about
Prostate-associated gene 4 (PAGE4), an intrinsically disordered cancer/testis antigen, is a novel therapeutic target for prostate cancerRNA polymerase and the ribosome: the close relationshipAn α Helix to β Barrel Domain Switch Transforms the Transcription Factor RfaH into a Translation FactorStructure and dynamics of a primordial catalytic fold generated by in vitro evolutionNew Tricks of an Old Pattern: STRUCTURAL VERSATILITY OF SCORPION TOXINS WITH COMMON CYSTEINE SPACINGMutational Tipping Points for Switching Protein Folds and FunctionsSelective unfolding of one Ribonuclease H domain of HIV reverse transcriptase is linked to homodimer formationMultiple stable conformations account for reversible concentration-dependent oligomerization and autoinhibition of a metamorphic metallopeptidaseConstraint methods that accelerate free-energy simulations of biomoleculesProtein stability: a crystallographer's perspectiveStructural Maturation of HIV-1 Reverse Transcriptase-A Metamorphic Solution to Genomic InstabilityFive Questions (with their Answers) on ER-Associated DegradationComputing the relative stabilities and the per-residue components in protein conformational changes.Virtual screening on an α-helix to β-strand switchable region of the FGFR2 extracellular domain revealed positive and negative modulators.Amino acid distribution rules predict protein fold: protein grammar for beta-strand sandwich-like structuresProtein secondary structure prediction using a small training set (compact model) combined with a Complex-valued neural network approach.Structural gymnastics of multifunctional metamorphic proteins.NMR-based structural biology of proteins in supercooled water.Conditionally disordered proteins: bringing the environment back into the fold.Evolutionary bridges to new protein folds: design of C-terminal Cro protein chameleon sequences.Is a malleable protein necessarily highly dynamic? The hydrophobic core of the nuclear coactivator binding domain is well ordered.Evolutionary dynamics on protein bi-stability landscapes can potentially resolve adaptive conflicts.A polymetamorphic protein.Escape from Adaptive Conflict follows from weak functional trade-offs and mutational robustnessA horizontal alignment tool for numerical trend discovery in sequence data: application to protein hydropathy.Bootstrapping new protein foldsSmooth functional transition along a mutational pathway with an abrupt protein fold switch.Biophysics of protein evolution and evolutionary protein biophysicsThe albumin-binding domain as a scaffold for protein engineering.Contribution to the prediction of the fold code: application to immunoglobulin and flavodoxin cases.Studying protein fold evolution with hybrids of differently folded homologsFolding simulations of the A and B domains of protein GPhosphorylation-induced Conformational Ensemble Switching in an Intrinsically Disordered Cancer/Testis Antigen.Fast learning optimized prediction methodology (FLOPRED) for protein secondary structure predictionRegulated unfolding of proteins in signalingRelief of autoinhibition by conformational switch explains enzyme activation by a catalytically dead paralogConverting a protein into a switch for biosensing and functional regulation.Structural and functional insights into human vitamin K epoxide reductase and vitamin K epoxide reductase-like1.Folding the proteome.Expanding Anfinsen's principle: contributions of synonymous codon selection to rational protein design.
P2860
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P2860
description
2010 nî lūn-bûn
@nan
2010 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Proteins that switch folds
@ast
Proteins that switch folds
@en
Proteins that switch folds
@nl
type
label
Proteins that switch folds
@ast
Proteins that switch folds
@en
Proteins that switch folds
@nl
prefLabel
Proteins that switch folds
@ast
Proteins that switch folds
@en
Proteins that switch folds
@nl
P2860
P1476
Proteins that switch folds
@en
P2093
John Orban
Philip N Bryan
P2860
P304
P356
10.1016/J.SBI.2010.06.002
P577
2010-06-28T00:00:00Z