sameAs
Porphyromonas gingivalis facilitates the development and progression of destructive arthritis through its unique bacterial peptidylarginine deiminase (PAD)Arginine-specific protease from Porphyromonas gingivalis activates protease-activated receptors on human oral epithelial cells and induces interleukin-6 secretionAttenuated kinin release from human neutrophil elastase-pretreated kininogens by tissue and plasma kallikreinsSalivary histatin 5 is an inhibitor of both host and bacterial enzymes implicated in periodontal diseaseGingipain enzymes from Porphyromonas gingivalis preferentially bind immobilized extracellular proteins: a mechanism favouring colonization?Crystal structure of gingipain R: an Arg-specific bacterial cysteine proteinase with a caspase-like foldThe Staphostatin-staphopain complex: a forward binding inhibitor in complex with its target cysteine proteaseThree-dimensional structure of MecI. Molecular basis for transcriptional regulation of staphylococcal methicillin resistanceStaphostatins resemble lipocalins, not cystatins in foldA novel class of cysteine protease inhibitors: solution structure of staphostatin A from Staphylococcus aureusOn the transcriptional regulation of methicillin resistance: MecI repressor in complex with its operatorA New Autocatalytic Activation Mechanism for Cysteine Proteases Revealed by Prevotella intermedia Interpain AStructural and functional characterization of SplA, an exclusively specific protease of Staphylococcus aureusUnique Structure and Stability of HmuY, a Novel Heme-Binding Protein of Porphyromonas gingivalisThe structure of the catalytic domain of Tannerella forsythia karilysin reveals it is a bacterial xenologue of animal matrix metalloproteinasesPorphyromonas gingivalis Virulence Factor Gingipain RgpB Shows a Unique Zymogenic Mechanism for Cysteine PeptidasesStructure of the catalytic domain of theTannerella forsythiamatrix metallopeptidase karilysin in complex with a tetrapeptidic inhibitorBiochemical and structural characterization of SplD protease from Staphylococcus aureusDevelopment and binding characteristics of phosphonate inhibitors of SplA protease from Staphylococcus aureusStaphylococcal SplB Serine Protease Utilizes a Novel Molecular Mechanism of ActivationA Unique Mdm2-Binding Mode of the 3-Pyrrolin-2-one- and 2-Furanone-Based Antagonists of the p53-Mdm2 InteractionThe 1.8 A crystal structure of human cathepsin G in complex with Suc-Val-Pro-PheP-(OPh)2: a Janus-faced proteinase with two opposite specificitiesAmino-acid sequence and three-dimensional structure of the Staphylococcus aureus metalloproteinase at 1.72 A resolutionGingival fibromatosis: clinical, molecular and therapeutic issuesThe serpin superfamily of proteinase inhibitors: structure, function, and regulationInhibition of distant caspase homologues by natural caspase inhibitorsActivation of blood coagulation factor IX by gingipains R, arginine-specific cysteine proteinases from Porphyromonas gingivalisIdentification and characterization of sigma, a novel component of the Staphylococcus aureus stress and virulence responsesA phage display selected 7-mer peptide inhibitor of the Tannerella forsythia metalloprotease-like enzyme Karilysin can be truncated to Ser-Trp-Phe-ProThe nucleocapsid protein of human coronavirus NL63Pyocyanina contributory factor in haem acquisition and virulence enhancement of Porphyromonas gingivalis in the lung [corrected]Inhibition of CDK9 as a therapeutic strategy for inflammatory arthritis.The link between periodontal disease and rheumatoid arthritis: an updated review.Role of OmpA2 surface regions of Porphyromonas gingivalis in host-pathogen interactions with oral epithelial cells.A structure-derived snap-trap mechanism of a multispecific serpin from the dysbiotic human oral microbiome.Role of gingipains R in the pathogenesis of Porphyromonas gingivalis-mediated periodontal disease.Staphostatins: an expanding new group of proteinase inhibitors with a unique specificity for the regulation of staphopains, Staphylococcus spp. cysteine proteinases.Porphyromonas gingivalis DPP-7 represents a novel type of dipeptidylpeptidase.A peptide domain on gingipain R which confers immunity against Porphyromonas gingivalis infection in mice.Cartilage proteoglycan degradation by a mouse transformed macrophage cell line is mediated by macrophage metalloelastase.
P50
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P50
description
Polish biologist and researcher
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Pools bioloog
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biolog polonez
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biologiste polonais
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biologo polacco
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biólogo polaco
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biólogo polonès
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polnischer Biologe und Forscher
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polski biolog
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Jan Potempa
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Jan Potempa
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Jan Potempa
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Jan Potempa
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Jan Potempa
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Jan Potempa
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Jan Potempa
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Jan Potempa
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Jan Potempa
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Jan Potempa
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Jan Potempa
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Jan Potempa
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Jan Potempa
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Jan Potempa
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Jan Potempa
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Jan Potempa
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Jan Potempa
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Jan Potempa
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Jan Potempa
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J Potempa
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J Potempa
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J Potempa
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Jan S. Potempa
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Jan Stanislaw Potempa
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Jan Stanisław Potempa
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Potempa J
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Potempa J
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Potempa J
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prefLabel
Jan Potempa
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Jan Potempa
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Jan Potempa
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Jan Potempa
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Jan Potempa
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Jan Potempa
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Jan Potempa
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Jan Potempa
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Jan Potempa
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P2038
Jan_Potempa
P21
P213
0000 0001 1606 7670
P214
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P27
P2798
P31
P3124
P496
0000-0002-3600-7461