Results 321 to 330 of about 47,940 (359)

p97/VCP is required for piecemeal autophagy of aggresomes. [PDF]

Nat Commun
Körner M, Müller P, Das H, Kraus F, Pfeuffer T, Spielhaupter S, Oeljeklaus S, Schülein-Völk C, Harper JW, Warscheid B, Buchberger A.   +10 more
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Exploring the Pleiotropy of PCSK9: A Wide Range of Influences from Lipid Regulation to Extrahepatic Function. [PDF]

J Inflamm Res
Wang H, Tang G, Wu J, Qin X.
europepmc   +1 more source

Purification and Characterization of a Rice Cysteine Proteinase Inhibitor

Agricultural and Biological Chemistry, 1987
A proteinaceous substance that inhibited the activity of papain (EC 3.4.22.2) was found in seeds of rice, Oryza sativa L. japonica. This cysteine proteinase inhibitor (CPI) was purified by a series of purification procedures including CM-Sephadex C-50, Sephadex G-75, and DEAE- Sephadex A-50 chromatography.
Soichi Arai, Keiko Abe, Hiroto Kondo
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Novel Cysteine Proteinase Inhibitors Homologous to the Proregions of Cysteine Proteinases

Current Protein & Peptide Science, 2002
Propeptides of papain-like cysteine proteinases such as papain, cathepsins B, L and S are potent inhibitors of their cognate cysteine proteinases with Ki values in the nanomolar range, and they exhibit highest inhibition selectivity for enzymes from which they originate. Recent studies have identified novel inhibitor proteins that are homologous to the
Mitsuhiro Kurata, Susumu Y. Takahashi, Shoji Watabe, Yoshimi Yamamoto, R. Murakami   +4 more
openaire   +3 more sources

Cysteine proteinase inhibitor levels in semen

Clinical Biochemistry, 1986
New proteinase inhibitors have recently been found in seminal plasma which specifically inhibit cysteine proteinases such as ficin, papain, cathepsin H and cathepsin B. The inhibitors consist of two components, In-A and In-B, both of which are effective in native semen.
Kayoko Minakata, Minoru Asano, Osamu Yonekawa   +2 more
openaire   +3 more sources

Cysteine proteinase inhibitors in human placenta

Placenta, 1985
When human placental extract was chromatographed on a Sephadex G-75 column, cysteine proteinase inhibitors with molecular weights of 80 000 and 12 300 were eluted. The high molecular weight peak (CPI-H) was identified as alpha-cysteine proteinase inhibitor.
G. Sawicki, M. Warwas
openaire   +3 more sources

Cysteine proteinase inhibitors in psoriatic epidermis

Archives of Dermatological Research, 1983
Human psoriatic epidermis and scales were demonstrated to contain two antigenically separate cysteine proteinase inhibitors, one acidic with an isoelectric point of 4.7-5.0 (ACPI) and one neutral with an isoelectric point of 6.0-6.5 (NCPI), while normal epidermis contains only ACPI.
Mikko Järvinen, Ari Rinne, I. Joronen, Väinö K. Hopsu-Havu   +3 more
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Osteoclastogenesis is decreased by cysteine proteinase inhibitors

Bone, 2004
The effects of cystatin C and other cysteine proteinase inhibitors on osteoclast formation and differentiation have been investigated. Cystatin C decreased osteoclast formation stimulated by parathyroid hormone (PTH), 1,25(OH)2-vitamin D3 or interleukin-6 (IL-6) (in the presence of its soluble receptor) as assessed by the number of tartrate-resistant ...
Monica Brage, Franciszek Kasprzykowski, Regina Kasprzykowska, Maria Ransjö, Anita Lie, Ulf H. Lerner, Magnus Abrahamson, Anders Grubb   +7 more
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Bombyx Cysteine Proteinase Inhibitor (BCPI) Homologous to Propeptide Regions of Cysteine Proteinases Is a Strong, Selective Inhibitor of Cathepsin L-like Cysteine Proteinases

Journal of Biochemistry, 2001
Bombyx cysteine proteinase inhibitor (BCPI) is a novel cysteine proteinase inhibitor. The protein sequence is homologous to the proregions of certain cysteine proteinases. Here we report the mechanism of its inhibition of several cysteine proteinases.
Yoshimi Yamamoto, Kazuo Ogawa, Susumu Y. Takahashi, Shoji Watabe, Yumiko Makino, Mitsuhiro Kurata   +5 more
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Cystatin S: A Cysteine Proteinase Inhibitor of Human Saliva

The Journal of Biochemistry, 1984
An acidic protein of human saliva, which we named SAP-1 previously, is now shown to be an inhibitor of several cysteine proteinases. The protein inhibited papain and ficin strongly, and stem bromelain and bovine cathepsin C partially. However, it did not inhibit either porcine cathepsin B or clostripain.
Satoko Isemura, Kazuo Sanada, Eiichi Saitoh, Seiki Ito, Mamoru Isemura   +4 more
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