A minimum folding unit in the ankyrin repeat protein p16(INK4)
about
Designed to be stable: crystal structure of a consensus ankyrin repeat proteinThe ankyrin repeat as molecular architecture for protein recognitionCloning and characterization of diacylglycerol kinase iota splice variants in rat brainFolding of a designed simple ankyrin repeat protein.Consensus design of repeat proteins.Biophysical characterization of the free IkappaBalpha ankyrin repeat domain in solution.Local and long-range stability in tandemly arrayed tetratricopeptide repeatsDistribution, expression, and motif variability of ankyrin domain genes in Wolbachia pipientis.Electrostatic interactions mediate binding of obscurin to small ankyrin 1: biochemical and molecular modeling studies.A novel p16(INK4A) mutation associated with esophageal squamous cell carcinoma in a high risk population.Transcriptomics and identification of the chemoreceptor superfamily of the pupal parasitoid of the oriental fruit fly, Spalangia endius Walker (Hymenoptera: Pteromalidae).Chimeras of p14ARF and p16: functional hybrids with the ability to arrest growthStaRProtein, a web server for prediction of the stability of repeat proteins.Probing a moving target with a plastic unfolding intermediate of an ankyrin-repeat protein.Repeat-protein folding: new insights into origins of cooperativity, stability, and topology.Folding landscapes of ankyrin repeat proteins: experiments meet theory.An experimentally determined protein folding energy landscape.Luminescence resonance energy transfer in the cytoplasm of live Escherichia coli cells.The leucine-rich repeat domain of Internalin B folds along a polarized N-terminal pathway.C-terminal domain of p16(INK4a) is adequate in inducing cell cycle arrest, growth inhibition and CDK4/6 interaction similar to the full length protein in HT-1080 fibrosarcoma cells.A compact native 24-residue supersecondary structure derived from the villin headpiece subdomain.Dissection of protein-protein interaction and CDK4 inhibition in the oncogenic versus tumor suppressing functions of gankyrin and P16.Simulation of different truncated p16(INK4a) forms and in silico study of interaction with Cdk4.Stabilizing IkappaBalpha by "consensus" design.Multiple primary melanoma revisited.Novel germline CDKN2A mutation associated with head and neck squamous cell carcinomas and melanomas.A biophysical analysis of the tetratricopeptide repeat-rich mitochondrial import receptor, Tom70, reveals an elongated monomer that is inherently flexible, unstable, and unfolds via a multistate pathway.
P2860
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P2860
A minimum folding unit in the ankyrin repeat protein p16(INK4)
description
2000 nî lūn-bûn
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2000年の論文
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2000年論文
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A minimum folding unit in the ankyrin repeat protein p16(INK4)
@ast
A minimum folding unit in the ankyrin repeat protein p16(INK4)
@en
A minimum folding unit in the ankyrin repeat protein p16(INK4)
@nl
type
label
A minimum folding unit in the ankyrin repeat protein p16(INK4)
@ast
A minimum folding unit in the ankyrin repeat protein p16(INK4)
@en
A minimum folding unit in the ankyrin repeat protein p16(INK4)
@nl
prefLabel
A minimum folding unit in the ankyrin repeat protein p16(INK4)
@ast
A minimum folding unit in the ankyrin repeat protein p16(INK4)
@en
A minimum folding unit in the ankyrin repeat protein p16(INK4)
@nl
P356
P1476
A minimum folding unit in the ankyrin repeat protein p16(INK4)
@en
P2093
P304
P356
10.1006/JMBI.2000.3803
P407
P577
2000-06-16T00:00:00Z