about
Structure-guided recombination creates an artificial family of cytochromes P450.Evolution favors protein mutational robustness in sufficiently large populationsThe loss of adaptive plasticity during long periods of environmental stasisEvolution of molecular error rates and the consequences for evolvability.In the light of directed evolution: pathways of adaptive protein evolutionProtein stability promotes evolvabilityOn the conservative nature of intragenic recombinationExploring protein fitness landscapes by directed evolutionConsensus protein designThe role of robustness in phenotypic adaptation and innovationMechanisms for the Evolution of a Derived Function in the Ancestral Glucocorticoid ReceptorMechanisms of mutational robustness in transcriptional regulationThermodynamics of neutral protein evolutionSelection for robustness in mutagenized RNA virusesDoes mutational robustness inhibit extinction by lethal mutagenesis in viral populations?A model of proteostatic energy cost and its use in analysis of proteome trends and sequence evolutionNatural Variants of the KPC-2 Carbapenemase have Evolved Increased Catalytic Efficiency for Ceftazidime Hydrolysis at the Cost of Enzyme StabilityStrong Selection Significantly Increases Epistatic Interactions in the Long-Term Evolution of a ProteinSelection for Protein Kinetic Stability Connects Denaturation Temperatures to Organismal Temperatures and Provides Clues to Archaean LifeRapid bursts and slow declines: on the possible evolutionary trajectories of enzymesEffects of metabolic rate on protein evolutionLethal mutagenesis of bacteriaTolerance of a Knotted Near-Infrared Fluorescent Protein to Random Circular PermutationPrediction of mutational tolerance in HIV-1 protease and reverse transcriptase using flexible backbone protein designMutagenesis-based definitions and probes of residue burial in proteins.Structural determinants of the rate of protein evolution in yeast.A nonadaptive origin of a beneficial trait: in silico selection for free energy of folding leads to the neutral emergence of mutational robustness in single domain proteins.Stylus: a system for evolutionary experimentation based on a protein/proteome model with non-arbitrary functional constraintsTranslationally optimal codons associate with structurally sensitive sites in proteinsThe evolvability of programmable hardwareEvolutionary fates within a microbial population highlight an essential role for protein folding during natural selection.Biophysical Models of Protein Evolution: Understanding the Patterns of Evolutionary Sequence Divergence.A computational-experimental approach identifies mutations that enhance surface expression of an oseltamivir-resistant influenza neuraminidase.Evolutionary dynamics on protein bi-stability landscapes can potentially resolve adaptive conflicts.Neutral genetic drift can alter promiscuous protein functions, potentially aiding functional evolution.Escape from Adaptive Conflict follows from weak functional trade-offs and mutational robustnessProbing impact of active site residue mutations on stability and activity of Neisseria polysaccharea amylosucrase.Fisher's geometric model of adaptation meets the functional synthesis: data on pairwise epistasis for fitness yields insights into the shape and size of phenotype spaceIn silico genetic robustness analysis of microRNA secondary structures: potential evidence of congruent evolution in microRNASoftware for the analysis and visualization of deep mutational scanning data.
P2860
Q21146061-A86E0881-ED6D-44D4-AAC3-831644732ABFQ21245352-33C1AA4A-D031-4F61-9719-4EF4069C45B9Q22066109-2F5E6C4E-A6BE-4008-8176-BE1834BDAE1AQ22066264-8499C663-4361-4FAC-A5BF-A8F9702492D7Q22066327-F1E97AA8-0095-4965-B0AE-1A6F292B7AA7Q24546311-C80187AC-2C77-40CF-9943-939941EDC3C1Q24555721-7A376F06-6D2E-4BEB-8040-2D151F53B1ABQ24630945-1DF295A9-52C3-4812-810A-3DD2E803A95FQ26748100-5179AD85-4C94-4397-83DB-CBD1C1BBCE23Q27011463-78712553-457F-46DB-8B41-08F9C5FF58C9Q27670528-A8E477B5-23C7-48A8-961C-F93215C42AA3Q28082759-86E61436-9F35-426D-97B1-F3C8908DBDA6Q28274517-3EBEDB8A-BDF0-4030-A1A6-A74DE93F5FCAQ28469235-50B07A15-1662-494B-ADC7-DC478AA1216AQ28474346-03A738C7-CEB5-493C-97B3-0660DA1D942CQ28540274-7CF8D905-50C4-43E8-BAE4-380C2ACFBD6DQ28547682-4625FBD8-65D2-4018-94DC-97ADFC7C0D64Q28551065-7A1C3CE7-F8DF-4204-806D-DF7B52346425Q28601855-8A962D62-EBE0-4753-A646-216FF76BBDA8Q28607014-22B80F95-399F-442A-B155-2DAA1A200C2DQ28754488-7ECBC2B3-3947-4ED1-B9F4-3CE193221BB2Q28756839-AABA50A9-87CA-46B0-AEBB-DA62F1656438Q28818951-F47C27AE-04F0-4C0C-B615-0A940EAFCA39Q28914732-2C344062-45D0-4922-B863-8A9627FEDDE2Q30351711-62D56D04-901A-4DEC-95C8-A389054A05B5Q30354999-B32BF025-4F55-4128-9AF7-BF6EE7774D03Q30357135-07240892-8127-4B9E-BF20-4FA8FAC6917CQ30369737-4E2F0A27-82EA-4D20-B967-294AEB015ACDQ30376006-24A32E1F-D4B9-418C-BF53-88D44E67D520Q30390157-D4998B7A-2969-459C-8716-9D745B6BDBA7Q30391409-44F97BC3-B9DC-421F-BC9E-48846055F873Q30399998-87E63904-2BDF-4E3C-B6C9-57CADDF449A9Q30405350-E991997C-0C57-47D3-9DA4-F2F9C0124E6EQ30421817-753382F7-BD95-42F9-9F7A-58978EDE7039Q30479736-A4C7CFDD-4741-407F-8B80-F6977591D5C3Q30524952-6754C145-B316-4F8F-8ADF-9C20E806194DQ30558087-A02B9B0C-C784-4E13-9A35-7C191EE60277Q30671403-CFFEDD6F-70EA-474C-82F0-5160F177FE3FQ30838235-134D6BE9-67F6-4CAF-8759-E2CBF3EE8564Q30954769-7B3728F5-F6C2-4EE6-BAE9-4205750504B9
P2860
description
2005 nî lūn-bûn
@nan
2005 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
name
Thermodynamic prediction of protein neutrality
@ast
Thermodynamic prediction of protein neutrality
@en
Thermodynamic prediction of protein neutrality
@nl
type
label
Thermodynamic prediction of protein neutrality
@ast
Thermodynamic prediction of protein neutrality
@en
Thermodynamic prediction of protein neutrality
@nl
prefLabel
Thermodynamic prediction of protein neutrality
@ast
Thermodynamic prediction of protein neutrality
@en
Thermodynamic prediction of protein neutrality
@nl
P2860
P50
P3181
P356
P1476
Thermodynamic prediction of protein neutrality
@en
P2093
Jonathan J Silberg
P2860
P304
P3181
P356
10.1073/PNAS.0406744102
P407
P577
2005-01-18T00:00:00Z
P5875
P698
P818
q-bio/0409013