Conformational dynamics of Thermus aquaticus DNA polymerase I during catalysis. - Wikidata - wikimedia - TriplyDB

Conformational dynamics of Thermus aquaticus DNA polymerase I during catalysis.

Conformational dynamics of Thermus aquaticus DNA polymerase I during catalysis.

http://www.wikidata.org/entity/Q33940532

about

Structural basis for the D-stereoselectivity of human DNA polymerase β.Kinetic analysis of bypass of 7,8-dihydro-8-oxo-2'-deoxyguanosine by the catalytic core of yeast DNA polymerase η.

P2860

Q33741144-EA82A477-439E-4941-A891-3631C6B0D26A Q37540918-EB188ECD-0D3F-470F-8344-066E6BDB37CA

P2860

Conformational dynamics of Thermus aquaticus DNA polymerase I during catalysis.

http://www.wikidata.org/entity/Q33940532

description

2014 nî lūn-bûn

@nan

2014 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2014年の論文

@ja

2014年論文

@yue

2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

@wuu

name

Conformational dynamics of Thermus aquaticus DNA polymerase I during catalysis.

@ast

Conformational dynamics of Thermus aquaticus DNA polymerase I during catalysis.

@en

type

label

Conformational dynamics of Thermus aquaticus DNA polymerase I during catalysis.

@ast

Conformational dynamics of Thermus aquaticus DNA polymerase I during catalysis.

@en

prefLabel

Conformational dynamics of Thermus aquaticus DNA polymerase I during catalysis.

@ast

Conformational dynamics of Thermus aquaticus DNA polymerase I during catalysis.

@en

P1433

Q33940532-E612877F-C232-40D5-86EA-3967DA2E9FC1

P1476

Q33940532-FB099E56-5132-4996-AD28-73CB570A4E90

P2093

Q33940532-880586D2-F8F0-4949-A832-3C4A3501EA05

Q33940532-D2138126-2F4B-4A30-90C2-CF38498E87C0

P2860

Q33940532-0AA2D230-48B9-4782-81B9-4564CA3300A0

Q33940532-0C48E3FF-A7B6-4237-9B99-A5EBA8FC80CA

Q33940532-1097A3D7-AD24-435B-A4CB-AAA75665752E

Q33940532-1113F528-B920-487B-A476-864A7BB8F2E2

Q33940532-17C26D17-B3AC-4CC1-B2A6-5D906A487855

Q33940532-198C0395-ADD5-43AE-A341-9C854C72D9CA

Q33940532-1AEE62A1-7AC5-4C1A-AAA5-0EA039000002

Q33940532-2931858E-58B9-43E6-A5F9-E7EDDA1AC2D9

Q33940532-2D75080C-AA7E-48EA-9097-F5299E7A2C6A

Q33940532-2E83B863-2E28-4591-8015-79E131237797

P304

Q33940532-407A3FFB-33CA-49B5-9F67-9803DD664A98

P31

Q33940532-7F0F478B-31A3-4EB5-9F3C-6545E17EE71B

P356

Q33940532-7CB96659-FAFE-4350-901F-184C0868BDCA

P407

Q33940532-DADB5F89-ADBC-47A3-A430-9B191E50479C

P433

Q33940532-23C5FFE0-8BED-4403-8E59-676A6074C4E7

P478

Q33940532-0402CF3C-ADC1-4BEF-809C-B5A3FBC01E4F

P50

Q33940532-41E3F31F-1017-42F2-B40A-4E94EE5BA661

P577

Q33940532-A392FE92-6A0D-45B2-8493-AA653B0854FD

P5875

Q33940532-078BA07E-8D26-4186-A1C3-13FBE80B7F50

P698

Q33940532-9C52B95C-CBDD-4133-B171-BCC56063D952

P932

Q33940532-5D14324D-D566-4C05-9357-56196C17C1B9

P356

J.JMB.2014.06.003

P1433

Journal of Molecular Biology

P1476

Conformational dynamics of Thermus aquaticus DNA polymerase I during catalysis.

@en

P2093

Cuiling Xu

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

Zucai Suo

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

P2860

Coupled protein domain motion in Taq polymerase revealed by neutron spin-echo spectroscopy.

Structures of HIV-1 reverse transcriptase with pre- and post-translocation AZTMP-terminated DNA.

Processive DNA synthesis observed in a polymerase crystal suggests a mechanism for the prevention of frameshift mutations.

The structure of a high fidelity DNA polymerase bound to a mismatched nucleotide reveals an "ajar" intermediate conformation in the nucleotide selection mechanism.

Crystal structure of Thermus aquaticus DNA polymerase

Structure of Taq polymerase with DNA at the polymerase active site

Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 A resolution

Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: implications for drug resistance

Crystal structures of a ddATP-, ddTTP-, ddCTP, and ddGTP- trapped ternary complex of Klentaq1: insights into nucleotide incorporation and selectivity

Crystal structures of open and closed forms of binary and ternary complexes of the large fragment of Thermus aquaticus DNA polymerase I: structural basis for nucleotide incorporation.

P304

2901-2917

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

P31

scholarly article

P356

10.1016/J.JMB.2014.06.003

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

P407

P433

16

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

P478

426

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

P50

Brian A. Maxwell

P577

2014-06-12T00:00:00Z

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

P5875

263130861

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

P698

24931550

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

P932

4108498

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