about
A Decade of Biochemical and Structural Studies of the DNA Repair Machinery of Deinococcus radiodurans: Major Findings, Functional and Mechanistic Insight and ChallengesAnalysis of Deinococcus radiodurans's transcriptional response to ionizing radiation and desiccation reveals novel proteins that contribute to extreme radioresistanceThe IrrE protein of Deinococcus radiodurans R1 is a novel regulator of recA expressionExpression, purification, crystallization and preliminary X-ray crystallographic studies of Deinococcus radiodurans thioredoxin reductasePurification, crystallization and preliminary crystallographic investigation of FrnE, a disulfide oxidoreductase from Deinococcus radiodurans.Dr-FtsA, an actin homologue in Deinococcus radiodurans differentially affects Dr-FtsZ and Ec-FtsZ functions in vitroCharacteristics of dr1790 disruptant and its functional analysis in Deinococcus radiodurans.DNA toroids: framework for DNA repair in Deinococcus radiodurans and in germinating bacterial spores.The protein PprI provides protection against radiation injury in human and mouse cells.Ring-like nucleoids and DNA repair through error-free nonhomologous end joining in Deinococcus radiodurans.Involvement of a protein kinase activity inducer in DNA double strand break repair and radioresistance of Deinococcus radiodurans.FrnE, a cadmium-inducible protein in Deinococcus radiodurans, is characterized as a disulfide isomerase chaperone in vitro and for its role in oxidative stress tolerance in vivo.PprA contributes to Deinococcus radiodurans resistance to nalidixic acid, genome maintenance after DNA damage and interacts with deinococcal topoisomerases.DR1769, a protein with N-terminal beta propeller repeats and a low-complexity hydrophilic tail, plays a role in desiccation tolerance of Deinococcus radiodurans.ATP-type DNA ligase requires other proteins for its activity in vitro and its operon components for radiation resistance in Deinococcus radiodurans in vivo.Characterization of an ATP-regulated DNA-processing enzyme and thermotolerant phosphoesterase in the radioresistant bacterium Deinococcus radiodurans.ParA encoded on chromosome II of Deinococcus radiodurans binds to nucleoid and inhibits cell division in Escherichia coli.Pyrroloquinoline quinone and a quinoprotein kinase support γ-radiation resistance in Deinococcus radiodurans and regulate gene expression.Identification of a DNA processing complex from Deinococcus radiodurans.Involvement of a periplasmic protein kinase in DNA strand break repair and homologous recombination in Escherichia coli.
P2860
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P2860
description
2000 nî lūn-bûn
@nan
2000 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի մարտին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Radiation resistance: the fragments that remain.
@ast
Radiation resistance: the fragments that remain.
@en
type
label
Radiation resistance: the fragments that remain.
@ast
Radiation resistance: the fragments that remain.
@en
prefLabel
Radiation resistance: the fragments that remain.
@ast
Radiation resistance: the fragments that remain.
@en
P1433
P1476
Radiation resistance: the fragments that remain.
@en
P2093
Battista JR
P304
P356
10.1016/S0960-9822(00)00353-5
P407
P577
2000-03-01T00:00:00Z