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ProteomicsC-terminal glycosylation of type IX secretion system cargo proteins in Prevotella intermedia bearing both short and long secretion signals
Prevotella intermedia is a Gram-negative bacterium that is notably linked to periodontitis and acute necrotizing ulcerative gingivitis. P. intermedia is known to utilise the T9SS to secrete and anchor virulence factors to the cell surface, presumably via C-terminal modification of the cargo protein ...
ORGANISM(S): Prevotella intermedia ATCC 25611 = DSM 20706 
2025-05-07 | PXD057272 | Pride
Glycosylation Secretion signal Surface proteins Prevotella intermedia Alaninamide Mass spectrometry Protein secretion 
UnknownThe RgpB C-terminal domain has a role in attachment of RgpB to the outer membrane and belongs to a novel C-terminal-domain family found in Porphyromonas gingivalis.
Not available
S-EPMC1595369 | biostudies-literature
UnknownCloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the regulatory domain of aspartokinase (Rv3709c) from Mycobacterium tuberculosis.
Not available
S-EPMC3053168 | biostudies-literature
UnknownC-terminal domain residues important for secretion and attachment of RgpB in Porphyromonas gingivalis.
Not available
S-EPMC3019955 | biostudies-literature
ProteomicsO-glycoproteome of Porphyromonas gingivalis
Porphyromonas gingivalis is an important human pathogen and also a model organism for the Bacteroidetes phylum. O-glycosylation has been reported in this phylum with findings that include the O-glycosylation motif, the structure of the O-glycans in a few species and an extensive O-glycoproteome anal...
ORGANISM(S): Porphyromonas gingivalis ATCC 33277 
2022-02-15 | PXD028120 | Pride
Porphyromonas gingivalis Glycan biosynthesis O-glycosylation Trifluoromethanesulfonic acid 
ProteomicsLocalisation of outer membrane proteins in Treponema denticola by quantitative proteome analyses of outer membrane vesicles and cellular fractions
The identification and localisation of outer membrane proteins (Omps) and lipoproteins in pathogenic treponemes such as T. denticola (periodontitis) and T. pallidum (syphilis) has been challenging largely due to the structural uniqueness of their outer membranes (OM), the high abundance of inner mem...
ORGANISM(S): Treponema denticola ATCC 35405 
2019-02-20 | PXD011495 | Pride
Treponema denticola Localization Outer membrane vesicles Bacterial lipoproteins Maxquant Outer membrane proteins Orbitrap 
TranscriptomicsA High-Fat Diet and NAD+ Rescue Premature Aging in Cockayne Syndrome
Cockayne syndrome (CS) is an accelerated aging disorder characterized by progressive neurodegeneration caused by mutations in the genes encoding the DNA repair proteins CSA or CSB. Csbm/m mice were given a high-fat, caloric-restricted or resveratrol-supplemented diet. The high-fat diet rescued the p...
ORGANISM(S): Mus musculus 
2014-12-22 | E-GEOD-62194 | biostudies-arrayexpress
ProteomicsO-glycoproteome of Tannerella forsythia
Tannerella forsythia is a Gram-negative oral pathogen known to possess an O-glycosylation system responsible for targeting multiple proteins associated with virulence at the three-residue motif (D)(S/T)(A/I/L/V/M/T). Multiple proteins have been identified to be decorated with a decasaccharide glycan...
ORGANISM(S): Tannerella forsythia 
2021-10-12 | PXD026989 | Pride
Tannerella forsythia O-glycosylation Trifluoromethanesulfonic acid 
ProteomicsGingipain transpeptidation - Porphyromonas gingivalis Gingipains Display Transpeptidation Activity
Porphyromonas gingivalis is a keystone periodontal pathogen that has been associated with autoimmune disorders. The cell surface proteases Lys-gingipain (Kgp) and Arg-gingipains (RgpA and RgpB) are major virulence factors and their proteolytic activity is enhanced by small peptides such as glycylgly...
ORGANISM(S): Homo sapiens (Human) 
2018-07-11 | PXD009950 | Pride
Transpeptidation Hemoglobin Gingipains Porphyromonas gingivalis 
UnknownThe C-terminal domain of p53 orchestrates the interplay between non-covalent and covalent poly(ADP-ribosyl)ation of p53 by PARP1.
Not available
S-EPMC5778597 | biostudies-literature
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