Regulation of Escherichia coli SOS mutagenesis by dimeric intrinsically disordered umuD gene products.
about
Fuzziness: linking regulation to protein dynamicsCaught in self-interaction: evolutionary and functional mechanisms of protein homooligomerizationFuzzy complexes: Specific binding without complete foldingThe Dimerization State of the Mammalian High Mobility Group Protein AT-Hook 2 (HMGA2)Conformational dynamics of the Escherichia coli DNA polymerase manager proteins UmuD and UmuD'.Intrinsic disorder in protein interactions: insights from a comprehensive structural analysisUmuD(2) inhibits a non-covalent step during DinB-mediated template slippage on homopolymeric nucleotide runs.The unusual UBZ domain of Saccharomyces cerevisiae polymerase ηThe dimeric SOS mutagenesis protein UmuD is active as a monomerEvolutionary, physicochemical, and functional mechanisms of protein homooligomerization.The intrinsically disordered cytoplasmic domain of the T cell receptor zeta chain binds to the nef protein of simian immunodeficiency virus without a disorder-to-order transition.Selective disruption of the DNA polymerase III α-β complex by the umuD gene products.The Acinetobacter regulatory UmuDAb protein cleaves in response to DNA damage with chimeric LexA/UmuD characteristics.In vivo protein complex topologies: sights through a cross-linking lensPolymerase manager protein UmuD directly regulates Escherichia coli DNA polymerase III α binding to ssDNA.Characterization of novel alleles of the Escherichia coli umuDC genes identifies additional interaction sites of UmuC with the beta clamp.Protein intrinsic disorder and oligomericity in cell signaling.The SCHOOL of nature: II. Protein order, disorder and oligomericity in transmembrane signaling.Unusual biophysics of immune signaling-related intrinsically disordered proteins.Direct interaction of otoferlin with syntaxin 1A, SNAP-25, and the L-type voltage-gated calcium channel Cav1.3.The Roles of UmuD in Regulating Mutagenesis.The intrinsically disordered RNR inhibitor Sml1 is a dynamic dimer.Electron spin labeling reveals the highly dynamic N-terminal arms of the SOS mutagenesis protein UmuD.Phosphorylation of human small heat shock protein HspB8 (Hsp22) by ERK1 protein kinase.
P2860
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P2860
Regulation of Escherichia coli SOS mutagenesis by dimeric intrinsically disordered umuD gene products.
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2008 nî lūn-bûn
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2008年の論文
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2008年学术文章
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2008年学术文章
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name
Regulation of Escherichia coli ...... disordered umuD gene products.
@ast
Regulation of Escherichia coli ...... disordered umuD gene products.
@en
type
label
Regulation of Escherichia coli ...... disordered umuD gene products.
@ast
Regulation of Escherichia coli ...... disordered umuD gene products.
@en
prefLabel
Regulation of Escherichia coli ...... disordered umuD gene products.
@ast
Regulation of Escherichia coli ...... disordered umuD gene products.
@en
P2093
P2860
P356
P1476
Regulation of Escherichia coli ...... disordered umuD gene products
@en
P2093
F J R Sousa
R Mohana-Borges
P2860
P304
P356
10.1073/PNAS.0706067105
P407
P50
P577
2008-01-23T00:00:00Z