Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Klaudia Szeler"'
Autor:
Kesava-Phaneendra Cherukuri, Misha Soskine, Dan S. Tawfik, Shina Caroline Lynn Kamerlin, Joel L. Sussman, Qinghua Liao, Klaudia Szeler, Orly Dym, Moshe Ben-David, Artem Dubovetskyi
Publikováno v:
'Molecular Biology and Evolution ', vol: 37, pages: 1133–1147 (2020)
Evolutionary trajectories are deemed largely irreversible. In a newly diverged protein, reversion of mutations that led to the functional switch typically results in loss of both the new and the ancestral functions. Nonetheless, evolutionary transiti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fd34e8fba5473a2ea01c78abf410bf7f
https://pubmed.ncbi.nlm.nih.gov/31873734
https://pubmed.ncbi.nlm.nih.gov/31873734
Autor:
Moshe Ben-David, David Blaha-Nelson, Klaudia Szeler, Dennis M. Krüger, Shina Caroline Lynn Kamerlin
Publikováno v:
Journal of the American Chemical Society
Serum paraoxonase 1 (PON1) is a native lactonase capable of promiscuously hydrolyzing a broad range of substrates, including organophosphates, esters, and carbonates. Structurally, PON1 is a six-bladed beta-propeller with a flexible loop (residues 70
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::76d389f50ac7396f3ff088a9cfc744ef
https://doi.org/10.1021/jacs.6b10801
https://doi.org/10.1021/jacs.6b10801
Phosphate ester hydrolysis is fundamental to many life processes, and has been the topic of substantial experimental and computational research effort. However, even the simplest of phosphate esters can be hydrolyzed through multiple possible pathway
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e930e05ed10e9589e2f2edddd5739dd0
http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-340612
http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-340612
Autor:
Joel L. Sussman, Dan S. Tawfik, Shina Caroline Lynn Kamerlin, Christopher I. Maxwell, Klaudia Szeler, Moshe Ben-David
Publikováno v:
Journal of Molecular Biology. 427:1359-1374
Despite the abundance of membrane-associated enzymes, the mechanism by which membrane binding stabilizes these enzymes and stimulates their catalysis remains largely unknown. Serum paraoxonase-1 (PON1) is a lipophilic lactonase whose stability and en
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0589fb1da0f45ffa7d17d74be28d0965
https://doi.org/10.1016/j.jmb.2015.01.013
https://doi.org/10.1016/j.jmb.2015.01.013
Publikováno v:
Chemical science. 7(2)
DERA, 2-deoxyribose-5-phosphate aldolase, catalyzes the retro-aldol cleavage of 2-deoxy-ribose-5-phosphate (dR5P) into glyceraldehyde-3-phosphate (G3P) and acetaldehyde in a branch of the pentose phosphate pathway. In addition to the physiological re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::23459b50651fbcd6584c6671ad5dfc44
https://pubmed.ncbi.nlm.nih.gov/29910900
https://pubmed.ncbi.nlm.nih.gov/29910900
Autor:
Alexandra T. P. Carvalho, Klaudia Szeler, Konstantinos Vavitsas, Shina Caroline Lynn Kamerlin, Johan Åqvist
Publikováno v:
Archives of Biochemistry and Biophysics. :80-90
Enzymes that hydrolyze GTP are currently in the spotlight, due to their molecular switch mechanism that controls many cellular processes. One of the best-known classes of these enzymes are small GTPases such as members of the Ras superfamily, which c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::575640b64f2ca7035b669c2da373d8d9