Zobrazeno 1 - 10
of 100
pro vyhledávání: '"Kaspar P, Locher"'
Autor:
Hongtao Liu, Dariusz Zakrzewicz, Kamil Nosol, Rossitza N. Irobalieva, Somnath Mukherjee, Rose Bang-Sørensen, Nora Goldmann, Sebastian Kunz, Lorenzo Rossi, Anthony A. Kossiakoff, Stephan Urban, Dieter Glebe, Joachim Geyer, Kaspar P. Locher
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-13 (2024)
Abstract Cellular entry of the hepatitis B and D viruses (HBV/HDV) requires binding of the viral surface polypeptide preS1 to the hepatobiliary transporter Na+-taurocholate co-transporting polypeptide (NTCP). This interaction can be blocked by bulevi
Externí odkaz:
https://doaj.org/article/f9ddf8c868954a5d843a6783bfb948e5
Autor:
Hongtao Liu, Rossitza N. Irobalieva, Julia Kowal, Dongchun Ni, Kamil Nosol, Rose Bang-Sørensen, Loïck Lancien, Henning Stahlberg, Bruno Stieger, Kaspar P. Locher
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-12 (2023)
Abstract BSEP (ABCB11) is an ATP-binding cassette transporter that is expressed in hepatocytes and extrudes bile salts into the canaliculi of the liver. BSEP dysfunction, caused by mutations or induced by drugs, is frequently associated with severe c
Externí odkaz:
https://doaj.org/article/93dab7cac18e4944ab60824ac944966c
Autor:
Anca-Denise Ciută, Kamil Nosol, Julia Kowal, Somnath Mukherjee, Ana S. Ramírez, Bruno Stieger, Anthony A. Kossiakoff, Kaspar P. Locher
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-13 (2023)
Abstract The organic anion transporting polypeptides OATP1B1 and OATP1B3 are membrane proteins that mediate uptake of drugs into the liver for subsequent conjugation and biliary excretion, a key step in drug elimination from the human body. Polymorph
Externí odkaz:
https://doaj.org/article/c4fbcf5a03ec431db295fe4ed7798bc0
Autor:
Ana S. Ramírez, Mario de Capitani, Giorgio Pesciullesi, Julia Kowal, Joël S. Bloch, Rossitza N. Irobalieva, Jean-Louis Reymond, Markus Aebi, Kaspar P. Locher
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-12 (2022)
Oligosaccharyltransferase (OST), the central enzyme in N-glycosylation, modifies acceptor proteins by attaching a complex glycan. Cryo-EM structures of OST in distinct states, reveal the molecular basis of substrate recognition and catalysis.
Externí odkaz:
https://doaj.org/article/43b2b3330caf4ca4bdb47a82b87d0d0f
Autor:
Qin Yu, Dongchun Ni, Julia Kowal, Ioannis Manolaridis, Scott M. Jackson, Henning Stahlberg, Kaspar P. Locher
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
ABCG2 is a transporter contributing to multidrug resistance of cancer cells. Here, structures of human ABCG2 under turnover conditions reveal distinct conformational states, provide insight into the transport cycle and suggest a mechanism of discrimi
Externí odkaz:
https://doaj.org/article/f3dae0a3a07a42eb9d31262f294b2505
Autor:
Ana S. Ramírez, Jérémy Boilevin, Ahmad Reza Mehdipour, Gerhard Hummer, Tamis Darbre, Jean-Louis Reymond, Kaspar P. Locher
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-11 (2018)
The glycosyltransferase PglH transfers three terminal N-acetylgalactosamine (GalNAc) residues to a carrier, which is a prerequisite for bacterial protein N-glycosylation. Here authors present the crystal structures of PglH in three distinct states an
Externí odkaz:
https://doaj.org/article/02fd06bf76d44363ac10479a0e87396b
Autor:
Amer Alam, Jae-Sung Woo, Jennifer Schmitz, Bernadette Prinz, Katharina Root, Fan Chen, Joël S. Bloch, Renato Zenobi, Kaspar P. Locher
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-9 (2016)
Cellular uptake of vitamin B12 (cobalamin) requires the binding of holo-transcobalamin (TC) from plasma by CD320. Here, the authors report the structure of a complex between CD320 and TC loaded with cyanocobalamin, alongside additional functional ana
Externí odkaz:
https://doaj.org/article/f7968f92215d4073a761f286014aedaa
Autor:
Mario M. de Capitani, Ana S. Ramírez, Lorenzo Rossi, J. Andrew N. Alexander, Sabrina De Lorenzo, Kaspar P. Locher, Jean-Louis Reymond
Publikováno v:
Tetrahedron, 136
Herein we report the synthesis of two fluorescently labelled analogues of C25 dolichol (Dol25) in which the terminal isoprene unit has been replaced by a dansyl or 7-amino-4-trifluoromethylcoumarin fluorophore, a transformation enabled by the regiose
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ca2561d425f081e1c320643867aecac2
Autor:
Joël S. Bloch, Alan John, Runyu Mao, Somnath Mukherjee, Jérémy Boilevin, Rossitza N. Irobalieva, Tamis Darbre, Nichollas E. Scott, Jean-Louis Reymond, Anthony A. Kossiakoff, Ethan D. Goddard-Borger, Kaspar P. Locher
Publikováno v:
Bloch, Joël S; John, Alan; Mao, Runyu; Mukherjee, Somnath; Boilevin, Jérémy; Irobalieva, Rossitza N; Darbre, Tamis; Scott, Nichollas E; Reymond, Jean-Louis; Kossiakoff, Anthony A; Goddard-Borger, Ethan D; Locher, Kaspar P (2023). Structure, sequon recognition and mechanism of tryptophan C-mannosyltransferase. Nature chemical biology, 19(5), pp. 575-584. Springer Nature 10.1038/s41589-022-01219-9
Nature Chemical Biology, 19 (5)
Nature Chemical Biology, 19 (5)
C-linked glycosylation is essential for the trafficking, folding and function of secretory and transmembrane proteins involved in cellular communication processes. The tryptophan C-mannosyltransferase (CMT) enzymes that install the modification attac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3b3befc530922426b9dd0cdfdbc85a20
Publikováno v:
PLoS ONE, Vol 12, Iss 9, p e0184932 (2017)
Vitamin B12 (cyanocobalamin, CNCbl) is an essential cofactor-precursor for two biochemical reactions in humans. When ingested, cobalamins (Cbl) are transported via a multistep transport system into the bloodstream, where the soluble protein transcoba
Externí odkaz:
https://doaj.org/article/e49b37b0f87c4ea392b7b2068a5a3426