Watching DNA polymerase η make a phosphodiester bond - Wikidata - wikimedia - TriplyDB

Watching DNA polymerase η make a phosphodiester bond

Watching DNA polymerase η make a phosphodiester bond

http://www.wikidata.org/entity/Q27670704

about

dUTPase: the frequently overlooked enzyme encoded by many retroviruses Structure-function studies of DNA polymerase λ Mechanism of the nucleotidyl-transfer reaction in DNA polymerase revealed by time-resolved protein crystallography A new paradigm of DNA synthesis: three-metal-ion catalysis.Molecular events during translocation and proofreading extracted from 200 static structures of DNA polymerase.Structures of dNTP Intermediate States during DNA Polymerase Active Site Assembly Differential Furanose Selection in the Active Sites of Archaeal DNA Polymerases Probed by Fixed-Conformation Nucleotide Analogues Watching the Bacteriophage N4 RNA Polymerase Transcription by Time-dependent Soak-trigger-freeze X-ray Crystallography Structures of DNA duplexes containing O6-carboxymethylguanine, a lesion associated with gastrointestinal cancer, reveal a mechanism for inducing pyrimidine transition mutations Mechanism of somatic hypermutation at the WA motif by human DNA polymerase η.Amino Acid Substitution in the Active Site of DNA Polymerase β Explains the Energy Barrier of the Nucleotidyl Transfer Reaction A conformational switch in PRP8 mediates metal ion coordination that promotes pre-mRNA exon ligation Observing a DNA Polymerase Choose Right from Wrong The E295K Cancer Variant of Human Polymerase Favors the Mismatch Conformational Pathway during Nucleotide Selection Aprataxin resolves adenylated RNA–DNA junctions to maintain genome integrity Metal-Dependent Conformational Activation Explains Highly Promutagenic Replication across O6-Methylguanine by Human DNA Polymerase β Kinetics, Structure, and Mechanism of 8-Oxo-7,8-dihydro-2'-deoxyguanosine Bypass by Human DNA Polymerase Structural and mechanistic studies of polymerase bypass of phenanthriplatin DNA damage Structural basis for processive DNA synthesis by yeast DNA polymerase ɛ Visualizing phosphodiester-bond hydrolysis by an endonuclease Capture of a third Mg²⁺ is essential for catalyzing DNA synthesis Structure and mechanism of DNA polymerase β An overview of Y-Family DNA polymerases and a case study of human DNA polymerase η Structural basis of viral RNA-dependent RNA polymerase catalysis and translocation The social fabric of the RNA degradosome Resolution of structural heterogeneity in dynamic crystallography.Catalytic mechanism of α-phosphate attack in dUTPase is revealed by X-ray crystallographic snapshots of distinct intermediates, 31P-NMR spectroscopy and reaction path modelling.Revealing the role of the product metal in DNA polymerase β catalysis.Structural comparison of DNA polymerase architecture suggests a nucleotide gateway to the polymerase active site.RB69 DNA polymerase structure, kinetics, and fidelity.Fluorescence resonance energy transfer studies of DNA polymerase β: the critical role of fingers domain movements and a novel non-covalent step during nucleotide selection.Quantum mechanical analysis of nonenzymatic nucleotidyl transfer reactions: kinetic and thermodynamic effects of β-γ bridging groups of dNTP substrates Phosphate steering by Flap Endonuclease 1 promotes 5'-flap specificity and incision to prevent genome instability.Capturing a mammalian DNA polymerase extending from an oxidized nucleotide.Structural and dynamic characterization of polymerase κ's minor groove lesion processing reveals how adduct topology impacts fidelity.Structure and function of TatD exonuclease in DNA repair.Calcium inhibition of ribonuclease H1 two-metal ion catalysis "Gate-keeper" residues and active-site rearrangements in DNA polymerase μ help discriminate non-cognate nucleotides.Parametrization of DFTB3/3OB for magnesium and zinc for chemical and biological applications Uncovering the polymerase-induced cytotoxicity of an oxidized nucleotide

P2860

Q26799724-D15FF269-CA37-4D25-B196-A7AEA1879DFB Q26849468-B83DE022-114A-4361-8A2B-080C9CF42215 Q27008294-08008679-B247-41C2-BE89-52475A4F3637 Q27320851-1A637501-B898-4869-96B5-66C76183882C Q27323040-2A2EE105-25D7-4BA3-B81E-16C8DAFBF75A Q27672742-7326B098-DDC3-49BC-AB28-CDCF6919DACD Q27674391-0CA24398-DA05-4773-A595-D9C91FBE405A Q27675455-7586EDEF-BE71-4679-B06F-3E5192DF1A89 Q27677331-26FD5F65-40E1-4FCE-B148-000E9E784880 Q27677864-6BB3D32D-29CD-40F2-AA42-C4ED31491A51 Q27678004-5A75B228-D0AD-445D-B7C3-753D3AFD3C5A Q27678185-03846F23-4757-4D76-9106-F8890649459B Q27678932-DE200678-2AFC-4247-813D-2F547D909D23 Q27680388-94E6438A-714F-42AC-B362-72CB5C70988C Q27681030-D483DC79-DA8C-4EE2-A87F-34EC8D6C81A6 Q27682793-B59EFE1B-DA40-4DA5-B589-9FD08B98B023 Q27683529-51EC091F-35B3-406B-B09D-DC05E9256848 Q27684330-D65EB151-2224-427A-8979-79C81B20D09A Q27687755-7B84E799-B0E5-43F0-A165-72CF80F08BBE Q27696542-1226A4D7-EC14-4CA3-8958-64868DD36246 Q27709553-3BCEFFDA-4189-4A4A-8B33-8D77EA1DC7BA Q28237870-05DF8899-7936-4D5C-BD0D-0B986AA5E0E7 Q28657572-C61444A0-879B-47FB-BB94-E80B2098E819 Q28829956-AE72496E-76FE-4312-8335-D04F4A9F2EA3 Q28972220-16EE0E98-8132-43C5-A149-AC6FBBD4DCAA Q30540047-18DE86ED-4BA5-4A97-9EC0-49303719941F Q30569983-A373BBDF-8D20-4099-AB43-A963D92B4F9E Q33557324-227FC531-A169-4C08-B5E2-6AB0A55ED454 Q33597718-A3F40084-A4E9-4EF6-95E2-2C5329DE3B03 Q33598642-20F7C5ED-8AB1-4C08-8334-765ED554A9B0 Q33718587-D1E475FD-F3A2-45FB-928A-12BF407F0CCD Q33843012-953A87ED-BDB9-48F8-8FA2-DDD53378EFE8 Q33851243-E79E6FC0-6C1C-48E1-BB95-1EB8D681CF85 Q33878893-A32DAABD-7B23-4C27-8E89-B26D96E078AE Q34155628-2D8F43C2-0C65-4FD7-86D4-FC21086B7F57 Q34249556-CF45893A-C4AB-473B-AE94-E7291F10C4A7 Q34402463-F7E9D4FD-D488-4FCB-A133-DCE0AEBA9296 Q34743729-57667BD4-07C6-4E73-BB27-F4266D9CBF71 Q35013411-4D0638D5-0AEB-4C75-908B-B910607CA637 Q35032502-26917DAE-EA81-4439-8815-C2DA5F37C92B

P2860

Watching DNA polymerase η make a phosphodiester bond

http://www.wikidata.org/entity/Q27670704

description

2012 nî lūn-bûn

@nan

2012 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

2012年の論文

@ja

2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

name

Watching DNA polymerase η make a phosphodiester bond

@ast

Watching DNA polymerase η make a phosphodiester bond

@en

Watching DNA polymerase η make a phosphodiester bond

@nl

type

label

Watching DNA polymerase η make a phosphodiester bond

@ast

Watching DNA polymerase η make a phosphodiester bond

@en

Watching DNA polymerase η make a phosphodiester bond

@nl

prefLabel

Watching DNA polymerase η make a phosphodiester bond

@ast

Watching DNA polymerase η make a phosphodiester bond

@en

Watching DNA polymerase η make a phosphodiester bond

@nl

P1433

Q27670704-D8C5E7B5-F850-4275-942A-A808176A26AC

P1476

Q27670704-38935107-3571-4632-9BB8-778F3F668179

P2093

Q27670704-1FD95D9C-E633-4D77-91D5-3C8015C47EF9

Q27670704-4785AB09-7355-4342-A7A3-67EC02083D62

Q27670704-D1E43F04-DB2B-4F43-B7C1-3D81425B9C98

Q27670704-D4154E72-B766-4BF0-B57F-EAA2EF79203F

P2860

Q27670704-06C4000A-66EA-4654-8423-788084C5D6E2

Q27670704-0EBC295A-5E09-416E-9D81-6A0091A5CCCB

Q27670704-125783D6-B4DC-4085-8FFF-C74CE9CA5F54

Q27670704-1988408F-077C-4BCC-9041-4472FA5A07ED

Q27670704-1BDA1F94-323E-466A-9451-866D60F6B0FC

Q27670704-1D3C6BE2-895D-4AE2-BB6C-E7B2FAA8193D

Q27670704-3198DCFF-D60A-4C37-B91A-D105681D6F6D

Q27670704-3A0612C5-B3EF-4A5B-A01E-4F3C976D3A24

Q27670704-3C4DDAC0-D932-444A-AB5E-3EA9A0274740

Q27670704-3E0E2439-63B3-4B2A-BB09-EC5F7E592397

P2888

Q27670704-6185C39D-B06D-402D-B0D9-797A37E25D62

P304

Q27670704-B0668173-4601-45E6-B67E-76197262F536

P31

Q27670704-387DD4BF-A8F4-49C1-AB56-553C3AF2D86F

P3181

Q27670704-9B3BA09F-5378-4D2E-AB7D-C92910F44253

P356

Q27670704-2B5E45D0-C695-4D8D-9D8B-E36A9A74922D

P407

Q27670704-176E8B04-C5C5-42DE-9591-802A4F995B75

P433

Q27670704-380E002B-92C6-41F0-BE5C-ECED88026F06

P478

Q27670704-9C593B95-792D-4B92-9C59-579B220A376A

P50

Q27670704-BC4A7192-656A-43D5-8A7A-DE7AB9107B15

P577

Q27670704-D75294B2-DC84-4D6A-B137-BCFAC5EB7C41

P5875

Q27670704-21C1C41B-E187-4170-A9F4-35859E3F9F71

P6179

Q27670704-68759DF2-04E3-4F1B-A93E-28A54A5D209E

P698

Q27670704-D531C78D-DBB7-46D8-8E9D-2A33F42B8CF6

P932

Q27670704-4F530769-A7FF-4BA7-B6A6-796D43137DB3

P3181

P356

P1433

P1476

Watching DNA polymerase η make a phosphodiester bond

@en

P2093

Teruya Nakamura

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

Wei Yang

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

Yue-jin Hua

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

Yuriko Yamagata

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

P2860

MgF(3)(-) as a transition state analog of phosphoryl transfer

A general two-metal-ion mechanism for catalytic RNA

PHENIX: a comprehensive Python-based system for macromolecular structure solution

Structures of phi29 DNA polymerase complexed with substrate: the mechanism of translocation in B-family polymerases.

Processing of X-ray diffraction data collected in oscillation mode

Capture and visualization of a catalytic RNA enzyme-product complex using crystal lattice trapping and X-ray holographic reconstruction

Structure of the replicating complex of a pol alpha family DNA polymerase

Crystal structure of a Y-family DNA polymerase in action: a mechanism for error-prone and lesion-bypass replication

Artificial evolution of an enzyme active site: structural studies of three highly active mutants of Escherichia coli alkaline phosphatase

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

P2888

P304

196-201

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

P31

scholarly article

P3181

2415655

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

P356

10.1038/NATURE11181

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

P407

P433

7406

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

P478

487

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

P50

P577

2012-07-11T00:00:00Z

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

P5875

229074503

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

P6179

1006554199

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

P698

22785315

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

P932

3397672

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