Results 41 to 50 of about 94,685 (278)

IGF-I receptor phosphorylation is impaired in cathepsin X-deficient prostate cancer cells [PDF]

open access: yes, 2012
The cysteine-type peptidase cathepsin X is highly upregulated in several cancers and presumably promotes tumor invasion through bypassing cellular senescence. Here, we present first evidence that the underlying mechanism may involve the regulation of the
Bunsen, Thea   +3 more
core   +1 more source

Osteopenia due to enhanced cathepsin K release by BK channel ablation in osteoclasts. [PDF]

open access: yesPLoS ONE, 2011
BACKGROUND: The process of bone resorption by osteoclasts is regulated by Cathepsin K, the lysosomal collagenase responsible for the degradation of the organic bone matrix during bone remodeling.
Ulrike Sausbier   +10 more
doaj   +1 more source

A cardinal role for cathepsin D in co-ordinating the host-mediated apoptosis of macrophages and killing of pneumococci [PDF]

open access: yes, 2011
The bactericidal function of macrophages against pneumococci is enhanced by their apoptotic demise, which is controlled by the anti-apoptotic protein Mcl-1.
Bewley, M.A.   +10 more
core   +5 more sources

Probing the activity modification space of the cysteine peptidase cathepsin K with novel allosteric modifiers.

open access: yesPLoS ONE, 2014
Targeting allosteric sites is gaining increasing recognition as a strategy for modulating the activity of enzymes, especially in drug design. Here we investigate the mechanisms of allosteric regulation of cathepsin K as a representative of cysteine ...
Marko Novinec   +2 more
doaj   +1 more source

Chondroitin Sulfate Promotes Activation of Cathepsin K [PDF]

open access: yesJournal of Biological Chemistry, 2014
Cathepsin K (CatK), a major lysosomal collagenase produced by osteoclasts, plays an important role in bone resorption. Evidence exists that the collagenase activity of CatK is promoted by chondroitin sulfate (CS), a sulfated glycosaminoglycan. This study examines the role of CS in facilitating CatK activation.
Peter A, Lemaire   +7 more
openaire   +2 more sources

Advances in the discovery of cathepsin K inhibitors on bone resorption

open access: yesJournal of Enzyme Inhibition and Medicinal Chemistry, 2018
Cathepsin K (Cat K), highly expressed in osteoclasts, is a cysteine protease member of the cathepsin lysosomal protease family and has been of increasing interest as a target of medicinal chemistry efforts for its role in bone matrix degradation ...
Jun Lu   +5 more
doaj   +1 more source

Cathepsin K-Cre causes unexpected germline deletion of genes in mice. [PDF]

open access: yesPLoS ONE, 2012
Osteoclasts are terminally differentiated cells that attach to bone and secrete proteases to degrade the bone matrix. The primary protease responsible for the degradation of the organic component of the bone matrix is Cathepsin K, which was largely ...
Crystal L Winkeler   +3 more
doaj   +1 more source

The role of proteases in pathologies of the synovial joint [PDF]

open access: yes, 2008
Synovial (diarthrodial) joints are employed within the body to provide skeletal mobility and have a characteristic structure adapted to provide a smooth almost frictionless surface for articulation.
Buttle, D, Jones, GC, Riley, GP
core   +1 more source

Inappropriate cathepsin K secretion promotes its enzymatic activation driving heart and valve malformation

open access: yesJCI Insight, 2020
Although congenital heart defects (CHDs) represent the most common birth defect, a comprehensive understanding of disease etiology remains unknown.
Po-Nien Lu   +5 more
doaj   +1 more source

Microplate assay for quantitative determination of cathepsin activities in viable cells using derivatives of 4-methoxy-β-naphthylamide

open access: yesBioTechniques, 2006
A method is described allowing the selective determination of four cathepsins (B, H, K, and L) in live cells. Adherently growing cells are incubated with partially selective substrates for each cathepsin (peptidic derivatives of 4-methoxy-β-naphthylamine)
Anke Rüttger   +4 more
doaj   +1 more source

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