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1
Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra α-helical domain
Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra α-helical domain
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Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra α-helical domain

Anand, Kanchan ; Palm, Gottfried J. ; Mesters, Jeroen R. ; Siddell, Stuart G. ; Ziebuhr, John ; Hilgenfeld, Rolf

The EMBO journal, 2002-07, Vol.21 (13), p.3213-3224 [Periódico revisado por pares]

Chichester, UK: John Wiley & Sons, Ltd

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2
Etk/Bmx regulates proteinase-activated-receptor1 (PAR1) in breast cancer invasion: signaling partners, hierarchy and physiological significance
Etk/Bmx regulates proteinase-activated-receptor1 (PAR1) in breast cancer invasion: signaling partners, hierarchy and physiological significance
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Etk/Bmx regulates proteinase-activated-receptor1 (PAR1) in breast cancer invasion: signaling partners, hierarchy and physiological significance

Cohen, Irit ; Maoz, Myriam ; Turm, Hagit ; Grisaru-Granovsky, Sorina ; Maly, Bella ; Uziely, Beatrice ; Weiss, Einat ; Abramovitch, Rinat ; Gross, Eithan ; Barzilay, Oded ; Qiu, Yun ; Bar-Shavit, Rachel Creighton, Chad

PloS one, 2010-06, Vol.5 (6), p.e11135-e11135 [Periódico revisado por pares]

United States: Public Library of Science

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3
Bikunin — not just a plasma proteinase inhibitor
Bikunin — not just a plasma proteinase inhibitor
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Bikunin — not just a plasma proteinase inhibitor

Fries, Erik ; Blom, Anna M

International Journal of Biochemistry and Cell Biology, 2000-02, Vol.32 (2), p.125-137 [Periódico revisado por pares]

Netherlands: Elsevier Ltd

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4
Neutrophil and Pathogen Proteinases versus Proteinase-Activated Receptor-2 Lung Epithelial Cells: More Terminators than Activators
Neutrophil and Pathogen Proteinases versus Proteinase-Activated Receptor-2 Lung Epithelial Cells: More Terminators than Activators
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Neutrophil and Pathogen Proteinases versus Proteinase-Activated Receptor-2 Lung Epithelial Cells: More Terminators than Activators

Chignard, Michel ; Pidard, Dominique

American journal of respiratory cell and molecular biology, 2006-04, Vol.34 (4), p.394-398 [Periódico revisado por pares]

United States: Am Thoracic Soc

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5
active Zot domain (aa 288-293) increases ZO-1 and myosin 1C serine/threonine phosphorylation, alters interaction between ZO-1 and its binding partners, and induces tight junction disassembly through proteinase activated receptor 2 activation
active Zot domain (aa 288-293) increases ZO-1 and myosin 1C serine/threonine phosphorylation, alters interaction between ZO-1 and its binding partners, and induces tight junction disassembly through proteinase activated receptor 2 activation
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active Zot domain (aa 288-293) increases ZO-1 and myosin 1C serine/threonine phosphorylation, alters interaction between ZO-1 and its binding partners, and induces tight junction disassembly through proteinase activated receptor 2 activation

Goldblum, Simeon E ; Rai, Usha ; Tripathi, Amit ; Thakar, Manjusha ; De Leo, Luigina ; Di Toro, Nicola ; Not, Tarcisio ; Ramachandran, Rithwik ; Puche, Adam C ; Hollenberg, Morley D ; Fasano, Alessio

The FASEB journal, 2011-01, Vol.25 (1), p.144-158 [Periódico revisado por pares]

United States: The Federation of American Societies for Experimental Biology

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6
IdeS, a novel streptococcal cysteine proteinase with unique specificity for immunoglobulin G
IdeS, a novel streptococcal cysteine proteinase with unique specificity for immunoglobulin G
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IdeS, a novel streptococcal cysteine proteinase with unique specificity for immunoglobulin G

von Pawel-Rammingen, Ulrich ; Johansson, Björn P. ; Björck, Lars

The EMBO journal, 2002-04, Vol.21 (7), p.1607-1615 [Periódico revisado por pares]

Chichester, UK: John Wiley & Sons, Ltd

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7
The retroviral proteinase active site and the N-terminus of Ddi1 are required for repression of protein secretion
The retroviral proteinase active site and the N-terminus of Ddi1 are required for repression of protein secretion
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The retroviral proteinase active site and the N-terminus of Ddi1 are required for repression of protein secretion

White, Rhian E. ; Dickinson, J. Richard ; Semple, Colin A.M. ; Powell, David J. ; Berry, Colin

FEBS letters, 2011-01, Vol.585 (1), p.139-142 [Periódico revisado por pares]

England: Elsevier B.V

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8
The NTR domain of procollagen C-proteinase enhancer-1 (PCPE-1) mediates PCPE-1 binding to syndecans-1, -2 and -4 as well as fibronectin
The NTR domain of procollagen C-proteinase enhancer-1 (PCPE-1) mediates PCPE-1 binding to syndecans-1, -2 and -4 as well as fibronectin
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The NTR domain of procollagen C-proteinase enhancer-1 (PCPE-1) mediates PCPE-1 binding to syndecans-1, -2 and -4 as well as fibronectin

Weiss, Tali ; Brusel, Marina ; Rousselle, Patricia ; Kessler, Efrat

The international journal of biochemistry & cell biology, 2014-12, Vol.57, p.45-53 [Periódico revisado por pares]

Netherlands: Elsevier Ltd

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9
Proteinase yscE, the yeast proteasome/multicatalytic-multifunctional proteinase: mutants unravel its function in stress induced proteolysis and uncover its necessity for cell survival
Proteinase yscE, the yeast proteasome/multicatalytic-multifunctional proteinase: mutants unravel its function in stress induced proteolysis and uncover its necessity for cell survival
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Proteinase yscE, the yeast proteasome/multicatalytic-multifunctional proteinase: mutants unravel its function in stress induced proteolysis and uncover its necessity for cell survival

Heinemeyer, W ; Kleinschmidt, J.A ; Saidowsky, J ; Escher, C ; Wolf, D.H

The EMBO journal, 1991-03, Vol.10 (3), p.555-562 [Periódico revisado por pares]

England

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10
Ddi1-like protein from Leishmania major is an active aspartyl proteinase
Ddi1-like protein from Leishmania major is an active aspartyl proteinase
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Ddi1-like protein from Leishmania major is an active aspartyl proteinase

Perteguer, María J. ; Gómez-Puertas, Paulino ; Cañavate, Carmen ; Dagger, Francehuli ; Gárate, Teresa ; Valdivieso, Elizabeth

Cell stress & chaperones, 2013-03, Vol.18 (2), p.171-181 [Periódico revisado por pares]

Dordrecht: Springer

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