Bacillus subtilis LrpC is a sequence-independent DNA-binding and DNA-bending protein which bridges DNA.
about
Role of LrpC from Bacillus subtilis in DNA transactions during DNA repair and recombination.Structural insight into gene transcriptional regulation and effector binding by the Lrp/AsnC family.Mechanistic insights from the crystal structures of a feast/famine regulatory protein from Mycobacterium tuberculosis H37RvCrystal structure of Mycobacterium tuberculosis LrpA, a leucine-responsive global regulator associated with starvation responseThe Arginine Pairs and C-Termini of the Sso7c4 from Sulfolobus solfataricus Participate in Binding and Bending DNAThe Sac10b homolog in Methanococcus maripaludis binds DNA at specific sitesIdentification, cloning and characterization of a new DNA-binding protein from the hyperthermophilic methanogen Methanopyrus kandleriGenome wide, supercoiling-dependent in vivo binding of a viral protein involved in DNA replication and transcriptional controlBinding of phage Phi29 architectural protein p6 to the viral genome: evidence for topological restriction of the phage linear DNA.Phage phi29 proteins p1 and p17 are required for efficient binding of architectural protein p6 to viral DNA in vivo.Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family transcriptional factors.Characterization of LrpC DNA-binding properties and regulation of Bacillus subtilis lrpC gene expressionPurification and characterization of Sa-lrp, a DNA-binding protein from the extreme thermoacidophilic archaeon Sulfolobus acidocaldarius homologous to the bacterial global transcriptional regulator Lrp.H-NS mediated compaction of DNA visualised by atomic force microscopy.Novel mechanism of gene regulation: the protein Rv1222 of Mycobacterium tuberculosis inhibits transcription by anchoring the RNA polymerase onto DNA.Acidic C-terminal domains autoregulate the RNA chaperone HfqConcentration-dependent organization of DNA by the dinoflagellate histone-like protein HCc3Characterization of DNA binding sites of the ComE response regulator from Streptococcus mutans.On the role of H-NS in the organization of bacterial chromatin: from bulk to single molecules and back.A novel member of the bacterial-archaeal regulator family is a nonspecific dna-binding protein and induces positive supercoiling.The Major Architects of Chromatin: Architectural Proteins in Bacteria, Archaea and Eukaryotes
P2860
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P2860
Bacillus subtilis LrpC is a sequence-independent DNA-binding and DNA-bending protein which bridges DNA.
description
2000 nî lūn-bûn
@nan
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
2000年论文
@zh
2000年论文
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name
Bacillus subtilis LrpC is a se ...... ing protein which bridges DNA.
@en
Bacillus subtilis LrpC is a se ...... ing protein which bridges DNA.
@nl
type
label
Bacillus subtilis LrpC is a se ...... ing protein which bridges DNA.
@en
Bacillus subtilis LrpC is a se ...... ing protein which bridges DNA.
@nl
prefLabel
Bacillus subtilis LrpC is a se ...... ing protein which bridges DNA.
@en
Bacillus subtilis LrpC is a se ...... ing protein which bridges DNA.
@nl
P2093
P2860
P356
P1476
Bacillus subtilis LrpC is a se ...... ing protein which bridges DNA.
@en
P2093
P2860
P304
P356
10.1093/NAR/28.2.552
P407
P577
2000-01-01T00:00:00Z