Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Cristina M. Viola"'
Autor:
Cristina M. Viola, Orsolya Frittmann, Huw T. Jenkins, Talha Shafi, Pierre De Meyts, Andrzej M. Brzozowski
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-13 (2023)
Abstract The insulin-related hormones regulate key life processes in Metazoa, from metabolism to growth, lifespan and aging, through an evolutionarily conserved insulin signalling axis (IIS). In humans the IIS axis is controlled by insulin, two insul
Externí odkaz:
https://doaj.org/article/05681134f42944749a2e698a554ca573
Autor:
Nikolaj Kulahin Roed, Cristina M. Viola, Ole Kristensen, Gerd Schluckebier, Mathias Norrman, Waseem Sajid, John D. Wade, Asser Sloth Andersen, Claus Kristensen, Timothy R. Ganderton, Johan P. Turkenburg, Pierre De Meyts, Andrzej M. Brzozowski
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-12 (2018)
Insulin-like polypeptide binding proteins (IBPs) from insects can bind diverse insulin-like proteins (ILPs) including human insulin and IGFs. Here, the authors present structures of a Drosophila IBP in its free and ILP-bound forms, providing insights
Externí odkaz:
https://doaj.org/article/ab49da7df68b46db823e2dfac264e41c
Autor:
Petr Pompach, Cristina M. Viola, Jelena Radosavljević, Jingjing Lin, Jiří Jiráček, Andrzej M. Brzozowski, Irena Selicharová
Publikováno v:
Frontiers in Endocrinology, Vol 10 (2019)
Structural details of changes accompanying interaction between insulin-related hormones and their binding partners are often enigmatic. Here, cross-linking/mass spectrometry could complement structural techniques and reveal details of these protein-p
Externí odkaz:
https://doaj.org/article/4bd794a741d7415cb3a66a17b4584e79
Autor:
Cristina M. Viola, Jiří Jiráček, Irena Selicharová, Jelena Radosavljević, Andrzej M. Brzozowski, Jingjing Lin, Petr Pompach
Publikováno v:
Frontiers in Endocrinology, Vol 10 (2019)
Frontiers in Endocrinology
Frontiers in Endocrinology
Structural details of changes accompanying interaction between insulin-related hormones and their binding partners are often enigmatic. Here, cross-linking/mass spectrometry could complement structural techniques and reveal details of these protein-p
Autor:
Pavel Jungwirth, Tim Ganderton, Vladimír Palivec, Cristina M. Viola, Elise Duboué-Dijon, Tomáš Křížek, Andrzej M. Brzozowski, Kryštof Březina, Jiří Jiráček
Publikováno v:
Journal of Physical Chemistry B
Journal of Physical Chemistry B, American Chemical Society, 2018, 122 (44), pp.10069-10076. ⟨10.1021/acs.jpcb.8b06557⟩
Journal of Physical Chemistry B, American Chemical Society, 2018, 122 (44), pp.10069-10076. ⟨10.1021/acs.jpcb.8b06557⟩
The oligomeric state of the storage form of human insulin in pancreas, which may be affected by several endogenous components of beta-cells storage granules such as arginine, is not known. Here, the effect of arginine on insulin oligomerisation is in
Publikováno v:
Nature structural & molecular biology
Heparan sulfate (HS) is a glycosaminoglycan that forms a key component of the extracellular matrix (ECM). Breakdown of HS is carried out by heparanase (HPSE), an endo-β-glucuronidase of the glycoside hydrolase 79 (GH79) family. Overexpression of HPS
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 54:166-169
Publikováno v:
Nature Structural & Molecular Biology. 23:91-91
Corrigendum: Structural characterization of human heparanase reveals insights into substrate recognition
Publikováno v:
Proteins; Jan2004, Vol. 54 Issue 1, p166-169, 4p