Evolutionary drivers of thermoadaptation in enzyme catalysis. - Wikidata - wikimedia - TriplyDB

Evolutionary drivers of thermoadaptation in enzyme catalysis.

Evolutionary drivers of thermoadaptation in enzyme catalysis.

http://www.wikidata.org/entity/Q42380666

about

Rational Engineering of a Cold-Adapted α-Amylase from the Antarctic Ciliate Euplotes focardii for Simultaneous Improvement of Thermostability and Catalytic Activity.Evolution of nonspectral rhodopsin function at high altitudes.Structural studies of a hyperthermophilic thymidylate kinase enzyme reveal conformational substates along the reaction coordinate.De novo active sites for resurrected Precambrian enzymes.Inducing high activity of a thermophilic enzyme at ambient temperatures by directed evolution.Some Liked It Hot: A Hypothesis Regarding Establishment of the Proto-Mitochondrial Endosymbiont During Eukaryogenesis.Thermosensitivity of growth is determined by chaperone-mediated proteome reallocation.Structural analyses of adenylate kinases from Antarctic and tropical fishes for understanding cold adaptation of enzymes.Structural and Dynamics Comparison of Thermostability in Ancient, Modern, and Consensus Elongation Factor Tus.Convergent selection pressures drive the evolution of rhodopsin kinetics at high altitudes via nonparallel mechanisms.Dynamical origins of heat capacity changes in enzyme-catalysed reactions.Dynamic allostery can drive cold adaptation in enzymes.Coevolution of both thermostability and activity of polyphosphate glucokinase from YX Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins

P2860

Q33820205-76C6338D-B955-4D2E-AA79-5DCDA3EB35CB Q36412903-65116084-9FB3-4381-814D-511D46D59005 Q38719901-BDFDDBCE-399D-4068-A074-671BE4AF6E54 Q41078215-1232620C-ECF5-49F2-AEEA-471399B2FCF3 Q43031824-0B588803-DD75-4BD2-A830-6FDBEB27CADF Q45357655-48306BDA-04F5-497D-A966-E2AFC8AD7B24 Q46138830-562F36E5-CDEA-4FBA-AC17-2CA271D77ACD Q47152848-08AC973D-2E99-41A4-B401-603CDF036EDE Q47177793-7C93B001-1289-4956-939E-C1D0AE3056AF Q47397497-098C99CB-8033-46B1-AD38-46222E32F33A Q52643932-2EE754BC-F89B-437E-955F-BA972CD502F1 Q54976855-BEC99562-4DC8-473B-83D3-93713B4CE350 Q56890080-DBA10582-14AD-494F-88FB-5F8E4BCA18AC Q58569521-AC3AF2BD-4A25-4436-8A31-8065635D115F

P2860

Evolutionary drivers of thermoadaptation in enzyme catalysis.

http://www.wikidata.org/entity/Q42380666

description

2016 nî lūn-bûn

@nan

2016年の論文

@ja

2016年論文

@yue

2016年論文

@zh-hant

2016年論文

@zh-hk

2016年論文

@zh-mo

2016年論文

@zh-tw

2016年论文

@wuu

2016年论文

@zh

2016年论文

@zh-cn

name

Evolutionary drivers of thermoadaptation in enzyme catalysis.

@en

Evolutionary drivers of thermoadaptation in enzyme catalysis.

@nl

type

label

Evolutionary drivers of thermoadaptation in enzyme catalysis.

@en

Evolutionary drivers of thermoadaptation in enzyme catalysis.

@nl

prefLabel

Evolutionary drivers of thermoadaptation in enzyme catalysis.

@en

Evolutionary drivers of thermoadaptation in enzyme catalysis.

@nl

P1433

Q42380666-BF9C6827-F2D5-4225-AACC-94A2D5DF9255

P1476

Q42380666-FD7EFF03-C9FE-4C20-97B8-1E428B921CDC

P2093

Q42380666-0D29239E-00DD-47D2-A428-5579F1731A3D

Q42380666-2A905CD3-3233-481B-A8AB-55F8BB94C2FF

Q42380666-6B83AC09-D51C-4747-A3C2-6D594B18F951

Q42380666-B12ACCCA-F273-4EC2-B6C3-1D4FD25CB354

Q42380666-BCDAFC4E-E2B5-4435-97D6-29F7CD6BDEFA

Q42380666-DDDC1D33-C954-4BC0-9EDA-4FF78EA232D3

P2860

Q42380666-00656C52-7DA2-4044-B85F-A99D8163F655

Q42380666-01BB71EC-C7BA-4230-A260-063EB8F420CC

Q42380666-04AC3744-D154-4C1C-A480-90E2F5F502E2

Q42380666-08805078-CE1C-47C4-B509-B7D1F0AAC294

Q42380666-0A368FA7-458D-45CA-95C7-F64C506D8C7F

Q42380666-0ADC485A-3A9F-46F1-966A-7323EC6B8519

Q42380666-0DD744F3-A98E-493E-BC89-573874E2A270

Q42380666-0F975965-4263-4603-90FD-AF7859670558

Q42380666-11C4DA8D-958B-4DF9-82E0-67507A88F008

Q42380666-1515904F-AB4E-4F7B-9C42-314E14DB170E

P304

Q42380666-02187586-96F2-4125-B92B-0BB93E9A47AF

P31

Q42380666-BBD311BB-FB31-4FE3-99D0-821CA3814840

P356

Q42380666-C2286175-A20E-4E00-88CF-CB6CEFD2032D

P407

Q42380666-570DBB14-A058-4A87-BC19-D8E3C7BB581D

P433

Q42380666-BF42533F-99FB-4993-95BF-AB45873AE434

P478

Q42380666-D4A27414-2146-439A-89C4-5E5995BF2262

P50

Q42380666-B2790736-334B-4BB8-89D7-451FA7A46042

Q42380666-D01A22F6-15C7-4A8F-BD8C-BD411C8201B6

Q42380666-F639EFA1-D548-4B27-804D-E0253A9BFB83

P577

Q42380666-CF7E2C37-14A1-430B-B1EF-E67690018478

P698

Q42380666-076336D8-6722-40A0-ADF8-78784828AB10

P932

Q42380666-427964FA-7CD8-449B-8726-1A70E88A10A1

P356

SCIENCE.AAH3717

P1433

P1476

Evolutionary drivers of thermoadaptation in enzyme catalysis.

@en

P2093

Dorothee Kern

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

Douglas L Theobald

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

John B Stiller

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

Justin English

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

Roman V Agafonov

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

Vy Nguyen

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

P2860

Assessing the accuracy of ancestral protein reconstruction methods

A genomic timescale of prokaryote evolution: insights into the origin of methanogenesis, phototrophy, and the colonization of land

Toward Automatic Reconstruction of a Highly Resolved Tree of Life

MAFFT: a novel method for rapid multiple sequence alignment based on fast Fourier transform

Basic local alignment search tool

Structure and biochemical characterization of an adenylate kinase originating from the psychrophilic organismMarinibacillus marinus

On the origin and evolution of thermophily: reconstruction of functional precambrian enzymes from ancestors of Bacillus

Experimental evidence for the thermophilicity of ancestral life

Hyperstability and substrate promiscuity in laboratory resurrections of Precambrian β-lactamases

Change in heat capacity for enzyme catalysis determines temperature dependence of enzyme catalyzed rates

P304

289-294

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

P31

scholarly article

P356

10.1126/SCIENCE.AAH3717

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

P407

P433

6322

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

P478

355

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

P50

Christopher Wilson

Marc Hoemberger

P577

2016-12-22T00:00:00Z

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

P698

28008087

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

P932

5649376

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