Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Katherine R. Kemplen"'
Autor:
Karen Skriver, Michael Ploug, Amelie Stein, Birthe B. Kragelund, Katherine R. Kemplen, Jane Clarke, Pétur O. Heidarsson, Lasse Staby
Publikováno v:
Staby, L, Kemplen, K R, Stein, A, Ploug, M, Clarke, J, Skriver, K, Heidarsson, P O & Kragelund, B B 2021, ' Disorder in a two-domain neuronal Ca 2+-binding protein regulates domain stability and dynamics using ligand mimicry ', Cellular and molecular life sciences : CMLS, vol. 78, pp. 2263-2278 . https://doi.org/10.1007/s00018-020-03639-z
Cellular and Molecular Life Sciences
Cellular and Molecular Life Sciences
Funder: Lundbeckfonden; doi: http://dx.doi.org/10.13039/501100003554
Funder: Villum Fonden (DK)
Understanding the interplay between sequence, structure and function of proteins has been complicated in recent years by the discovery of intrin
Funder: Villum Fonden (DK)
Understanding the interplay between sequence, structure and function of proteins has been complicated in recent years by the discovery of intrin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::82478c8a92daae4d85864bac2fbd3fb6
https://www.repository.cam.ac.uk/handle/1810/318856
https://www.repository.cam.ac.uk/handle/1810/318856
Autor:
Katherine R. Kemplen, Charlotte O'Shea, Johan G. Olsen, Katrine Bugge, Karen Skriver, Lasse Staby, Sidsel Krogh Bendsen, Mikael Kryger Jensen, Birthe B. Kragelund
Publikováno v:
Structure (London, England : 1993). 26(5)
Summary Communication within cells relies on a few protein nodes called hubs, which organize vast interactomes with many partners. Frequently, hub proteins are intrinsically disordered conferring multi-specificity and dynamic communication. Conversel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f310087a1b277a4e0e88079c54684f7c
https://pubmed.ncbi.nlm.nih.gov/29657132
https://pubmed.ncbi.nlm.nih.gov/29657132
Autor:
Alessandro Borgia, Robert B. Best, Bengt Wunderlich, Jane Clarke, Benjamin Schuler, Madeleine B. Borgia, Andrea Soranno, Daniel Nettels, Katherine R. Kemplen
Publikováno v:
ResearcherID
The covalently linked domains constituting a multidomain protein typically share a similar fold and sequence, are generally stable in isolation, and are largely capable of independent folding. However, the elegant interplay of forces leading an amino
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3fc2c2e19298c1dc06c24abb0befe065
Autor:
Yasushi Kondo, Jane Clarke, Tina Perica, Xiuwei Zhang, Annette Steward, Sarah A. Teichmann, Sandhya Premnath Tiwari, Katherine R. Kemplen, Nathalie Reuter, Stephen H. McLaughlin
Publikováno v:
Science
Introduction Evolution and design of protein complexes are frequently viewed through the lens of amino acid mutations at protein interfaces, but we showed previously that residues distant from interfaces are also commonly involved in the evolution of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7797c99d360d60eb5e5090d08e429b7c
https://www.repository.cam.ac.uk/handle/1810/246409
https://www.repository.cam.ac.uk/handle/1810/246409