Zobrazeno 1 - 10
of 234
pro vyhledávání: '"H. Ronald Kaback"'
Autor:
Parameswaran Hariharan, Yuqi Shi, Satoshi Katsube, Katleen Willibal, Nathan D Burrows, Patrick Mitchell, Amirhossein Bakhtiiari, Samantha Stanfield, Els Pardon, H Ronald Kaback, Ruibin Liang, Jan Steyaert, Rosa Viner, Lan Guan
Publikováno v:
eLife, Vol 12 (2024)
While many 3D structures of cation-coupled transporters have been determined, the mechanistic details governing the obligatory coupling and functional regulations still remain elusive. The bacterial melibiose transporter (MelB) is a prototype of majo
Externí odkaz:
https://doaj.org/article/188cecb299784d0297390ce222ce9b14
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:
Satoshi Katsube, Katleen Willibal, Sangama Vemulapally, Parameswaran Hariharan, Elena Tikhonova, Els Pardon, H. Ronald Kaback, Jan Steyaert, Lan Guan
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a6e2540b81597c8ecbc4544bedc08df3
https://doi.org/10.2139/ssrn.4355089
https://doi.org/10.2139/ssrn.4355089
Publikováno v:
PLoS ONE, Vol 11, Iss 5, p e0156392 (2016)
Bacterial sugar symporters in the Major Facilitator Superfamily (MFS) use the H+ (and in a few cases Na+) electrochemical gradients to achieve active transport of sugar into the cell. Because a number of structures of MFS sugar symporters have been s
Externí odkaz:
https://doaj.org/article/1931cb7e20264ad9bc8500f26913829f
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, vol 117, iss 2
Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America
Significance Protonation and deprotonation of Glu325 with a pKa of 10.5 is required for symport. Moreover, the H+ electrochemical gradient (∆μ∼H+) accelerates deprotonation on the intracellular side with a 50- to 100-fold decrease in the Km. To
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::940092633e2c6c20ea87894a1b80321d
https://doi.org/10.1073/pnas.1916563117
https://doi.org/10.1073/pnas.1916563117
Publikováno v:
The Journal of Biological Chemistry
Bacterial transporters are difficult to study using conventional electrophysiology because of their low transport rates and the small size of bacterial cells. Here, we applied solid-supported membrane–based electrophysiology to derive kinetic param
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::173ab5f163d13e9c80e23eacd2a83eef
http://europepmc.org/articles/PMC8784342
http://europepmc.org/articles/PMC8784342
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2019, 116 (11), pp.4934-4939. ⟨10.1073/pnas.1820744116⟩
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2019, 116 (11), pp.4934-4939. ⟨10.1073/pnas.1820744116⟩
Significance The alkaline pK for galactoside binding by the lactose permease of Escherichia coli correlates precisely with the pK a of Glu325, as determined by reaction-induced surface-enhanced infrared absorption spectroscopy (SEIRAS). Glu325 must b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bdc2fba7852c204111a814557c212a12
https://doi.org/10.1073/pnas.1820744116
https://doi.org/10.1073/pnas.1820744116
Publikováno v:
FEBS Letters
FEBS Letters, Wiley, 2020, 594 (20), pp.3356-3362. ⟨10.1002/1873-3468.13907⟩
FEBS Letters, Wiley, 2020, 594 (20), pp.3356-3362. ⟨10.1002/1873-3468.13907⟩
The monoclonal antibody 4B1 binds to a conformational epitope on the periplasmic side of lactose permease (LacY) of Escherichia coli and inhibits H+ /lactose symport and lactose efflux under nonenergized conditions. At the same time, ligand binding a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ccc4757109f01e68be424da861a80836
https://hal.archives-ouvertes.fr/hal-03343107
https://hal.archives-ouvertes.fr/hal-03343107
Publikováno v:
FEBS lettersReferences. 594(20)
The monoclonal antibody 4B1 binds to a conformational epitope on the periplasmic side of lactose permease (LacY) of Escherichia coli and inhibits H
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::74c593627e8fc0c2c6ae2ac0b7878e53
https://pubmed.ncbi.nlm.nih.gov/32780424
https://pubmed.ncbi.nlm.nih.gov/32780424
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