The Tla protein of Porphyromonas gingivalis W50: a homolog of the RI protease precursor (PrpRI) is an outer membrane receptor required for growth on low levels of hemin (Q35626963)

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scientific article published on August 1997

Language	Label	Description	Also known as
English	The Tla protein of Porphyromonas gingivalis W50: a homolog of the RI protease precursor (PrpRI) is an outer membrane receptor required for growth on low levels of hemin	scientific article published on August 1997

Statements

scholarly article

1 reference

Europe PubMed Central

9 August 2017

The Tla protein of Porphyromonas gingivalis W50: a homolog of the RI protease precursor (PrpRI) is an outer membrane receptor required for growth on low levels of hemin (English)

1 reference

Europe PubMed Central

9 August 2017

Porphyromonas gingivalis

0 references

author name string

Aduse-Opoku J

1

1 reference

Europe PubMed Central

9 August 2017

Slaney JM

2

1 reference

Europe PubMed Central

9 August 2017

Rangarajan M

3

1 reference

Europe PubMed Central

9 August 2017

Muir J

4

1 reference

Europe PubMed Central

9 August 2017

Young KA

5

1 reference

Europe PubMed Central

9 August 2017

Curtis MA

6

1 reference

Europe PubMed Central

9 August 2017

language of work or name

0 references

publication date

1 August 1997

1 reference

Europe PubMed Central

9 August 2017

Journal of Bacteriology

1 reference

Europe PubMed Central

9 August 2017

179

1 reference

Europe PubMed Central

9 August 2017

4778-4788

1 reference

Europe PubMed Central

9 August 2017

15

1 reference

Europe PubMed Central

9 August 2017

Biochemical characterization of the arginine-specific proteases of Porphyromonas gingivalis W50 suggests a common precursor

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=179324

12 July 2018

The prpR1 and prR2 arginine-specific protease genes of Porphyromonas gingivalis W50 produce five biochemically distinct enzymes.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=179324

12 July 2018

The hemagglutinin gene A (hagA) of Porphyromonas gingivalis 381 contains four large, contiguous, direct repeats.

1 reference

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12 July 2018

Cloning and sequencing of the gene encoding a novel lysine-specific cysteine proteinase (Lys-gingipain) in Porphyromonas gingivalis: structural relationship with the arginine-specific cysteine proteinase (Arg-gingipain).

1 reference

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Characterization of an adherence and antigenic determinant of the ArgI protease of Porphyromonas gingivalis which is present on multiple gene products.

1 reference

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Characterization of the binding activities of proteinase-adhesin complexes from Porphyromonas gingivalis

1 reference

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Analysis of the prtP gene encoding porphypain, a cysteine proteinase of Porphyromonas gingivalis

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Molecular cloning of a member of the gene family that encodes pMGA, a hemagglutinin of Mycoplasma gallisepticum

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The structure and function of proline-rich regions in proteins

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Lysine- and arginine-specific proteinases from Porphyromonas gingivalis. Isolation, characterization, and evidence for the existence of complexes with hemagglutinins

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A functional tonB gene is required for both utilization of heme and virulence expression by Haemophilus influenzae type b

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Purification and characterization of a novel arginine-specific cysteine proteinase (argingipain) involved in the pathogenesis of periodontal disease from the culture supernatant of Porphyromonas gingivalis.

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Characterisation of IS1126 from Porphyromonas gingivalis W83: a new member of the IS4 family of insertion sequence elements

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Virulence of a Porphyromonas gingivalis W83 mutant defective in the prtH gene

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The multiple forms of trypsin-like activity present in various strains of Porphyromonas gingivalis are due to the presence of either Arg-gingipain or Lys-gingipain

1 reference

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Structural characterization of argingipain, a novel arginine-specific cysteine proteinase as a major periodontal pathogenic factor from Porphyromonas gingivalis.

1 reference

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Complete nucleotide sequence of a gene prtR of Porphyromonas gingivalis W50 encoding a 132 kDa protein that contains an arginine-specific thiol endopeptidase domain and a haemagglutinin domain.

1 reference

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12 July 2018

Molecular cloning and structural characterization of the Arg-gingipain proteinase of Porphyromonas gingivalis. Biosynthesis as a proteinase-adhesin polyprotein

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Signal peptides: exquisitely designed transport promoters

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Signal transfer through three compartments: transcription initiation of the Escherichia coli ferric citrate transport system from the cell surface

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Characterization, genetic analysis, and expression of a protease antigen (PrpRI) of Porphyromonas gingivalis W50

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Effect of hemin on the physiology and virulence of Bacteroides gingivalis W50.

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Hemin levels in culture medium of Porphyromonas (Bacteroides) gingivalis regulate both hemin binding and trypsinlike protease production.

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based on heuristic

inferred from PubMed ID database lookup

Iron-regulated outer membrane proteins in the periodontopathic bacterium, Bacteroides gingivalis

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https://pubmed.ncbi.nlm.nih.gov/9244265

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based on heuristic

inferred from PubMed ID database lookup

Purification and characterization of a potent 70-kDa thiol lysyl-proteinase (Lys-gingivain) from Porphyromonas gingivalis that cleaves kininogens and fibrinogen

1 reference

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based on heuristic

inferred from PubMed ID database lookup

Production and characterisation of monoclonal antibodies to the principle sonicate antigens of Porphyromonas gingivalis w50

1 reference

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based on heuristic

inferred from PubMed ID database lookup

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1 reference

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based on heuristic

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1 reference

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based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1128/JB.179.15.4778-4788.1997

1 reference

Europe PubMed Central

9 August 2017

1 reference

Europe PubMed Central

9 August 2017

1 reference

Europe PubMed Central

9 August 2017

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