Zobrazeno 1 - 10
of 109
pro vyhledávání: '"Oleg Y Dmitriev"'
Autor:
Natalia Dolgova, Eva-Maria E Uhlemann, Michal T Boniecki, Frederick S Vizeacoumar, Anjuman Ara, Paria Nouri, Martina Ralle, Marco Tonelli, Syed A Abbas, Jaala Patry, Hussain Elhasasna, Andrew Freywald, Franco J Vizeacoumar, Oleg Y Dmitriev
Publikováno v:
eLife, Vol 13 (2024)
Mediator of ERBB2-driven cell motility 1 (MEMO1) is an evolutionary conserved protein implicated in many biological processes; however, its primary molecular function remains unknown. Importantly, MEMO1 is overexpressed in many types of cancer and wa
Externí odkaz:
https://doaj.org/article/3f0c34f4546f414eb0c25d9910cef1a9
Autor:
Michael Pöhler, Sarah Guttmann, Oksana Nadzemova, Malte Lenders, Eva Brand, Andree Zibert, Hartmut H. Schmidt, Vanessa Sandfort, Oleg Y. Dmitriev
Publikováno v:
PLoS ONE, Vol 15, Iss 9 (2020)
Wilson's disease (WD) is a monogenetic liver disease that is based on a mutation of the ATP7B gene and leads to a functional deterioration in copper (Cu) excretion in the liver. The excess Cu accumulates in various organs such as the liver and brain.
Externí odkaz:
https://doaj.org/article/d2f80616f03c4820a600d9c5a8bb32f3
Autor:
Natalia Dolgova, Eva-Maria E. Uhlemann, Michal T. Boniecki, Frederick S. Vizeacoumar, Martina Ralle, Marco Tonelli, Syed A. Abbas, Jaala Patry, Hussain Elhasasna, Andrew Freywald, Franco J. Vizeacoumar, Oleg Y. Dmitriev
Mediator of ERBB2-driven Cell Motility 1 (MEMO1) is an evolutionary conserved protein implicated in many biological processes; however, its primary molecular function remains unknown. Importantly, MEMO1 is overexpressed in many types of cancer and wa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e9f6dff595e7e1ac42a51174cf73e82e
https://doi.org/10.1101/2023.02.28.530460
https://doi.org/10.1101/2023.02.28.530460
Autor:
Natalia Dolgova, Eva-Maria E. Uhlemann, Michal T. Boniecki, Frederick S. Vizeacoumar, Martina Ralle, Marco Tonelli, Syed A. Abbas, Jaala Patry, Hussain Elhasasna, Andrew Freywald, Franco J. Vizeacoumar, Oleg Y. Dmitriev
Publikováno v:
SSRN Electronic Journal.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::550aea57662ae694f0ce0651af05e38c
https://doi.org/10.2139/ssrn.4084075
https://doi.org/10.2139/ssrn.4084075
At sixes and sevens: cryptic domain in the metal binding chain of the human copper transporter ATP7A
Publikováno v:
Biophys J
ATP7A and ATP7B are structurally similar but functionally distinct active copper transporters that regulate copper levels in the human cells and deliver copper to the biosynthetic pathways. Both proteins have a chain of six cytosolic metal-binding do
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b30beb4d644aa4920090fc2a2358b646
https://europepmc.org/articles/PMC8553599/
https://europepmc.org/articles/PMC8553599/
Nanobodies against the metal binding domains of ATP7B as tools to study copper transport in the cell
Autor:
Jaala Patry, Serge Muyldermans, Eva Maria E. Uhlemann, Svetlana Lutsenko, Oleg Y. Dmitriev, Corey H. Yu, Natalia V. Dolgova
Publikováno v:
Metallomics : integrated biometal science. 12(12)
Nanobodies are genetically engineered single domain antibodies derived from the unusual heavy-chain only antibodies found in llamas and camels. The small size of the nanobodies and flexible selection schemes make them uniquely versatile tools for pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::40ec40f6d9f70d969ffbd43410c2a26f
https://pubmed.ncbi.nlm.nih.gov/33094790
https://pubmed.ncbi.nlm.nih.gov/33094790
Autor:
Yuliang Wu, Anthony Kusalik, Oleg Y. Dmitriev, Daniel J. Hogan, Manisha Yadav, Miroslaw Cygler, Shizhuo Yang, Venkatasubramanian Vidhyasagar, Ivy Yeuk Wah Chung, Ravi Shankar Singh
Publikováno v:
The Journal of Biological Chemistry
The K-homology (KH) domain is a nucleic acid–binding domain present in many proteins. Recently, we found that the DEAD-box helicase DDX43 contains a KH domain in its N-terminus; however, its function remains unknown. Here, we purified recombinant D
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98c0590cfc7d941ddd4693dd73165b67
https://pubmed.ncbi.nlm.nih.gov/33199368
https://pubmed.ncbi.nlm.nih.gov/33199368
Autor:
Hannah E. Pierson, Christopher O’Grady, Mandeep Kaler, Oleg Y. Dmitriev, Eva Maria E. Uhlemann
Publikováno v:
Scientific Reports, Vol 8, Iss 1, Pp 1-8 (2018)
Scientific Reports
Scientific Reports
ATP synthase is powered by the flow of protons through the molecular turbine composed of two α-helical integral membrane proteins, subunit a, which makes a stator, and a cylindrical rotor assembly made of multiple copies of subunit c. Transient prot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f582a839812edc500b5b7f45f8a5140
http://link.springer.com/article/10.1038/s41598-018-29693-z
http://link.springer.com/article/10.1038/s41598-018-29693-z
Autor:
Svetlana Lutsenko, Sergiy Nokhrin, Lelita T. Braiterman, Jameson R. Bothe, Marco Tonelli, Oleg Y. Dmitriev, Nan Yang, Corey H. Yu, Natalia V. Dolgova
Publikováno v:
Journal of Biological Chemistry. 292:18169-18177
The human transporter ATP7B delivers copper to the biosynthetic pathways and maintains copper homeostasis in the liver. Mutations in ATP7B cause the potentially fatal hepatoneurological disorder Wilson disease. The activity and intracellular localiza
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8f62c943dae8d1a2fdb89ba7417ed5fe
https://doi.org/10.1074/jbc.m117.811752
https://doi.org/10.1074/jbc.m117.811752
The copper-transporting ATPase ATP7B (Wilson ATPase) is a large trans-membrane protein with a complex multidomain architecture. ATP7B uses the subset of these domains to hydrolyze adenosine triphosphate (ATP) and to couple ATP hydrolysis with the tra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f6ebca51f849b3c0d75bcd4a34e84511
https://doi.org/10.1016/b978-0-12-810532-0.00005-7
https://doi.org/10.1016/b978-0-12-810532-0.00005-7