Search Results - "Banbula, Agnieszka"

Role of bacterial proteinases in matrix destruction and modulation of host responses by POTEMPA, JAN, BANBULA, AGNIESZKA, TRAVIS, JIM

“…Recently accumulated large bodies of evidence have strongly implicated proteolytic enzymes released by subgingival plaque bacteria in the pathogenicity of…”
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Activation of Human Prothrombin by Arginine-specific Cysteine Proteinases (Gingipains R) from Porphyromonas gingivalis by Imamura, Takahisa, Banbula, Agnieszka, Pereira, Pedro J.B., Travis, James, Potempa, Jan

“…The effect of 95- (HRgpA) and 50-kDa gingipain R (RgpB), arginine-specific cysteine proteinases from periodontopathogenic bacterium Porphyromonas gingivalis on…”
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Rapid and Efficient Inactivation of IL-6 Gingipains, Lysine- and Arginine-Specific Proteinases from Porphyromonas Gingivalis by Banbula, Agnieszka, Bugno, Marcin, Kuster, Andrea, Heinrich, Peter C., Travis, James, Potempa, Jan

“…Deregulation of the cytokine network is an important adaptation of pathogenic bacteria to modulate and evade a host immune response. Here we describe that IL-6…”
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The C‐terminal domains of the gingipain K polyprotein are necessary for assembly of the active enzyme and expression of associated activities by Sztukowska, Maryta, Sroka, Aneta, Bugno, Marcin, Banbula, Agnieszka, Takahashi, Yusuke, Pike, Robert N., Genco, Caroline A., Travis, James, Potempa, Jan

“…Summary The Porphyromonas gingivalis lysine‐specific cysteine protease (gingipain K, Kgp) is expressed as a large precursor protein consisting of a leader…”
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Isolation and Properties of Stachyrase A, a Chymotrypsin-Like Serine Proteinase from Stachybotrys chartarum by KORDULA, Tomasz, BANBULA, Agnieszka, MACOMSON, Jeremy, TRAVIS, James

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The Properties of Rabbit α1-Macroglobulin upon Activation Are Distinct from Those of Rabbit and Human α2-Macroglobulins by Banbula, Agnieszka, Chang, Lara S., Beyer, Wayne F., Bohra, Charu L., Cianciolo, George J., Pizzo, Salvatore V.

“…We have characterized native and activated forms of rabbit α1M and compared them to rabbit and human α2M. Similar to human α2M, rabbit α1M is a tetramer…”
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Porphyromonas gingivalis DPP-7 Represents a Novel Type of Dipeptidylpeptidase by Banbula, Agnieszka, Yen, Jane, Oleksy, Aneta, Mak, Pawel, Bugno, Marcin, Travis, James, Potempa, Jan

“…A novel dipeptidylpeptidase (DPP-7) was purified from the membrane fraction of Porphyromonas gingivalis.This enzyme, with an apparent molecular mass of 76 kDa,…”
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Proteolysis of interleukin-6 receptor (IL-6R) by Porphyromonas gingivalis cysteine proteinases (gingipains) inhibits interleukin-6-mediated cell activation by Oleksy, Aneta, Banbula, Agnieszka, Bugno, Marcin, Travis, James, Potempa, Jan

“…Current consensus is that periodontitis is an infectious disease in which a deregulated chronic inflammatory reaction not only may lead to periodontal tissue…”
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Isolation and characterization of a highly specific serine endopeptidase from an oral strain of Staphylococcus epidermidis by Moon, J L, Banbula, A, Oleksy, A, Mayo, J A, Travis, J

“…Infection by Staphylococcus epidermidis, an opportunistic pathogen, has become a major problem due to the increased use of implanted medical devices and the…”
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Prolyl Tripeptidyl Peptidase from Porphyromonas gingivalis by Banbula, Agnieszka, Mak, Pawel, Bugno, Marcin, Silberring, Jerzy, Dubin, Adam, Nelson, Daniel, Travis, James, Potempa, Jan

“…Porphyromonas gingivalis possesses a complex proteolytic system, which is essential for both its growth and evasion of host defense mechanisms. In this report…”
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Crystal structure of gingipain R: an Arg-specific bacterial cysteine proteinase with a caspase-like fold by Eichinger, Andreas, Beisel, Hans-Georg, Jacob, Uwe, Huber, Robert, Medrano, Francisco-Javier, Banbula, Agnieszka, Potempa, Jan, Travis, Jim, Bode, Wolfram

“…Gingipains are cysteine proteinases acting as key virulence factors of the bacterium Porphyromonas gingivalis, the major pathogen in periodontal disease. The…”
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Blood inhibitory capacity toward exogenous plasmin by Banbula, Agnieszka, Zimmerman, Thomas P, Novokhatny, Valery V

“…Stabilized, active plasmin is a novel thrombolytic for direct delivery to clots. Although it is known that protease inhibitors in plasma inhibit plasmin, the…”
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Emerging family of proline-specific peptidases of Porphyromonas gingivalis : Purification and characterization of serine dipeptidyl peptidase, a structural and functional homologue of mammalian prolyl dipeptidyl peptidase IV by BANBULA, A, BUGNO, M, GOLDSTEIN, J, YEN, J, NELSON, D, TRAVIS, J, POTEMPA, J

“…Porphyromonas gingivalis is an asaccharolytic and anaerobic bacterium that possesses a complex proteolytic system which is essential for its growth and evasion…”
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Prolyl tripeptidyl peptidase from Porphyromonas gingivalis. A novel enzyme with possible pathological implications for the development of periodontitis by Banbula, A, Mak, P, Bugno, M, Silberring, J, Dubin, A, Nelson, D, Travis, J, Potempa, J

“…Porphyromonas gingivalis possesses a complex proteolytic system, which is essential for both its growth and evasion of host defense mechanisms. In this report…”
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The properties of rabbit alpha1-macroglobulin upon activation are distinct from those of rabbit and human alpha2-macroglobulins by Banbula, Agnieszka, Chang, Lara S, Beyer, Wayne F, Bohra, Charu L, Cianciolo, George J, Pizzo, Salvatore V

“…We have characterized native and activated forms of rabbit alpha1M and compared them to rabbit and human alpha2M. Similar to human alpha2M, rabbit alpha1M is a…”
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Properties of Rabbit [alpha]₁-Macroglobulin upon Activation Are Distinct from Those of Rabbit and Human [alpha]₂-Macroglobulins by Banbula, Agnieszka, Chang, Lara S, Beyer, Wayne F, Bohra, Charu L, Cianciolo, George J, Pizzo, Salvatore V

“…We have characterized native and activated forms of rabbit [alpha]₁M and compared them to rabbit and human [alpha]₂M. Similar to human [alpha]₂M, rabbit…”
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Serpin α1proteinase inhibitor probed by intrinsic tryptophan fluorescence spectroscopy by Koloczek, Henryk, Banbula, Agnieszka, Potempa, Jan, Salvesen, Guy S.

“…Various conformational forms of the archetypal serpin human α1proteinase inhibitor (α1PI), including ordered polymers, active and inactive monomers, and…”
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Emerging Family of Proline-Specific Peptidases ofPorphyromonas gingivalis: Purification and Characterization of Serine Dipeptidyl Peptidase, a Structural and Functional Homologue of Mammalian Prolyl Dipeptidyl Peptidase IV by Agnieszka Banbula, Marcin Bugno, Jason Goldstein, Jane Yen, Daniel Nelson, James Travis, Jan Potempa

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Serpin α 1 proteinase inhibitor probed by intrinsic tryptophan fluorescence spectroscopy by Koloczek, Henryk, Banbula, Agnieszka, Potempa, Jan, Salvesen, Guy S.

“…Various conformational forms of the archetypal serpin human α 1 proteinase inhibitor (α 1 PI), including ordered polymers, active and inactive monomers, and…”
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Crystallization and preliminary X‐ray diffraction analysis of gingipain R2 from Porphyromonas gingivalis in complex with H‐D‐Phe‐Phe‐Arg‐chloromethylketone by Banbula, Agnieszka, Potempa, Jan, Travis, James, Bode, Wolfram, Medrano, Francisco‐Javier

“…Gingipain R2 is a 50 kDa proteinase from the oral pathogenic bacterium Porphyromonas gingivalis. This proteinase, which displays no significant sequence…”
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