Results 11 to 20 of about 124,559,533 (209)

Seprase: An overview of an important matrix serine protease [PDF]

, 2008
Seprase or Fibroblast Activation Protein (FAP) is an integral membrane serine peptidase, which has been shown to have gelatinase activity. Seprase has a dual function in tumour progression.
O\u27Brien, Pamela, O'Brien, Pamela, O'Connor, Brendan, O\u27Connor, Brendan   +3 more
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The purification and characterisation of novel dipeptidyl peptidase IV-like activity from bovine serum [PDF]

, 2004
The discovery of a potentially novel proline-specific peptidase from bovine serum is presented which is capable of cleaving the dipeptidyl peptidase IV (DPIV) substrate Gly-Pro-MCA.
Buckley, Seamus J., O'Connor, Brendan, O\u27Connor, Brendan, Collins, Patrick   +3 more
core   +2 more sources

Ecotin-like serine peptidase inhibitor ISP1 of Leishmania major plays a role in flagellar pocket dynamics and promastigote differentiation [PDF]

, 2012
Leishmania ISPs are ecotin-like natural peptide inhibitors of trypsin-family serine peptidases, enzymes that are absent from the Leishmania genome. This led to the proposal that ISPs inhibit host serine peptidases and we have recently shown that ISP2 ...
Petr Volf, Mottram, Jeremy C, Gareth D. Westrop, Eschenlauer, Sylvain C, Volf, Petr, Amy Goundry, Sylvain C. Eschenlauer, Jeremy C. Mottram, Lima, Ana Paula C A, Lima, Ana Paula C.A., Morrison, Lesley S, Morrison, Lesley S., Lesley S. Morrison, Ana Paula C. A. Lima, Goundry, Amy, Faria, Marilia S, Marilia S. Faria, Graham H. Coombs, Westrop, Gareth D., Coombs, Graham H, Anna Dostalova, Laurence Tetley, Faria, Marilia S., Tetley, Laurence, Dostalova, Anna, Westrop, Gareth D, Mottram, Jeremy C., Eschenlauer, Sylvain C., Coombs, Graham H.   +28 more
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Solvent and thermal stability, and pH kinetics, of proline-specific dipeptidyl peptidase IV-like enzyme from bovine serum [PDF]

, 2007
Proline-specific dipeptidyl peptidase-like (DPP IV; EC 3.4.14.5) activity in bovine serum has attracted little attention despite its ready availability and the paucity of useful proline-cleaving enzymes.
Ruth, Deborah M., Buckley, Seamus J., Ó Fágáin, Ciarán, O'Connor, Brendan, O\u27Connor, Brendan   +4 more
core   +2 more sources

Crystal structures of trypanosoma brucei oligopeptidase B broaden the paradigm of catalytic regulation in prolyl oligopeptidase family enzymes [PDF]

, 2013
Oligopeptidase B cleaves after basic amino acids in peptides up to 30 residues. As a virulence factor in bacteria and trypanosomatid pathogens that is absent in higher eukaryotes, this is a promising drug target.
Rory E Morty, Canning Peter, Rea, Dean, Dean Rea (483664), Morty Rory E., Morty, Rory E., Dean Rea, Vilmos Fülöp, Rory E. Morty (341515), Canning, Peter, Fülöp, Vilmos, Peter Canning, Peter Canning (483663), Vilmos Fülöp (483665), Rea Dean, Fülöp Vilmos   +15 more
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Mitochondrial protein import [PDF]

, 1988
Transport of nuclear-encoded precursor proteins into mitochondria includes proteolytic cleavage of aminoterminal targeting sequences in the mitochondrial matrix. We have isolated the processing activity from Neurospora crassa.
Hawlitschek, Gerhard, Schneider, Helmut, Tropschug, Maximilian, Hartl, Franz-Ulrich, Neupert, Walter, Schmidt, Bernd   +5 more
core   +1 more source

The study of a new and specific proline cleaving peptidase from bovine serum [PDF]

, 2003
Prolyl oligopeptidase is a serine peptidase characterised by oligoendopeptidase activity. Definitive evidence for the discrete biological role of prolyl oligopeptidase remains unknown, though its role in the maturation and degradation of peptide hormones
Collins, Patrick
core   +1 more source

HTRA2 (HtrA serine peptidase 2) [PDF]

, 2012
Review on HTRA2 (HtrA serine peptidase 2), with data on DNA, on the protein encoded, and where the gene is ...
Zurawa-Janicka, D, Lipinska, B, Jarzab, M   +2 more
core   +1 more source

T-SP1: a novel serine protease-like protein predominantly expressed in testis [PDF]

, 2008
Here, we describe a novel member in the group of membrane-anchored chymotrypsin (S1)-like serine proteases, namely testis serine protease 1 (T-SP1), as it is principally expressed in testis tissue.
Nerlich, Andreas, Profanter, Birgit, Geissler, Claudia, Neth, Peter, Sommerhoff, Christian P., Naegler, Dorit K., Jochum, Marianne   +6 more
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A comprehensive nomenclature for serine proteases with homology to tissue kallikreins [PDF]

, 2006
The human kallikrein locus on chromosome 19q13.3-13.4 contains kallikrein 1 - the tissue kallikrein - and 14 related serine proteases. Recent investigations into their function and evolution have indicated that the present nomenclature for these proteins
Scorilas, Andreas, Malm, Johan,, Talieri, M, Courty, Yves, Ulf-Håkan Stenman, Lundwall, Åke,, Yousef, George M, Georgia Sotiropoulou, Lois J. Maltais, Talieri, Maroulio, Olsson, A Yvonne, Yousef, George, Talieri, M., Malm, Johan, Carsten Stephan, Stephan, Carsten, Blaber, M., Liija, H., Malm, J., Fritz, Hans, Petraki, C, Scorilas, A, Diamandis, EP, Blaber, Michael, Clements, Judith A, Lundwall, A., Lilja, Hans, Andreas Scorilas, Scorilas, A., Olsson, A. Yvonne, Hans Fritz, Judith A. Clements, Clements, JA, Fritz, H., Lundwall, Åke, Constantina Petraki, Maltais, Lois J, Sotiropoulou, Georgia, Clements, J A, Clements, Judith, Lilja, H, Lund University., Blaber, M, Olsson, AY, Vimla Band, A. Yvonne Olsson, Lundwall, A, Band, Vimla, Maroulio Talieri, Stephan, C., Sotiropoulou, G, Lilja, Hans,, Yousef, G M, Petraki, Constantina, Courty, Y, Fritz, H, Sotiropoulou, G., Courty, Y., Eleftherios P. Diamandis, Maltais, LJ, Åke Lundwall, Michael Blaber, Yousef, GM, Diamandis, Eleftherios P, Hans Lilja, Stenman, Ulf-Hakan, Diamandis, E P, Maltais, L J, Stephan, C, Petraki, C., George M. Yousef, Stenman, UH, Malm, J, Band, V, Yves Courty, Olsson, A Y, Band, V., Maltais, Lois, Diamandis, Eleftherios, Johan Malm   +79 more
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