Results 301 to 310 of about 108,576 (328)

Cathepsin L, But Not Cathepsin B, Is a Potential Kininogenase

Biological Chemistry, 2001
Although papain-like enzymes are strongly inhibited by their natural tight-binding inhibitors of the cystatin superfamily, cathepsins B and L may still retain some residual proteolytic activity toward Z-Phe-Arg-AMC in the presence of an excess of kininogen. This activity is abolished by adding E-64 or chicken cystatin.
C, Desmazes, F, Gauthier, G, Lalmanach
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Inhibition of cathepsin L-like proteases by cathepsin V propeptide

bchm, 2007
Abstract The N-terminal propeptide domains of several cathepsin L-like cysteine proteases have been shown to possess potent inhibitory activity. Here we report the first kinetic characterisation of the inhibition properties of the cathepsin V propeptide (CatV PP).
Burden, Roberta, Snoddy, P., Jefferies, C.A., Walker, Brian, Scott, Christopher   +4 more
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Dipeptidyl nitrile inhibitors of Cathepsin L

Bioorganic & Medicinal Chemistry Letters, 2009
A series of potent Cathepsin L inhibitors with good selectivity with respect to other cysteine Cathepsins is described and SAR is discussed with reference to the crystal structure of a protein-ligand complex.
Asaad, Nabil, Bethel, Paul A., Coulson, Michelle D., Dawson, Jack E., Ford, Susannah J., Gerhardt, Stefan, Grist, Matthew, Hamlin, Gordon A., James, Michael J., Jones, Emma V., Karoutchi, Galith I., Kenny, Peter W., Morley, Andrew D., Oldham, Keith, Rankine, Neil, Ryan, David, Wells, Stuart L., Wood, Linda, Augustin, Martin A., Krapp, Stephan, Simader, Hannes, Steinbacher, Stefan   +21 more
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Surface activation of pro-cathepsin L

Biochemical and Biophysical Research Communications, 1992
Pro-cathepsin L is an inactive zymogen that has been shown previously to undergo autolysis at pH 3.0 to give mature forms of the enzyme. We have now been able to demonstrate that this enzyme can undergo activation at pH 5.5 in the presence of negatively charged surfaces.
R W, Mason, S D, Massey
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Cathepsin L gene organization in crustaceans

Gene, 1998
The gene structure of a cathepsin L of the shrimp Penaeus vannamei has been determined by the polymerase chain reaction. It comprises six exons of various lengths spanning a total of 1792bp. This architecture is homologous to that of rat cathepsin L, three conserved sites of intron position have been effectively identified, with the exception of the ...
C, Le Boulay, D, Sellos, A, Van Wormhoudt   +2 more
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Clinical significance of cathepsin L and cathepsin B in dilated cardiomyopathy

Molecular and Cellular Biochemistry, 2017
Dysregulated expression of lysosomal cysteine cathepsins is associated with adverse cardiac remodeling, a characteristic of several cardiovascular diseases. However, the information regarding the role of cysteine cathepsin L (CTSL) and cathepsin B (CTSB) in dilated cardiomyopathy (DCM) is limited.
Siddharth, Mehra, Manish, Kumar, Mansi, Manchanda, Ratnakar, Singh, Bhaskar, Thakur, Neha, Rani, Sudheer, Arava, Rajiv, Narang, Dharamvir Singh, Arya, Shyam S, Chauhan   +9 more
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Cathepsin L Digestion of Nanobioconjugates upon Endocytosis

ACS Nano, 2009
Understanding the dynamic fate and interactions of bioconjugated nanoparticles within living cells and organisms is a prerequisite for their use as in situ sensors or actuators. While recent research has provided indications on the effect of size, shape, and surface properties of nanoparticles on their internalization by living cells, the biochemical ...
Sée, Violaine, Free, Paul, Cesbron, Yann, Nativo, Paula, Shaheen, Umbreen, Rigden, Daniel J., Spiller, David G., Fernig, David G., White, Michael R H, Prior, Ian A., Brust, Mathias, Lounis, Brahim, Levy, Raphaël   +12 more
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Primary digestive cathepsins L of Tribolium castaneum larvae: Proteomic identification, properties, comparison with human lysosomal cathepsin L

Insect Biochemistry and Molecular Biology, 2022
We previously described the most highly expressed enzymes from the gut of the red flour beetle, Tribolium castaneum, as cathepsins L. In the present study, two C1 family-specific cysteine cathepsin L enzymes from the larval midgut were isolated and identified using MALDI-TOF MS analysis. The isolated T. castaneum cathepsins were characterized according
E.A. Dvoryakova, K.S. Vinokurov, V.F. Tereshchenkova, Y.E. Dunaevsky, M.A. Belozersky, B. Oppert, I.Y. Filippova, E.N. Elpidina   +7 more
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Baboon (Papio ursinus) cathepsin L: purification, characterization and comparison with human and sheep cathepsin L

Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 1995
Cathepsin L was purified from the liver of a higher primate, the baboon (Papio ursinus), largely in a single-chain form and in the form of proteolytically active complexes with an endogenous cystatin. This mimics the situation found in both human and sheep livers. Both forms of cathepsin L were active at physiological pH.
T H, Coetzer, K M, Dennehy, R N, Pike, C, Dennison   +3 more
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Cathepsin L (EC 3.4.22.15)

1998
Abstract In 1971, Bohley and co-workers [1248] and, in 1972, Kirschke et al. [340] described a new enzyme from rat liver lysosomes which degraded proteins but not synthetic substrates. In 1974 the enzyme was named cathepsin L (in which 'L' stands for lysosomes) by the same authors [343, 1284].
Heidrun Kirschke, Alan J Barrett, Neil D Rawlings   +2 more
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