Human full-length Securin is a natively unfolded protein.
about
Dematin exhibits a natively unfolded core domain and an independently folded headpiece domainPTTG1 attenuates drug-induced cellular senescenceStructure-Based Identification, Characterization, and Disruption of Human Securin-Binding SH3 Domains in Lung Cancer.Functional anthology of intrinsic disorder. 3. Ligands, post-translational modifications, and diseases associated with intrinsically disordered proteins.PR65, the HEAT-repeat scaffold of phosphatase PP2A, is an elastic connector that links force and catalysisCritical differences between isoforms of securin reveal mechanisms of separase regulationAnnular arrangement and collaborative actions of four domains of protein-disulfide isomerase: a small angle X-ray scattering study in solution.NMR determines transient structure and dynamics in the disordered C-terminal domain of WASp interacting proteinAlanine and proline content modulate global sensitivity to discrete perturbations in disordered proteins.Hydrodynamic Radii of Intrinsically Disordered Proteins Determined from Experimental Polyproline II Propensities.Tryptophan fluorescence reveals the presence of long-range interactions in the denatured state of ribonuclease Sa.A closed conformation of the Caenorhabditis elegans separase-securin complex.The relevance of protein-protein interactions for p53 function: the CPE contribution.Pituitary tumor-transforming gene and its binding factor in endocrine cancer.Intrinsic α helix propensities compact hydrodynamic radii in intrinsically disordered proteins.Biology and insights into the role of cohesin protease separase in human malignancies.A J-modulated protonless NMR experiment characterizes the conformational ensemble of the intrinsically disordered protein WIP.Molecular epitopes of the ankyrin-spectrin interaction.Cryo-EM structure of a metazoan separase-securin complex at near-atomic resolution.Temperature-dependent structural changes in intrinsically disordered proteins: formation of alpha-helices or loss of polyproline II?The ABBA motif binds APC/C activators and is shared by APC/C substrates and regulatorsConformation of the EPEC Tir protein in solution: investigating the impact of serine phosphorylation at positions 434/463.Virulence factor of potato virus Y, genome-attached terminal protein VPg, is a highly disordered protein.Structural biology of the separase-securin complex with crucial roles in chromosome segregation.
P2860
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P2860
Human full-length Securin is a natively unfolded protein.
description
2005 nî lūn-bûn
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2005年の論文
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2005年学术文章
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2005年学术文章
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name
Human full-length Securin is a natively unfolded protein.
@en
Human full-length Securin is a natively unfolded protein.
@nl
type
label
Human full-length Securin is a natively unfolded protein.
@en
Human full-length Securin is a natively unfolded protein.
@nl
prefLabel
Human full-length Securin is a natively unfolded protein.
@en
Human full-length Securin is a natively unfolded protein.
@nl
P2860
P356
P1433
P1476
Human full-length Securin is a natively unfolded protein.
@en
P2093
Nuria Sánchez-Puig
P2860
P304
P356
10.1110/PS.051368005
P577
2005-06-01T00:00:00Z