Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Jennifer Virginia Roche"'
Autor:
Louise Hamborg, Daniele Granata, Johan G. Olsen, Jennifer Virginia Roche, Lasse Ebdrup Pedersen, Alex Toftgaard Nielsen, Kresten Lindorff-Larsen, Kaare Teilum
Publikováno v:
Communications Biology, Vol 4, Iss 1, Pp 1-9 (2021)
Louise Hamborg et al. use a cell-based screen in E. coli to look for mutants of chymotrypsin inhibitor 2 which are either destabilized or stabilized, in an effort to identify a larger library of mutants which might improve stability prediction. Their
Externí odkaz:
https://doaj.org/article/e62f07713f7946109276026a00012c4c
Autor:
Louise Hamborg, Daniele Granata, Johan G. Olsen, Jennifer Virginia Roche, Lasse Ebdrup Pedersen, Alex Toftgaard Nielsen, Kresten Lindorff-Larsen, Kaare Teilum
Most single point mutations destabilize folded proteins. Mutations that stabilize a protein typically only have a small effect and multiple mutations are often needed to substantially increase the stability. Multiple point mutations may act synergist
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d80f96658819d0ba1226c0df22793147
https://doi.org/10.1101/2020.12.01.406082
https://doi.org/10.1101/2020.12.01.406082
Autor:
Sabeen Survery, Maria Gourdon, Peter M.T. Deen, Henry Ampah-Korsah, Veronika Nesverova, Susanna Törnroth-Horsefield, Jennifer Virginia Roche, Stefan Kreida
Publikováno v:
Journal of Biological Chemistry, 292, 14636-14648
Journal of Biological Chemistry, 292, 35, pp. 14636-14648
Journal of Biological Chemistry, 292, 35, pp. 14636-14648
Contains fulltext : 177875.pdf (Publisher’s version ) (Open Access) The interaction between the renal water channel aquaporin-2 (AQP2) and the lysosomal trafficking regulator-interacting protein LIP5 targets AQP2 to multivesicular bodies and facili
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bcacab8685436160ee42aa2dee50eaaf
https://hdl.handle.net/https://repository.ubn.ru.nl/handle/2066/177875
https://hdl.handle.net/https://repository.ubn.ru.nl/handle/2066/177875
Autor:
Jennifer Virginia Roche, Veronika Nesverova, Caroline Olsson, Peter M.T. Deen, Susanna Törnroth-Horsefield
Publikováno v:
International Journal of Molecular Sciences, Vol 20, Iss 21, p 5351 (2019)
International Journal of Molecular Sciences
International Journal of Molecular Sciences, 20
International Journal of Molecular Sciences, 20, 21
Volume 20
Issue 21
International Journal of Molecular Sciences
International Journal of Molecular Sciences, 20
International Journal of Molecular Sciences, 20, 21
Volume 20
Issue 21
Vasopressin-dependent trafficking of AQP2 in the renal collecting duct is crucial for the regulation of water homeostasis. This process involves the targeting of AQP2 to the apical membrane during dehydration as well as its removal when hydration lev
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e6ab472ed8e2a8d1f56efb688a151dd
https://doi.org/10.3390/ijms20215351
https://doi.org/10.3390/ijms20215351
Autor:
Sara Linse, Susanna Törnroth-Horsefield, Jennifer Virginia Roche, Caroline Olsson, Stefan Kreida
Publikováno v:
Faraday discussions. 209
Protein-protein interactions play important roles in regulating human aquaporins (AQP) by gating as well as trafficking. While structural and functional studies have provided detailed knowledge of AQP transport mechanisms, selectivity as well as gati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::402d8303ef59e73df593d5abe6279111
https://pubmed.ncbi.nlm.nih.gov/29972182
https://pubmed.ncbi.nlm.nih.gov/29972182
Publikováno v:
International Journal of Molecular Sciences
International Journal of Molecular Sciences, Vol 18, Iss 11, p 2255 (2017)
International Journal of Molecular Sciences, Vol 18, Iss 11, p 2255 (2017)
Aquaporins are tetrameric membrane-bound channels that facilitate transport of water and other small solutes across cell membranes. In eukaryotes, they are frequently regulated by gating or trafficking, allowing for the cell to control membrane perme
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5f607f25e73d706e1b409ad5b4d600c6
https://pubmed.ncbi.nlm.nih.gov/29077056
https://pubmed.ncbi.nlm.nih.gov/29077056