Mechanisms by Which Human DNA Primase Chooses To Polymerize a Nucleoside Triphosphate

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F10%3A00342344" target="_blank" >RIV/61388963:_____/10:00342344 - isvavai.cz</a>

Result on the web

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DOI - Digital Object Identifier

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Result language

angličtina

Original language name

Mechanisms by Which Human DNA Primase Chooses To Polymerize a Nucleoside Triphosphate

Original language description

We used an extensive series of purine and pyrimidine nucleotide analogues to provide further insights into the mechanism by which primase chooses whether or not to polymerize a NTP. The data demonstrate that human primase strongly depends on Watson-Crickhydrogen bonds for efficient nucleotide polymerization.

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

CC - Organic chemistry

OECD FORD branch

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Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year

2010

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Biochemistry

ISSN

0006-2960

e-ISSN

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Volume of the periodical

49

Issue of the periodical within the volume

4

Country of publishing house

US - UNITED STATES

Number of pages

9

Pages from-to

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UT code for WoS article

000273831500009

EID of the result in the Scopus database

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