Improvement of the Thermostability and Activity of a Pectate Lyase by Single Amino Acid Substitutions, Using a Strategy Based on Melting-Temperature-Guided Sequence Alignment - Wikidata - awgldk - TriplyDB

Improvement of the Thermostability and Activity of a Pectate Lyase by Single Amino Acid Substitutions, Using a Strategy Based on Melting-Temperature-Guided Sequence Alignment

Improvement of the Thermostability and Activity of a Pectate Lyase by Single Amino Acid Substitutions, Using a Strategy Based on Melting-Temperature-Guided Sequence Alignment

http://www.wikidata.org/entity/Q27649410

about

Design of thermostable rhamnogalacturonan lyase mutants from Bacillus licheniformis by combination of targeted single point mutations Cloning, expression and characterization of a pectate lyase from Paenibacillus sp. 0602 in recombinant Escherichia coli In silico characterization of pectate lyase protein sequences from different source organisms.Nanotechnology enabled enhancement of enzyme activity and thermostability: study on impaired pectate lyase from attenuated Macrophomina phaseolina in presence of hydroxyapatite nanoparticle Enhancing RGI lyase thermostability by targeted single point mutations.Directed Evolution and Structural Analysis of Alkaline Pectate Lyase from the Alkaliphilic Bacterium Bacillus sp. Strain N16-5 To Improve Its Thermostability for Efficient Ramie Degumming Common protein sequence signatures associate with Sclerotinia borealis lifestyle and secretion in fungal pathogens of the Sclerotiniaceae.Exploring the thermostable properties of halohydrin dehalogenase from Agrobacterium radiobacter AD1 by a combinatorial directed evolution strategy.Aquatic adaptation of a laterally acquired pectin degradation pathway in marine gammaproteobacteria.Modulating protein stability - directed evolution strategies for improved protein function.An ancestral member of the polysaccharide lyase family 2 displays endolytic activity and magnesium dependence.Computational design of a thermostable mutant of cocaine esterase via molecular dynamics simulations.Characterization of two Paenibacillus amylolyticus strain 27C64 pectate lyases with activity on highly methylated pectin.A pectate lyase from a deep subseafloor Georgenia muralis with unusual molecular characteristics.Engineering the thermostability of β-glucuronidase from Penicillium purpurogenum Li-3 by loop transplant.Improving the thermoactivity and thermostability of pectate lyase from Bacillus pumilus for ramie degumming.Immobilization of recombinant pectate lyase from Clostridium thermocellum ATCC-27405 on magnetic nanoparticles for bioscouring of cotton fabric.ProtDataTherm: A database for thermostability analysis and engineering of proteins.Survey of protein engineering strategies Loss of a conserved salt bridge in bacterial glycosyl hydrolase BgIM-G1 improves substrate binding in temperate environments

P2860

Q27688892-61ABD447-7684-40D2-9543-872D57454F7F Q33557322-C68DDE5D-ACE3-454E-9327-9DE8B4F6FE95 Q34234545-9DA3B150-C4DD-4713-BBD5-40136482B376 Q34730700-F61BB7A1-F8BE-4166-8DE1-632971773C89 Q34977310-7AAEFC15-F42C-44EF-A91D-B52203584B64 Q36000437-B5697A92-F938-4055-A9B8-8DB1573527EF Q36097815-BD674643-D192-4C88-BB02-355B23ECCBC9 Q36245944-BD968EDD-4F06-44B8-B1E7-ADD725EC076B Q36301757-16AC2031-BE37-494E-B397-9163BC96A9AB Q38109676-C4D21AA6-EB89-4911-B6FC-9C86C9407411 Q41393781-CC271F4A-A43A-47BF-9C34-A3618385CB5D Q41851551-065DAD04-7748-4DB9-B2E6-B8E2104638A5 Q42430182-38C01084-4E9A-442F-9D8E-2EC5415F694A Q43022827-308E5DF4-CFDF-4B2D-A387-DC237A427C99 Q43027757-5EFE35DE-5382-41D8-978A-A8D822E909BE Q45740786-483FDA5D-FF79-4F62-8AC2-F9C999D948BA Q47647227-C7B65E17-BF0D-491E-9D5B-1F7B2F1C9766 Q48149849-4BF13F44-1A50-4A0E-ACB9-EF1FE0CB3A9E Q56895981-56305623-73C9-4209-9AF6-1D6118097F0F Q57813224-5F74DBBD-81E2-44A2-AC4B-606BD50A01B2

P2860

Improvement of the Thermostability and Activity of a Pectate Lyase by Single Amino Acid Substitutions, Using a Strategy Based on Melting-Temperature-Guided Sequence Alignment

http://www.wikidata.org/entity/Q27649410

description

2008 nî lūn-bûn

@nan

2008 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2008年の論文

@ja

2008年論文

@yue

2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

@zh-mo

2008年論文

@zh-tw

2008年论文

@wuu

name

Improvement of the Thermostabi ...... ture-Guided Sequence Alignment

@ast

Improvement of the Thermostabi ...... ture-Guided Sequence Alignment

@en

Improvement of the Thermostabi ...... ture-Guided Sequence Alignment

@nl

type

label

Improvement of the Thermostabi ...... ture-Guided Sequence Alignment

@ast

Improvement of the Thermostabi ...... ture-Guided Sequence Alignment

@en

Improvement of the Thermostabi ...... ture-Guided Sequence Alignment

@nl

prefLabel

Improvement of the Thermostabi ...... ture-Guided Sequence Alignment

@ast

Improvement of the Thermostabi ...... ture-Guided Sequence Alignment

@en

Improvement of the Thermostabi ...... ture-Guided Sequence Alignment

@nl

P1433

Q27649410-A2BA68E5-D0B5-4D47-9A6D-DDC96AF8C36F

P1476

Q27649410-5817972F-470F-413E-A8D9-3265340AAF9F

P2093

Q27649410-0029C901-9AB6-47F1-B879-9E531D25209C

Q27649410-095982FB-C969-49F1-9507-ABC31FAE4F6A

Q27649410-0C0797CF-D78D-41BD-B008-2C17980E905A

Q27649410-2316F3AF-C7D7-4A69-B492-BB86CDB9CA62

Q27649410-3CF5CE7F-F58E-46CE-8C3C-01A8E242EAE3

Q27649410-913DA0DF-D285-479E-91D2-9AB5773D0329

Q27649410-A7881EED-CB5C-4622-9ECD-ACE87EA37051

Q27649410-BE212F4D-2C9C-42B0-B610-8936BA9485AD

P2860

Q27649410-1295EC1E-906D-4073-9984-B8A701C629FA

Q27649410-16D75CFF-AB03-448B-B808-C76D2F625B76

Q27649410-1C671CFE-3DEE-401D-8C91-4C56570FA669

Q27649410-209DC3DB-77D0-4EDC-A009-73F3C32F9B19

Q27649410-2826074F-DF22-4352-A5BD-E03A11319705

Q27649410-2E27E22C-E88E-4513-92F5-AAD00851B6A2

Q27649410-2F6F48BB-A135-4BC1-B44A-CBD0E3EACB53

Q27649410-305245F2-859A-4D17-86CE-5BB02E5559B5

Q27649410-30F44D87-7CFB-4646-BB64-161824460325

Q27649410-333FE761-4420-4194-AF34-216C86D3FF6B

P304

Q27649410-FB243BB7-5E37-4636-AF17-BEDB0724FEF0

P31

Q27649410-1B876D76-6FB3-4CB6-BB7D-FFE64E4C243D

P356

Q27649410-D498AA6C-7EAB-40E3-BAB8-35730EBE5ADC

P407

Q27649410-C42B6F7C-4204-4CCD-BC2E-A415BC3CE682

P433

Q27649410-E953904B-8B90-4B31-AADB-0AD084B6379B

P478

Q27649410-5D5B6D9F-B08B-449C-A278-92AF1EE7252E

P50

Q27649410-632408E7-4DA2-4FC7-8CB6-182168617348

P577

Q27649410-AF9940AB-4381-4882-89E0-77A9D1CC4F26

P698

Q27649410-BC32629B-5897-4971-93F0-0127C023C5CB

P921

Q27649410-0C9CA874-3BD8-4148-86E0-325317E9E9F7

Q27649410-A7CD4AF2-B7E1-4F5C-826D-BDD5B7187B6F

Q27649410-BDF62498-5C7E-45B8-AC77-DBE968E2B931

P932

Q27649410-B484B37B-A285-4336-B506-F5FCD328BA64

P356

P1433

Applied and Environmental Microbiology

P1476

Improvement of the Thermostabi ...... ture-Guided Sequence Alignment

@en

P2093

David Shaya

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

Hélène Bergeron

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

Manon Beauchemin

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

Marie-Line Garron

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

Peter C K Lau

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

Stephan Grosse

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

Traian Sulea

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

Zhizhuang Xiao

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

P2860

Comparison of the genomes of two Xanthomonas pathogens with differing host specificities

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

The Refined Three-Dimensional Structure of Pectate Lyase E from Erwinia chrysanthemi at 2.2 A Resolution

Effect of mutations in the T1.5 loop of pectate lyase A from Erwinia chrysanthemi EC16

Coot: model-building tools for molecular graphics

ARP/wARP and molecular replacement

WHAT IF: a molecular modeling and drug design program

Solvent content of protein crystals

Refinement of macromolecular structures by the maximum-likelihood method

Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability

P304

1183-9

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

P31

scholarly article

P356

10.1128/AEM.02220-07

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

P407

P433

4

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

P478

74

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

P50

Miroslaw Cygler

P577

2008-02-01T00:00:00Z

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

P698

18156340

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

P921

P932

2258563

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