Robust protein protein interactions in crowded cellular environments.
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Protein stickiness, rather than number of functional protein-protein interactions, predicts expression noise and plasticity in yeastThe interface of protein structure, protein biophysics, and molecular evolutionInteraction between IGFBP7 and insulin: a theoretical and experimental studyExperimental evolution of protein-protein interaction networksProtein social behavior makes a stronger signal for partner identification than surface geometryAn inter-species protein-protein interaction network across vast evolutionary distanceAnalytic markovian rates for generalized protein structure evolution.Protein-binding dynamics imaged in a living cell.Targeting ligand-gated ion channels in neurology and psychiatry: is pharmacological promiscuity an obstacle or an opportunity?Interplay between pleiotropy and secondary selection determines rise and fall of mutators in stress response.Evolution of specificity in protein-protein interactionsNonspecific binding limits the number of proteins in a cell and shapes their interaction networks.Analysis of genetic interaction networks shows that alternatively spliced genes are highly versatile.Topology of protein interaction network shapes protein abundances and strengths of their functional and nonspecific interactions.Protein misinteraction avoidance causes highly expressed proteins to evolve slowlyRelative Cosolute Size Influences the Kinetics of Protein-Protein Interactions.A one-shot germinal center model under protein structural stability constraintsConstraints imposed by non-functional protein-protein interactions on gene expression and proteome size.Probing the mechanisms of fibril formation using lattice modelsEvolutionary pressure on the topology of protein interface interaction networks.Transient protein-protein interactions perturb E. coli metabolome and cause gene dosage toxicity.Signatures of protein biophysics in coding sequence evolutionGreat interactions: How binding incorrect partners can teach us about protein recognition and function.Molecular organization of cytochrome c2 near the binding domain of cytochrome bc1 studied by electron spin-lattice relaxation enhancementCounterbalance of ligand- and self-coupled motions characterizes multispecificity of ubiquitinIs catalytic activity of chaperones a selectable trait for the emergence of heat shock response?A Simple Model of Protein Domain Swapping in Crowded Cellular Environments.Mutation rates and evolution of multiple coding in RNA-based protocells.Alternative splicing and protein interaction data sets.Rigid-body motions of interacting proteins dominate multispecific binding of ubiquitin in a shape-dependent manner.Phase Transitions in Biological Systems with Many Components.Effect of non-specific interactions on formation and stability of specific complexes.Statistically enhanced promiscuity of structurally correlated patterns.RNA catalysis through compartmentalization.
P2860
Q21093159-052B8F66-EF2A-4C56-BC74-754AD00DE4FBQ26863623-879E570A-281E-4EBF-917A-42E3D662A9E2Q27301256-3D2D8E26-C67B-416B-90AD-4AC35E28B9B9Q28691691-E9064FA0-5688-4800-AEF5-8AAB04171335Q28818852-190236EC-174A-45EB-9523-98BD980B20C4Q28834024-254A6E22-FB12-40D5-A1D4-81CD6084F7F8Q30417959-2F5F698C-6775-4A82-B4F8-0CCCAC8C23CDQ30505105-50C076D6-1DD0-4E4B-BC9F-B42BE57F1C20Q33536146-285DC2BD-C991-4628-9628-999F66AF3706Q33543179-F5456A9A-4C4B-47CF-BF01-127795E06402Q34310281-03E90D91-1B19-4EC1-B9D2-4B27509D3CD6Q34490809-469DBEEB-47F4-49CA-831A-EDBBBC005B30Q34586190-F2CF1FB0-D762-4D5F-A921-EB59FE113A96Q34652806-5193F6F9-C05B-4CF6-8C69-BFB336FFB29CQ35887320-B3037318-0AD6-4924-BE4C-7AF51AEEFDEEQ36062965-78C5C9D4-163A-4BF8-B2D2-AFAC75E3D4D7Q36648968-75EE7740-451E-428B-882C-FD608F7BCD36Q36883198-26778670-34CC-427D-A0C0-03E9C6E6D526Q37165313-285FD2BB-46C7-49F3-9AA4-2DA698FC9731Q37255749-ED32288F-2010-4E74-875C-1585C1DD15C5Q37524872-FA027AB4-32C1-47C9-8431-1B780BE41D79Q37731692-C0BF2421-AE3E-48F2-BFA5-255D788F4C87Q39692552-7F7F0E1A-29CB-4A61-B13C-13EBECD5F661Q40942326-30351C37-4741-47A5-B048-993444B42F3BQ41583765-939DA68B-2EE0-4E2E-BDF3-92AE07A75558Q41853435-10E4B6D0-4BEF-4592-83BF-CD33F751F744Q42576606-797DEAE1-A787-4517-B491-A8ED5ACB4633Q42864380-714B55E7-1346-4132-B283-DB39B64B823AQ45770441-B3658F69-84CA-4D8E-B525-E65AFDD8D509Q47966241-DAFEF2EF-E1BE-49DB-9AA6-6E82A487EF13Q50323477-23C05D30-1DD6-4C44-BC45-E2B0A5AF867BQ51725890-A7F9D871-E43A-435B-BC61-20718B503EDFQ51890546-6AB70D2D-0DD5-42DB-B12D-1E76BE699C34Q53356383-3BEF2DB5-7AB5-4EF0-B778-450275E7575F
P2860
Robust protein protein interactions in crowded cellular environments.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Robust protein protein interactions in crowded cellular environments.
@ast
Robust protein protein interactions in crowded cellular environments.
@en
type
label
Robust protein protein interactions in crowded cellular environments.
@ast
Robust protein protein interactions in crowded cellular environments.
@en
prefLabel
Robust protein protein interactions in crowded cellular environments.
@ast
Robust protein protein interactions in crowded cellular environments.
@en
P2093
P2860
P356
P1476
Robust protein protein interactions in crowded cellular environments.
@en
P2093
Eric J Deeds
Jaline Gerardin
Orr Ashenberg
P2860
P304
14952-14957
P356
10.1073/PNAS.0702766104
P407
P577
2007-09-11T00:00:00Z
P5875
P698
P818
q-bio/0703060