Zobrazeno 1 - 10
of 26
pro vyhledávání: '"M Kristian, Koski"'
Publikováno v:
Scientific Reports, Vol 14, Iss 1, Pp 1-11 (2024)
Abstract Fibulin-2 is a multidomain, disulfide-rich, homodimeric protein which belongs to a broader extracellular matrix family. It plays an important role in the development of elastic fiber structures. Malfunction of fibulin due to mutation or poor
Externí odkaz:
https://doaj.org/article/07b6c39d37bc4aaba300f8dc23304b3f
Autor:
M. Tanvir Rahman, M. Kristian Koski, Joanna Panecka-Hofman, Werner Schmitz, Alexander J. Kastaniotis, Rebecca C. Wade, Rik K. Wierenga, J. Kalervo Hiltunen, Kaija J. Autio
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-15 (2023)
Abstract Mitochondrial fatty acid synthesis (mtFAS) is essential for respiratory function. MtFAS generates the octanoic acid precursor for lipoic acid synthesis, but the role of longer fatty acid products has remained unclear. The structurally well-c
Externí odkaz:
https://doaj.org/article/d16d0b2bf48f43899654c6293ec0c770
Autor:
Abhinandan V, Murthy, Ramita, Sulu, Andrey, Lebedev, Antti M, Salo, Kati, Korhonen, Rajaram, Venkatesan, Hongmin, Tu, Ulrich, Bergmann, Janne, Jänis, Mikko, Laitaoja, Lloyd W, Ruddock, Johanna, Myllyharju, M Kristian, Koski, Rik K, Wierenga
Publikováno v:
The Journal of biological chemistry. 298(12)
Collagen prolyl 4-hydroxylases (C-P4H) are α
Publikováno v:
Amino Acids. 52:619-627
The trimeric transmembrane collagen BP180, also known as collagen XVII, is an essential component of hemidesmosomes at the dermal–epidermal junction and connects the cytoplasmic keratin network to the extracellular basement membrane. Dysfunction of
Autor:
Alun W. Ashton, Neil Smith, Subhadra Dalwani, Ekaterina Biterova, Joel L. Sussman, M. Kristian Koski, Tiila Riikka Kiema, Sudarshan Murthy, Shruthi Sridhar, Ville Ratas, Lari Lehtiö, Rajaram Venkatesan, Ed Daniel, Mahbubur Rahman, Mirko M. Maksimainen, Jaime Prilusky, Rik K. Wierenga, Gabriele Cordara, Orly Dym
Publikováno v:
Acta Crystallographica. Section D, Structural Biology
The IceBear web application for monitoring and recording the results of crystallization experiments is introduced. This software includes tools for interacting directly with the ISPyB synchrotron database: metadata from shipped crystals can be upload
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4c0ea95486fbf4e30db4fcf4571e9b51
http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-455593
http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-455593
Akademický článek
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Publikováno v:
Protein Science. 25:987-998
The type III secretion system (T3SS) is required for the virulence of many gram-negative bacterial human pathogens. It is composed of several structural proteins, forming the secretion needle and its basis, the basal body. In Chlamydia spp., the T3SS
Autor:
Aleksi Sutinen, M. Kristian Koski, Johanna Myllyharju, Juha P. Kallio, Rik K. Wierenga, Peppi Koivunen, Arne Raasakka, Matti Myllykoski
Publikováno v:
Journal of Biological Chemistry
The Journal of Biological Chemistry
The journal of biological chemistry 296, 100197 (2021). doi:10.1074/jbc.RA120.016542
The Journal of Biological Chemistry
The journal of biological chemistry 296, 100197 (2021). doi:10.1074/jbc.RA120.016542
The journal of biological chemistry 296, 100197 (2021). doi:10.1074/jbc.RA120.016542
Prolyl 4-hydroxylases (P4Hs) catalyze post-translational hydroxylation of peptidyl proline residues. In addition to collagen P4Hs and hypoxia-inducible factor P
Prolyl 4-hydroxylases (P4Hs) catalyze post-translational hydroxylation of peptidyl proline residues. In addition to collagen P4Hs and hypoxia-inducible factor P
Publikováno v:
The FEBS Journal. 282:746-768
The catalytic domain of the trimeric human Δ(3),Δ(2)-enoyl-CoA isomerase, type 2 (HsECI2), has the typical crotonase fold. In the active site of this fold two main chain NH groups form an oxyanion hole for binding the thioester oxygen of the 3E- or
Autor:
J. Anantharajan, Petri Kursula, Johanna Myllyharju, Ulrich Bergmann, Rik K. Wierenga, Reija Hieta, M. Kristian Koski
Publikováno v:
Structure 21(12), 2107-2118 (2013). doi:10.1016/j.str.2013.09.005
Structure 21(12), 2107 - 2118 (2013). doi:10.1016/j.str.2013.09.005
Published by Elsevier Science, London [u.a.]
Published by Elsevier Science, London [u.a.]