Structure and function of repetitive sequence elements associated with a highly polymorphic domain of the Neisseria meningitidis PilQ protein.
about
Diversity in coding tandem repeats in related Neisseria sppStructure of the cytoplasmic domain of TcpE, the inner membrane core protein required for assembly of the Vibrio cholerae toxin-coregulated pilusBiofilm formation by Neisseria meningitidis.Resistance of neisseria meningitidis to the toxic effects of heme iron and other hydrophobic agents requires expression of ght.Comparative proteomic analysis of Neisseria meningitidis wildtype and dprA null mutant strains links DNA processing to pilus biogenesis.Structural characterization of outer membrane components of the type IV pili system in pathogenic Neisseria.The outer membrane secretin PilQ from Neisseria meningitidis binds DNA.NafA negatively controls Neisseria meningitidis piliation.Analysis of the PilQ secretin from Neisseria meningitidis by transmission electron microscopy reveals a dodecameric quaternary structure.Development and evaluation of an improved mouse model of meningococcal colonization.Three-dimensional structure of the Neisseria meningitidis secretin PilQ determined from negative-stain transmission electron microscopy.Characterization of DsbD in Neisseria meningitidis.Ehrlichia chaffeensis TRP120 binds a G+C-rich motif in host cell DNA and exhibits eukaryotic transcriptional activator function.The Inner Membrane Protein PilG Interacts with DNA and the Secretin PilQ in Transformation.Loss of meningococcal PilU delays microcolony formation and attenuates virulence in vivoCharacterization of the Neisseria meningitidis Helicase RecG.Meningococcal genome dynamics.Type IV pili in Gram-positive bacteria.Functional and structural characteristics of bacterial proteins that bind host cytokines.pilQ Missense mutations have diverse effects on PilQ multimer formation, piliation, and pilus function in Neisseria gonorrhoeae.Components and dynamics of fiber formation define a ubiquitous biogenesis pathway for bacterial pili.Simple sequence repeats in Escherichia coli: abundance, distribution, composition, and polymorphismPhylogeny and strain typing of Escherichia coli, inferred from variation at mononucleotide repeat loci.Identification of neisserial DNA binding components.Interactions between the lipoprotein PilP and the secretin PilQ in Neisseria meningitidis.Structure-function relationships of the competence lipoprotein ComL and SSB in meningococcal transformation.New functional identity for the DNA uptake sequence in transformation and its presence in transcriptional terminatorsThe helicase DinG responds to stress due to DNA double strand breaks.
P2860
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P2860
Structure and function of repetitive sequence elements associated with a highly polymorphic domain of the Neisseria meningitidis PilQ protein.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
1998年學術文章
@zh-hant
name
Structure and function of repe ...... ria meningitidis PilQ protein.
@en
Structure and function of repe ...... ria meningitidis PilQ protein.
@nl
type
label
Structure and function of repe ...... ria meningitidis PilQ protein.
@en
Structure and function of repe ...... ria meningitidis PilQ protein.
@nl
prefLabel
Structure and function of repe ...... ria meningitidis PilQ protein.
@en
Structure and function of repe ...... ria meningitidis PilQ protein.
@nl
P2093
P2860
P1476
Structure and function of repe ...... ria meningitidis PilQ protein.
@en
P2093
P2860
P304
P356
10.1046/J.1365-2958.1998.00910.X
P407
P577
1998-07-01T00:00:00Z