Results 121 to 130 of about 11,934 (162)

ADAM and ADAMTS proteases as integrative hubs in heart failure pathogenesis and therapy. [PDF]

iScience
Wang X, He Y, Wang Y, Liu Y, Dai X, Xia Y, Du L, Li C, Zhang D.   +8 more
europepmc   +1 more source

Current Advances in the Physiological Roles and Disease-Associated Mechanisms of ADAMTS16. [PDF]

Int J Mol Sci
Wang L, Zhang J, Zhang Y.
europepmc   +1 more source

Inflammaging and osteoarthritis - therapeutic opportunities. [PDF]

Front Immunol
Chan M, Low P, Ong SC, Choy SM, Lee WX, Goh KY, Ng KM, Chua K, Lee JY, Guo AK, Jia J, Tan EK, Tang HW, Chua K.   +13 more
europepmc   +1 more source

ADAMTS-13 R1206K variant exhibits an open conformation and an enhanced proteolytic activity toward von Willebrand factor. [PDF]

J Thromb Haemost
Liu S, Dong X, Bonnez Q, Chai Z, Meng C, Gil M, Vanhoorelbeke K, Halkidis K, Zheng XL.   +8 more
europepmc   +1 more source

ADAMTS-7 Increase Contributes to Worsened Neurological Outcome in Mice on High Fat Diet. [PDF]

CNS Neurosci Ther
Xu Y, Li J, Zuo Z.
europepmc   +1 more source

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Human glioblastomas overexpress ADAMTS-5 that degrades brevican

Acta Neuropathologica, 2005
Selective cleavage of the Glu395-Ser396 bond of brevican, one of the major proteoglycans in adult brain tissues, is thought to be important for glioma cell invasion. Our previous biochemical study demonstrated that ADAMTS-4, a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) family, has such an activity.
Yasunori Okada, Mitsutoshi Nakada
exaly   +3 more sources

ADAMTS-4 and ADAMTS-5: Key enzymes in osteoarthritis

Journal of Cellular Biochemistry, 2011
Osteoarthritis (OA) is a progressive disease of the joints characterized by degradation of articular cartilage. Although disease initiation may be multi-factorial, the cartilage destruction appears to be a result of uncontrolled proteolytic extracellular matrix destruction.
Priyanka, Verma, Krishna, Dalal
openaire   +2 more sources

Characterization of the promoter in ADAMTS‐5 (aggrecanase‐2)

International Journal of Experimental Pathology, 2004
Introduction  Loss of aggrecan metabolites from the cartilage matrix into the surrounding synovial fluid have allowed for identification of two major cleavage sites within aggrecan: Asn341–Phe342 and Glu373–Ala374 peptide bonds. Proteolysis at the Glu373–Ala374 bond has been specifically attributed to ADAMTS‐4 and ADAMTS‐5.
M.R. Heming, S.D. Wainwright, B. Caterson, C.E. Hughes   +3 more
openaire   +1 more source

ADAMTS-4 and ADAMTS-5

2006
Osteoarthritis (OA) is characterized by articular cartilage erosion as a consequence of proteolytic cleavage of its two major functional macromolecules, type II collagen and aggrecan. Aggrecan degradation in OA and rheumatoid arthritis is attributed to cleavage at the Glu373-Ala374 bond by the aggrecanases.
Anne-Marie Malfait, Micky Tortorella, Elizabeth Arner   +2 more
openaire   +1 more source