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Expression of cathepsin K in chordoma

Human Pathology, 2000
Invasive growth of chordoma is accompanied by severe destruction of adjacent bone tissue, a fact that requires high proteolytic activity at the tumor invasion fronts. In this context, cathepsin K is a candidate molecule. It is a protease with high collagenolytic and elastinolytic activity and previously thought to be restricted to osteoclasts and ...
C, Haeckel   +8 more
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Novel scaffold for cathepsin K inhibitors

Bioorganic & Medicinal Chemistry Letters, 2007
Pyrrolopyrimidine, a novel scaffold, allows to adjust interactions within the S3 subsite of cathepsin K. The core intermediate 10 facilitated the P3 optimization and identified highly potent and selective cathepsin K inhibitors 11-20.
Naoki, Teno   +21 more
openaire   +2 more sources

Peptidomimetic Inhibitors of Cathepsin K

Current Topics in Medicinal Chemistry, 2010
Cathepsin K (Cat K) is the primary enzyme involved in Type I collagen degradation in bone resorption. The development of a Cat K inhibitor should provide an effective treatment for osteoporosis. Key components of a clinically viable inhibitor are oral bioavailability, high selectivity over related cathepsins, and a covalent, reversible warhead to bind ...
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Keto-1,3,4-oxadiazoles as cathepsin K inhibitors

Bioorganic & Medicinal Chemistry Letters, 2006
AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 200 leading journals. To access a ChemInform Abstract, please click on HTML or PDF.
James T, Palmer   +6 more
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Cathepsin K Expression in Human Lung

2006
Tissue remodeling is crucial in different lung diseases, in the embryonal development as well as in bronchial carcinoma. Cathepsins were proposed to be involved in the degradation of matrix proteins. Cathepsin K is one of the most potent matrix-degrading cysteine proteinases known as yet.
F, Bühling   +9 more
openaire   +2 more sources

Cathepsin K: The association between Cathepsin K expression and sphenoid sinus invasion of pituitary adenomas

Medical Hypotheses, 2016
Pituitary adenomas with sphenoid sinus or clivus invasion are not uncommon, but the pathogenesis responsible for this phenomenon remains unclear. Cathepsin K, expressed predominantly in osteoclasts, can degrade type I collagen and plays an essential role in bone resorption.
Hongyan, Liu   +3 more
openaire   +2 more sources

Cathepsin K (EC 3.4.22.38)

1998
Abstract peptidase named OC-2. In the same year, human equivalents of the rabbit gene were mentioned independently in two abstracts by Drake et al. [1787] and Li et al. [1797] and the sequence was published in 1995 (in order of date of submission) by Li et al. [ 1798], lnaoka et al. [1792], Shi et al.
Heidrun Kirschke   +2 more
openaire   +1 more source

Cathepsin K inhibitors, 2000 – 2004

Expert Opinion on Therapeutic Patents, 2005
Cathepsin K is one of eleven cysteine proteases from the papain superfamily known to be expressed in the human genome. Its selective and abundant expression in osteoclasts and critical role in the degradative phase of bone remodelling suggests that selective inhibition of cathepsin K may provide an effective therapy for the treatment of osteoporosis ...
Jiaqiang Cai   +3 more
openaire   +1 more source

Functions of cathepsin K in bone resorption. Lessons from cathepsin K deficient mice.

Advances in experimental medicine and biology, 2000
Cathepsin K is a cysteine proteinase expressed predominantly in osteoclasts. Cathepsin K cleaves key bone matrix proteins and is believed to play an important role in degrading the organic phase of bone during bone resorption. Pycnodysostosis, an autosomal recessive osteosclerosing skeletal disorder has recently been shown to result from mutations in ...
Saftig, P.   +7 more
openaire   +4 more sources

Peptide Ketobenzoxazole Inhibitors Bound to Cathepsin K

Biochemistry, 2003
Potent inhibitors of human cysteine proteases of the papain family have been made and assayed versus a number of relevant family members. We describe the synthesis of peptide alpha-ketoheterocyclic inhibitors that occupy binding subsites S1'-S3 of the cysteine protease substrate recognition cleft and that form a reversible covalent bond with the Cys 25
Mary E, McGrath   +7 more
openaire   +2 more sources

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