Zobrazeno 1 - 10
of 103
pro vyhledávání: '"Janet Finer-Moore"'
Autor:
Hemant Kumar, Janet Finer-Moore, Irina Smirnova, Vladimir Kasho, Els Pardon, Jan Steyaert, H Ronald Kaback, Robert M Stroud
Publikováno v:
PLoS ONE, Vol 15, Iss 5, p e0232846 (2020)
The structure of lactose permease, stabilized in a periplasmic open conformation by two Gly to Trp replacements (LacYww) and complexed with a nanobody directed against this conformation, provides the highest resolution structure of the symporter. The
Externí odkaz:
https://doaj.org/article/676111b34599439695d95acf5299468e
Autor:
Sun Kyung Kim, Miles Sasha Dickinson, Janet Finer-Moore, Ziqiang Guan, Robyn M. Kaake, Ignacia Echeverria, Jen Chen, Ernst H. Pulido, Andrej Sali, Nevan J. Krogan, Oren S. Rosenberg, Robert M. Stroud
Publikováno v:
bioRxiv
SummaryMycobacterium tuberculosisis currently the leading cause of death by any bacterial infection1. The mycolic acid layer of the cell wall is essential for viability and virulence, and the enzymes responsible for its synthesis are therefore front
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::12b1a1820c2b376477cbd4460387228e
https://doi.org/10.1101/2023.01.27.525930
https://doi.org/10.1101/2023.01.27.525930
Autor:
Fei Li, Jacob Eriksen, Juan A. Oses-Prieto, Yessica K. Gomez, Hongfei Xu, Janet Finer-Moore, Phuong Nguyen, Alisa Bowen, Andrew Nelson, Alma Burlingame, Michael Grabe, Robert M. Stroud, Robert H. Edwards
Concentration of neurotransmitter inside synaptic vesicles (SVs) underlies the quantal nature of synaptic transmission. In contrast to many transporters, SV uptake of the principal excitatory neurotransmitter glutamate is driven by membrane potential
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::15833a188380fd3b371e447d3f205db6
https://doi.org/10.1101/2022.07.26.501550
https://doi.org/10.1101/2022.07.26.501550
Publikováno v:
Curr Opin Struct Biol
Originally identified as transporters for inorganic phosphate, solute carrier 17 (SLC17) family proteins subserve diverse physiological roles. The vesicular glutamate transporters (VGLUTs) package the principal excitatory neurotransmitter glutamate i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0d31672b9dccb91b88c58f8d1d968cba
https://europepmc.org/articles/PMC9884543/
https://europepmc.org/articles/PMC9884543/
Autor:
Amnon Kohen, Kemel Arafet, Vicent Moliner, Robert M. Stroud, Janet Finer-Moore, Katarzyna Świderek, Svetlana A. Kholodar
Publikováno v:
Repositori Universitat Jaume I
Universitat Jaume I
Universitat Jaume I
Methylation of 2-deoxyuridine-5′-monophosphate (dUMP) at the C5 position by the obligate dimeric thymidylate synthase (TSase) in the sole de novo biosynthetic pathway to thymidine 5′-monophosphate (dTMP) proceeds by forming a covalent ternary com
Publikováno v:
Biophysical Journal. 121:342a
Autor:
Alisa Bowen, Alexander G. Myasnikov, Phuong Nguyen, Roger Chang, David Bulkley, Robert H. Edwards, Janet Finer-Moore, Fei Li, Zanlin Yu, Robert M. Stroud, Yifan Cheng, Jacob Eriksen
Publikováno v:
Science
Transport dependent on context Transporter proteins move substrates across a membrane, often coupling this activity to cellular ion concentration gradients. For neurotransmitter transporters, which reside in synaptic vesicles that fuse with the plasm
Autor:
Els Pardon, H. Ronald Kaback, Robert M. Stroud, Vladimir N. Kasho, Hemant Kumar, Janet Finer-Moore, Irina Smirnova, Jan Steyaert
Publikováno v:
PloS one, vol 15, iss 5
PLoS ONE, Vol 15, Iss 5, p e0232846 (2020)
PLoS ONE
PLoS ONE, Vol 15, Iss 5, p e0232846 (2020)
PLoS ONE
Funder: research foundation-flanders
The structure of lactose permease, stabilized in a periplasmic open conformation by two Gly to Trp replacements (LacYww) and complexed with a nanobody directed against this conformation, provides the highest
The structure of lactose permease, stabilized in a periplasmic open conformation by two Gly to Trp replacements (LacYww) and complexed with a nanobody directed against this conformation, provides the highest
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d5b32a2fde5658007e7e83fbed41f0c4
https://escholarship.org/uc/item/36t656kj
https://escholarship.org/uc/item/36t656kj
Autor:
Irina Smirnova, H. Ronald Kaback, Xiaoxu Jiang, Els Pardon, Robert M. Stroud, Jan Steyaert, Vladimir N. Kasho, Janet Finer-Moore, Hemant Kumar
Publikováno v:
Proceedings of the National Academy of Sciences. 115:8769-8774
The lactose permease of Escherichia coli (LacY), a dynamic polytopic membrane transport protein, catalyzes galactoside/H(+) symport and operates by an alternating access mechanism that exhibits multiple conformations, the distribution of which is alt
Publikováno v:
Biochemistry, vol 57, iss 19
In Escherichia coli thymidylate synthase (EcTS), rate-determining hydride transfer from the cofactor 5,10-methylene-5,6,7,8-tetrahydrofolate to the intermediate 5-methylene-2'-deoxyuridine 5'-monophosphate occurs by hydrogen tunneling, requiring prec