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Comparing models of evolution for ordered and disordered proteins.

Comparing models of evolution for ordered and disordered proteins.

http://www.wikidata.org/entity/Q30382652

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Classification of intrinsically disordered regions and proteins Causes of evolutionary rate variation among protein sites The Cellular Prion Protein: A Player in Immunological Quiescence Computational approaches for inferring the functions of intrinsically disordered proteins Disease mutations in disordered regions--exception to the rule?Physical motif clustering within intrinsically disordered nucleoporin sequences reveals universal functional features Markov models of amino acid substitution to study proteins with intrinsically disordered regions A widely employed germ cell marker is an ancient disordered protein with reproductive functions in diverse eukaryotes Parallel dynamics and evolution: Protein conformational fluctuations and assembly reflect evolutionary changes in sequence and structure.The evolution of protein structures and structural ensembles under functional constraint.Evolutionary patterns in coiled-coils.Uncertainty analysis in protein disorder prediction.Disease-associated mutations disrupt functionally important regions of intrinsic protein disorder A comparative study of Whi5 and retinoblastoma proteins: from sequence and structure analysis to intracellular networks.Emergence and evolution of an interaction between intrinsically disordered proteins.Intrinsically disordered domains deviate significantly from random sequences in mammalian proteins.Interplay between chaperones and protein disorder promotes the evolution of protein networks.Describing sequence-ensemble relationships for intrinsically disordered proteins.The evolution of the coding exome of the Arabidopsis species--the influences of DNA methylation, relative exon position, and exon length.Impacts of pretranscriptional DNA methylation, transcriptional transcription factor, and posttranscriptional microRNA regulations on protein evolutionary rate Detecting remote sequence homology in disordered proteins: discovery of conserved motifs in the N-termini of Mononegavirales phosphoproteins Biophysics of protein evolution and evolutionary protein biophysics Sequence evolution of the intrinsically disordered and globular domains of a model viral oncoprotein.Cellulase linkers are optimized based on domain type and function: insights from sequence analysis, biophysical measurements, and molecular simulation.Origins of Myc proteins--using intrinsic protein disorder to trace distant relatives.Evolution and disorder.Slow protein evolutionary rates are dictated by surface-core association.Increased polymorphism near low-complexity sequences across the genomes of Plasmodium falciparum isolates.The relationships among microRNA regulation, intrinsically disordered regions, and other indicators of protein evolutionary rate.The intrinsically disordered regions of the Drosophila melanogaster Hox protein ultrabithorax select interacting proteins based on partner topology.Interspecific adaptation by binary choice at de novo polyomavirus T antigen site through accelerated codon-constrained Val-Ala toggling within an intrinsically disordered region Polymorphism Analysis Reveals Reduced Negative Selection and Elevated Rate of Insertions and Deletions in Intrinsically Disordered Protein Regions.Determinants of exon-level evolutionary rates in Arabidopsis species.Selective constraint on human pre-mRNA splicing by protein structural properties From sequence and forces to structure, function, and evolution of intrinsically disordered proteins The case for intrinsically disordered proteins playing contributory roles in molecular recognition without a stable 3D structure.Characterization of the bipartite degron that regulates ubiquitin-independent degradation of thymidylate synthase.Evolution of disorder in Mediator complex and its functional relevance Conserved properties of individual Ca2+-binding sites in calmodulin Purifying selection shapes the coincident SNP distribution of primate coding sequences.

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P2860

Comparing models of evolution for ordered and disordered proteins.

http://www.wikidata.org/entity/Q30382652

description

2009 nî lūn-bûn

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2009 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

@zh-hk

2009年論文

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2009年論文

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2009年论文

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name

Comparing models of evolution for ordered and disordered proteins.

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Comparing models of evolution for ordered and disordered proteins.

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type

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Comparing models of evolution for ordered and disordered proteins.

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Comparing models of evolution for ordered and disordered proteins.

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prefLabel

Comparing models of evolution for ordered and disordered proteins.

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Comparing models of evolution for ordered and disordered proteins.

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Molecular Biology and Evolution

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Comparing models of evolution for ordered and disordered proteins.

@en

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Audra K Johnson

http://www.w3.org/2001/XMLSchema#string

Celeste J Brown

http://www.w3.org/2001/XMLSchema#string

Gary W Daughdrill

http://www.w3.org/2001/XMLSchema#string

P2860

Improved disorder prediction by combination of orthogonal approaches

Intrinsically Disordered Proteins in Human Diseases: Introducing the D 2 Concept

Intrinsically unstructured proteins and their functions

Prediction and Functional Analysis of Native Disorder in Proteins from the Three Kingdoms of Life

Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain

The Protein Data Bank

Gapped BLAST and PSI-BLAST: a new generation of protein database search programs

Amino acid substitution matrices from protein blocks

NMR chemical shift and relaxation measurements provide evidence for the coupled folding and binding of the p53 transactivation domain

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10.1093/MOLBEV/MSP277

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3

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27

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19923193

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protein evolution

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2822292

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