes with T4 lysozyme reveals the structural basis of multimode binding (Q36620780) (← links)
• Differential role of arginine mutations on the structure and functions of α-crystallin (Q37021424) (← links)
• Mutation R120G in alphaB-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function (Q37198800) (← links)
• An alphaA-crystallin gene mutation, Arg12Cys, causing inherited cataract-microcornea exhibits an altered heat-shock response. (Q37213683) (← links)
• alphaB-crystallin: a hybrid solid-state/solution-state NMR investigation reveals structural aspects of the heterogeneous oligomer (Q37218362) (← links)
• Structure and mechanism of protein stability sensors: chaperone activity of small heat shock proteins (Q37424170) (← links)
• Species-Specific Structural and Functional Divergence of α-Crystallins: Zebrafish αBa- and Rodent αA(ins)-Crystallin Encode Activated Chaperones (Q37589738) (← links)
• Small heat-shock proteins: important players in regulating cellular proteostasis (Q38263437) (← links)
• Mutation of alpha B-crystallin: effects on chaperone-like activity (Q38335911) (← links)
• Trimethylamine N-oxide alleviates the severe aggregation and ER stress caused by G98R alphaA-crystallin (Q39759924) (← links)
• Ligand binding site of tear lipocalin: contribution of a trigonal cluster of charged residues probed by 8-anilino-1-naphthalenesulfonic acid (Q40641400) (← links)
• The pivotal role of the beta 7 strand in the intersubunit contacts of different human small heat shock proteins (Q41833984) (← links)
• Thermal stability of human alpha-crystallins sensed by amide hydrogen exchange (Q41864727) (← links)
• Mutations and modifications support a 'pitted-flexiball' model for alpha-crystallin (Q42680131) (← links)
• Subunit exchange, conformational stability, and chaperone-like function of the small heat shock protein 16.5 from Methanococcus jannaschii (Q43480275) (← links)
• Structural and Functional Defects Caused by Point Mutations in the α-Crystallin Domain of a Bacterial α-Heat Shock Protein (Q44428756) (← links)
• Role of the conserved SRLFDQFFG region of alpha-crystallin, a small heat shock protein. Effect on oligomeric size, subunit exchange, and chaperone-like activity (Q44610052) (← links)
• alpha-Crystallin C-terminal domain: on the track of an Ig fold (Q47897000) (← links)
• alpha-Crystallin quaternary structure and interactive properties control eye lens transparency (Q47897014) (← links)
• Recent advances in site-directed spin labeling of proteins (Q56902488) (← links)
• Transgenic zebrafish models reveal distinct molecular mechanisms for cataract-linked αA-crystallin mutants (Q59811448) (← links)
• The determinants of the oligomeric structure in Hsp16.5 are encoded in the alpha-crystallin domain (Q74144036) (← links)
• Mechanism of chaperone function in small heat shock proteins. Two-mode binding of the excited states of T4 lysozyme mutants by alphaA-crystallin (Q74633092) (← links)
• Engineering of a Polydisperse Small Heat-Shock Protein Reveals Conserved Motifs of Oligomer Plasticity (Q89462234) (← links)
• Clinical characteristics of congenital lamellar cataract and myopia in a Chinese family (Q89499090) (← links)