A novel "clip-and-link" activity of repeat in toxin (RTX) proteins from gram-negative pathogens. Covalent protein cross-linking by an Asp-Lys isopeptide bond upon calcium-dependent processing at an Asp-Pro bond.
about
RTX proteins: a highly diverse family secreted by a common mechanismConnecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxinCharacterization of member of DUF1888 protein family, self-cleaving and self-assembling endopeptidase.An unusual mechanism of isopeptide bond formation attaches the collagenlike glycoprotein BclA to the exosporium of Bacillus anthracis.Probing of Actinobacillus pleuropneumoniae ApxIIIA toxin-dependent cytotoxicity towards mammalian peripheral blood mononucleated cellsRegulation of the type I protein secretion system by the MisR/MisS two-component system in Neisseria meningitidis.Unusual genetic organization of a functional type I protein secretion system in Neisseria meningitidis.MARTX, multifunctional autoprocessing repeats-in-toxin toxins.Single-step affinity purification of recombinant proteins using a self-excising module from Neisseria meningitidis FrpC.Self-cleaving fusion tags for recombinant protein production.Biological Functions of the Secretome of Neisseria meningitidisPorcine CD18 mediates Actinobacillus pleuropneumoniae ApxIII species-specific toxicity.Cleavage in the GDPH sequence of the C-terminal cysteine-rich part of the human MUC5AC mucin.NMR assignment of intrinsically disordered self-processing module of the FrpC protein of Neisseria meningitidis.Characterization of the self-cleaving effector protein NopE1 of Bradyrhizobium japonicum.Crystallization and preliminary crystallographic characterization of the iron-regulated outer membrane lipoprotein FrpD from Neisseria meningitidis.Structural basis of the interaction between the putative adhesion-involved and iron-regulated FrpD and FrpC proteins of Neisseria meningitidis.Intrinsically disordered proteins drive enamel formation via an evolutionarily conserved self-assembly motifIdentification and analysis of four candidate symbiosis genes from 'Chlorochromatium aggregatum', a highly developed bacterial symbiosis.A bacterial RTX toxin causes programmed necrotic cell death through calcium-mediated mitochondrial dysfunction.The Neisseria meningitidis outer membrane lipoprotein FrpD binds the RTX protein FrpC.Probing the Ca(2+)-assisted π-π interaction during Ca(2+)-dependent protein folding.
P2860
Q24630254-2CC24782-4C6B-4A47-92AC-797447F71F3DQ24653785-8E2567CA-6AC7-4399-A8BB-ED39B4279B2EQ27678442-8D5DF78E-DDB2-4402-824B-0F5D130ED108Q30403296-5BDA8815-44DA-45D1-8434-670E24016F05Q33388553-00A87F96-E5E7-4C01-B5F6-928834CF6055Q33928835-3EEB89A7-7B7A-4CF0-9D67-7C8B422C89E2Q34034177-4BEEAF69-5BBF-4D84-B498-5328CDDE185FQ36313852-3AAC2723-232B-4073-8C26-13C9D0DADC86Q36901603-7ABE95C3-589E-4C05-A211-5B8B8BB7BE87Q37832436-34DC223A-0D7A-4CE1-8AA5-3918444BF346Q39410503-D7ADAFED-57FF-47B9-BE3C-8562ECB825A3Q39862744-DF2B3ED2-1EEB-4549-A1A1-D25FB6C97A71Q40265025-3B80C48F-0F92-43BB-8797-0D132810B1B3Q41126092-3085BFC5-56D3-4476-B9CD-65C340425C63Q42116577-8A08D407-ACEE-4FE6-8EE5-5AD2C5FF97BCQ42124015-ABE9DF65-E68B-4E02-B735-3B45AA96C741Q42132567-631C41B3-3DD0-4479-BF3F-9515F1135175Q42318119-3718C219-820C-4932-9AB5-0EF312DFB394Q42594731-FEE3E5DE-1FEA-4E29-98D2-E14E737079C2Q43017226-C16F3DC0-BFE3-4048-8A87-B2CC7C8E37D9Q45138614-A595E8D2-B293-4C15-963A-E99EEA933CD0Q47830418-4FFBACD1-916D-4BDE-8B59-A5BB6FA8BFC2
P2860
A novel "clip-and-link" activity of repeat in toxin (RTX) proteins from gram-negative pathogens. Covalent protein cross-linking by an Asp-Lys isopeptide bond upon calcium-dependent processing at an Asp-Pro bond.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
2004年學術文章
@zh-hant
name
A novel "clip-and-link" activi ...... processing at an Asp-Pro bond.
@en
A novel "clip-and-link" activity of repeat in toxin
@nl
type
label
A novel "clip-and-link" activi ...... processing at an Asp-Pro bond.
@en
A novel "clip-and-link" activity of repeat in toxin
@nl
prefLabel
A novel "clip-and-link" activi ...... processing at an Asp-Pro bond.
@en
A novel "clip-and-link" activity of repeat in toxin
@nl
P2860
P50
P356
P1476
A novel "clip-and-link" activi ...... processing at an Asp-Pro bond.
@en
P2093
Irena Linhartová
Katerina Procházková
P2860
P304
24944-24956
P356
10.1074/JBC.M314013200
P407
P577
2004-03-24T00:00:00Z