Highly expressed and slowly evolving proteins share compositional properties with thermophilic proteins
about
Merging molecular mechanism and evolution: theory and computation at the interface of biophysics and evolutionary population geneticsProtein thermodynamics can be predicted directly from biological growth ratesDeterminants of the rate of protein sequence evolutionProtein biophysics explains why highly abundant proteins evolve slowlyBioinformatics analysis of disordered proteins in prokaryotes.Impact of translational error-induced and error-free misfolding on the rate of protein evolution.The influence of selection for protein stability on dN/dS estimationsSlow protein evolutionary rates are dictated by surface-core association.Lineage-specific sequence evolution and exon edge conservation partially explain the relationship between evolutionary rate and expression level in A. thalianaThe human phosphotyrosine signaling network: evolution and hotspots of hijacking in cancer.Viral diversity threshold for adaptive immunity in prokaryotes.Contribution of selection for protein folding stability in shaping the patterns of polymorphisms in coding regions.Signatures of protein biophysics in coding sequence evolutionStructure-based analysis of Bacilli and plasmid dihydrofolate reductase evolution.Sequence-Based Analysis of Thermal Adaptation and Protein Energy Landscapes in an Invasive Blue Mussel (Mytilus galloprovincialis).Adaptation to environmental temperature is a major determinant of molecular evolutionary rates in archaea.Thermophilic adaptation in prokaryotes is constrained by metabolic costs of proteostasis.Highly abundant proteins favor more stable 3D structures in yeast.Avoidance of toxic misfolding and protein stability do not explain the sequence constraints of highly expressed proteins.Slow evolution of sex-biased genes in the reproductive tissue of the dioecious plant Salix viminalis.Arabidopsis Heat Stress-Induced Proteins Are Enriched in Electrostatically Charged Amino Acids and Intrinsically Disordered Regions
P2860
Q26861515-7BC35EA1-3110-4613-B94B-C21E49FAB582Q28538355-5757F0A8-0D3E-49AA-B0DC-A491554A6039Q28645761-184D4B64-D9E3-4A75-900D-EB401C1D9F1EQ30530907-6593DF14-C780-4552-8AF5-E8F8D4F3F989Q33834903-E3730324-68FD-4CC0-AA7B-526479D7E3B2Q34344306-6E8054CC-A0CB-4211-9F9C-E2B03162CAB0Q34472599-00FFC7EE-2A07-4A61-B5E8-03D72CB92039Q35091081-77E04322-C349-478D-BED5-2CB7EFA75CC9Q35781197-C9FC18E8-EE2F-45EC-B299-CB6D9146CDC5Q36093876-90660293-3064-42A3-9066-762EAB9D33B6Q36454957-6946AFBA-1683-4643-8499-21EB38BD441DQ37428442-58DA349B-EB8C-4524-8E3B-C348E2895F53Q37731692-0638B5ED-2784-4039-8F32-58659A2E42C5Q39134079-C11B843E-F914-49C5-8268-E4C91B991800Q42659230-FF782447-2BF9-4F6D-899D-4875DDBCBC30Q43031065-CAA3671B-C2EE-44B7-87F8-AF352282D63EQ43033480-F808CB23-9ABC-4921-909A-4C1B593D69E0Q43198178-45DA7E7D-D155-4892-B739-91E3C483E844Q47197817-74CE6E2F-712B-4D75-BCEB-824AFD7BF7ECQ47560472-6E5BD101-394F-427D-8ED3-03D46712D285Q58800968-1D049462-2BD5-4250-BBF0-D2A5627C98D0
P2860
Highly expressed and slowly evolving proteins share compositional properties with thermophilic proteins
description
2009 nî lūn-bûn
@nan
2009 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Highly expressed and slowly ev ...... ies with thermophilic proteins
@ast
Highly expressed and slowly ev ...... ies with thermophilic proteins
@en
type
label
Highly expressed and slowly ev ...... ies with thermophilic proteins
@ast
Highly expressed and slowly ev ...... ies with thermophilic proteins
@en
prefLabel
Highly expressed and slowly ev ...... ies with thermophilic proteins
@ast
Highly expressed and slowly ev ...... ies with thermophilic proteins
@en
P2860
P356
P1476
Highly expressed and slowly ev ...... ies with thermophilic proteins
@en
P2093
Joshua L Cherry
P2860
P304
P356
10.1093/MOLBEV/MSP270
P577
2009-11-12T00:00:00Z