Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Pearl Magala"'
Autor:
Dagmara I Kisiela, Pearl Magala, Gianluca Interlandi, Laura A Carlucci, Angelo Ramos, Veronika Tchesnokova, Benjamin Basanta, Vladimir Yarov-Yarovoy, Hovhannes Avagyan, Anahit Hovhannisyan, Wendy E Thomas, Ronald E Stenkamp, Rachel E Klevit, Evgeni V Sokurenko
Publikováno v:
PLoS Pathogens, Vol 17, Iss 4, p e1009440 (2021)
Critical molecular events that control conformational transitions in most allosteric proteins are ill-defined. The mannose-specific FimH protein of Escherichia coli is a prototypic bacterial adhesin that switches from an 'inactive' low-affinity state
Externí odkaz:
https://doaj.org/article/92724f2113474eaeae020cdd9e9e6a36
Publikováno v:
ACS Omega, Vol 2, Iss 8, Pp 4581-4592 (2017)
Externí odkaz:
https://doaj.org/article/69bac3c9029d49a6b0bd802ce0de035d
Autor:
Wendy E Thomas, Laura Carlucci, Olga Yakovenko, Gianluca Interlandi, Isolde Le Trong, Pavel Aprikian, Pearl Magala, Lydia Larson, Yulia Sledneva, Veronika Tchesnokova, Ronald E. Stenkamp, Evgeni V. Sokurenko
Publikováno v:
J Mol Biol
The FimH protein of Escherichia coli is a model two-domain adhesin that is able to mediate an allosteric catch bond mechanism of bacterial cell attachment, where the mannose-binding lectin domain switches from an ‘inactive’ conformation with fast
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::86e20b32e8724bc42cba3059516c33a2
https://doi.org/10.1016/j.jmb.2022.167681
https://doi.org/10.1016/j.jmb.2022.167681
Autor:
Hovhannes Avagyan, Rachel E. Klevit, Laura A. Carlucci, Evgeni V. Sokurenko, Benjamin Basanta, Dagmara I. Kisiela, Angelo Ramos, Wendy E. Thomas, Ronald E. Stenkamp, Pearl Magala, Veronika Tchesnokova, Vladimir Yarov-Yarovoy, Anahit Hovhannisyan, Gianluca Interlandi
Publikováno v:
PLoS pathogens, vol 17, iss 4
PLoS Pathogens, Vol 17, Iss 4, p e1009440 (2021)
PLoS Pathogens
PLoS Pathogens, Vol 17, Iss 4, p e1009440 (2021)
PLoS Pathogens
Critical molecular events that control conformational transitions in most allosteric proteins are ill-defined. The mannose-specific FimH protein of Escherichia coli is a prototypic bacterial adhesin that switches from an ‘inactive’ low-affinity s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::76213e01c3c0afb912f1ba322843b6b0
https://escholarship.org/uc/item/0j29f4b5
https://escholarship.org/uc/item/0j29f4b5
Publikováno v:
Proteins
FimH is a bacterial adhesin protein located at the tip of Escherichia coli fimbria that functions to adhere bacteria to host cells. Thus, FimH is a critical factor in bacterial infections such as urinary tract infections and is of interest in drug de
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6c9a38d05a2b9a1135cc25d3e7fd5ad1
https://pubmed.ncbi.nlm.nih.gov/31622514
https://pubmed.ncbi.nlm.nih.gov/31622514
Autor:
Cynthia Wolberger, Joel R. Tolman, Pearl Magala, Pankaj Kumar, Kathryn Geiger-Schuller, Ananya Majumdar
Publikováno v:
Nucleic Acids Research
Rad6 is a yeast E2 ubiquitin conjugating enzyme that monoubiquitinates histone H2B in conjunction with the E3, Bre1, but can non-specifically modify histones on its own. We determined the crystal structure of a Rad6∼Ub thioester mimic, which reveal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8217475feeabea2a04e631679131956b
https://doi.org/10.1093/nar/gkv845
https://doi.org/10.1093/nar/gkv845
Publikováno v:
ACS Omega
ACS Omega, Vol 2, Iss 8, Pp 4581-4592 (2017)
ACS Omega, Vol 2, Iss 8, Pp 4581-4592 (2017)
The ubiquitin conjugating enzyme Ube2g2 together with its cognate E3 ligase gp78 catalyzes the synthesis of lysine-48 polyubiquitin chains constituting signals for the proteasomal degradation of misfolded proteins in the endoplasmic reticulum. Here,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc90487e99ada0b0671af80cbeb8de69
https://pubmed.ncbi.nlm.nih.gov/28884161
https://pubmed.ncbi.nlm.nih.gov/28884161