Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Protease Inhibitors/chemistry"'
Autor:
Audrey Hessel, Katharina Weinhäupl, Adrián Velázquez-Campoy, Christophe Chipot, Cécile Morlot, Paul Schanda, Jan Felix, François Dehez, Olga Abian, Hugo Pacheco de Freitas Fraga, Irina Gutsche, Diego F. Gauto
Publikováno v:
Zaguán. Repositorio Digital de la Universidad de Zaragoza
instname
'Science Advances ', vol: 5, pages: eaaw3818-1-eaaw3818-19 (2019)
Science Advances
Science Advances, American Association for the Advancement of Science (AAAS), 2019, 5 (9), pp.eaaw3818. ⟨10.1126/sciadv.aaw3818⟩
SCIENCE ADVANCES
Digital.CSIC. Repositorio Institucional del CSIC
Science Advances, 2019, 5 (9), pp.eaaw3818. ⟨10.1126/sciadv.aaw3818⟩
instname
'Science Advances ', vol: 5, pages: eaaw3818-1-eaaw3818-19 (2019)
Science Advances
Science Advances, American Association for the Advancement of Science (AAAS), 2019, 5 (9), pp.eaaw3818. ⟨10.1126/sciadv.aaw3818⟩
SCIENCE ADVANCES
Digital.CSIC. Repositorio Institucional del CSIC
Science Advances, 2019, 5 (9), pp.eaaw3818. ⟨10.1126/sciadv.aaw3818⟩
18 pags., 6 figs., 1 tab. -- Open Access funded by Creative Commons Atribution Licence 4.0
Coordinated conformational transitions in oligomeric enzymatic complexes modulate function in response to substrates and play a crucial role in enzyme inh
Coordinated conformational transitions in oligomeric enzymatic complexes modulate function in response to substrates and play a crucial role in enzyme inh
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7a1324138b0f4d564dc88daa4ccd2c80
Autor:
Christine R. Schar, Jan K. Jensen, Trine Tamberg, Daniel M. Dupont, Lotte K. Vogel, Zebin Hong, Signe Skovbjerg, Karsten Skjoedt, Daphné De Schepper, Lars Vitved
Publikováno v:
Tamberg, T, Hong, Z, De Schepper, D, Skovbjerg, S, Dupont, D M, Vitved, L, Schar, C R, Skjoedt, K, Vogel, L K & Jensen, J K 2019, ' Blocking the proteolytic activity of zymogen matriptase with antibody-based inhibitors ', Journal of Biological Chemistry, vol. 294, no. 1, pp. 314-326 . https://doi.org/10.1074/jbc.RA118.004126
Matriptase is a member of the type-II transmembrane serine protease (TTSP) family and plays a crucial role in the development and maintenance of epithelial tissues. As all chymotrypsin-like serine proteases, matriptase is synthesized as a zymogen (pr
Autor:
Preety Panwar, Liming Xue, Kent Søe, Kamini Srivastava, Simon Law, Jean‐Marie Delaisse, Dieter Brömme
Publikováno v:
Panwar, P, Xue, L, Søe, K, Srivastava, K, Law, S, Delaisse, J-M & Brömme, D 2017, ' An Ectosteric Inhibitor of Cathepsin K Inhibits Bone Resorption in Ovariectomized Mice ', Journal of Bone and Mineral Research, vol. 32, no. 12, pp. 2415-2430 . https://doi.org/10.1002/jbmr.3227
The potent cathepsin K (CatK) inhibitor, Tanshinone IIA sulfonic sodium (T06), was tested for its in vitro and in vivo antiresorptive activities. T06 binds in an ectosteric site of CatK remote from its active site and selectively inhibits collagen de
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4eaa770e17770366d7386291b80ce37a
https://portal.findresearcher.sdu.dk/da/publications/e9798d3b-a927-43a3-91e2-b4ca24479986
https://portal.findresearcher.sdu.dk/da/publications/e9798d3b-a927-43a3-91e2-b4ca24479986
Publikováno v:
Proteins
Proteins, 2017, 85 (8), pp.1413-1421. ⟨10.1002/prot.25301⟩
Proteins, 2017, 85 (8), pp.1413-1421. ⟨10.1002/prot.25301⟩
Aminopeptidases are ubiquitous hydrolases that cleave the N-terminal residues of proteins and oligopeptides. They are broadly distributed throughout all kingdoms of life and have been implicated in a wide variety of physiological processes, including
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::994ef31d4e1a5848d744de518bf2f2ff
https://hal.archives-ouvertes.fr/hal-02161625
https://hal.archives-ouvertes.fr/hal-02161625
Autor:
Ekegren, Jenny
Diss. (sammanfattning) Uppsala : Uppsala universitet, 2006.
Härtill 4 uppsatser.
Härtill 4 uppsatser.
Externí odkaz:
http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-6737
Autor:
Arnaud Blondel, Técio G Benetti-Barbosa, Paulo R. Batista, Paulo Mascarello Bisch, Mauricio G. S. Costa, Nathan Desdouits, Pedro G. Pascutti
Publikováno v:
BMC Genomics
BMC Genomics, 2014, 15 (Suppl 7), pp.S5. ⟨10.1186/1471-2164-15-S7-S5⟩
BMC Genomics, BioMed Central, 2014, 15 (Suppl 7), pp.S5. ⟨10.1186/1471-2164-15-S7-S5⟩
BMC Genomics, 2014, 15 (Suppl 7), pp.S5. ⟨10.1186/1471-2164-15-S7-S5⟩
BMC Genomics, BioMed Central, 2014, 15 (Suppl 7), pp.S5. ⟨10.1186/1471-2164-15-S7-S5⟩
Background Over the last decades, a vast structural knowledge has been gathered on the HIV-1 protease (PR). Noticeably, most of the studies focused the B-subtype, which has the highest prevalence in developed countries. Accordingly, currently availab