Elafin is specifically inactivated by RgpB from Porphyromonas gingivalis by distinct proteolytic cleavage.
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Determinants of Affinity and Proteolytic Stability in Interactions of Kunitz Family Protease Inhibitors with MesotrypsinThe solution structure of the kallikrein-related peptidases inhibitor SPINK6Diagnostic evaluation of a nanobody with picomolar affinity toward the protease RgpB from Porphyromonas gingivalis.A novel matrix metalloprotease-like enzyme (karilysin) of the periodontal pathogen Tannerella forsythia ATCC 43037Dichotomy of gingipains action as virulence factors: from cleaving substrates with the precision of a surgeon's knife to a meat chopper-like brutal degradation of proteins.Adsorption of components of the plasma kinin-forming system on the surface of Porphyromonas gingivalis involves gingipains as the major docking platforms.Comparison of gingival crevicular fluid sampling methods in patients with severe chronic periodontitis.A functional variant of elafin with improved anti-inflammatory activity for pulmonary inflammation.Periodontal pathogens affect the level of protease inhibitors in gingival crevicular fluid.Protease inhibitor levels in periodontal health and disease.Functional study of elafin cleaved by Pseudomonas aeruginosa metalloproteinases.Cleavage of IgG1 in gingival crevicular fluid is associated with the presence of Porphyromonas gingivalisPeriodontal treatment downregulates protease-activated receptor 2 in human gingival crevicular fluid cells.Secretory leukocyte protease inhibitor and elafin/trappin-2: versatile mucosal antimicrobials and regulators of immunity.Antimicrobial peptides and periodontal disease.Gingipains from Porphyromonas gingivalis - Complex domain structures confer diverse functionsAlarm Anti-protease Trappin-2 Negatively Correlates With Proinflammatory Cytokines in Patients With Periodontitis.Gingipains of Porphyromonas gingivalis Affect the Stability and Function of Serine Protease Inhibitor of Kazal-type 6 (SPINK6), a Tissue Inhibitor of Human Kallikreins.Differential effects of periopathogens on host protease inhibitors SLPI, elafin, SCCA1, and SCCA2.
P2860
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P2860
Elafin is specifically inactivated by RgpB from Porphyromonas gingivalis by distinct proteolytic cleavage.
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
@pt
bilimsel makale
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scientific article published on December 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Elafin is specifically inactiv ...... distinct proteolytic cleavage.
@en
Elafin is specifically inactiv ...... distinct proteolytic cleavage.
@nl
type
label
Elafin is specifically inactiv ...... distinct proteolytic cleavage.
@en
Elafin is specifically inactiv ...... distinct proteolytic cleavage.
@nl
prefLabel
Elafin is specifically inactiv ...... distinct proteolytic cleavage.
@en
Elafin is specifically inactiv ...... distinct proteolytic cleavage.
@nl
P2093
P2860
P356
P1433
P1476
Elafin is specifically inactiv ...... distinct proteolytic cleavage.
@en
P2093
Jens-Michael Schröder
Joachim Bartels
Oliver Wiedow
Regine Gläser
Ties Latendorf
Tomasz Kantyka
Ulf Meyer-Hoffert
P2860
P304
P356
10.1515/BC.2009.136
P577
2009-12-01T00:00:00Z