Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Snehal Jadey"'
Autor:
Matthew B Tessier, Oliver C Grant, Jamie Heimburg-Molinaro, David Smith, Snehal Jadey, Andrew M Gulick, John Glushka, Susan L Deutscher, Kate Rittenhouse-Olson, Robert J Woods
Publikováno v:
PLoS ONE, Vol 8, Iss 1, p e54874 (2013)
Recombinant antibodies are of profound clinical significance; yet, anti-carbohydrate antibodies are prone to undesirable cross-reactivity with structurally related-glycans. Here we introduce a new technology called Computational Carbohydrate Grafting
Externí odkaz:
https://doaj.org/article/5463c8da170842a0ae77c464d711b708
Publikováno v:
The Journal of General Physiology
A primary target for nicotine is the acetylcholine receptor channel (AChR). Some of the ability of nicotine to activate differentially AChR subtypes has been traced to a transmitter-binding site amino acid that is glycine in lower affinity and lysine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8a80cb48ed72ed0436b6039b1e99e419
https://doi.org/10.1085/jgp.201210896
https://doi.org/10.1085/jgp.201210896
Autor:
Snehal Jadey, Anthony Auerbach
Publikováno v:
The Journal of General Physiology
In neuromuscular acetylcholine (ACh) receptor channels (AChRs), agonist molecules bind with a low affinity (LA) to two sites that can switch to high affinity (HA) and increase the probability of channel opening. We measured (by using single-channel k
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::71141c470e1c0af9121733e26c461516
https://doi.org/10.1085/jgp.201210801
https://doi.org/10.1085/jgp.201210801
Publikováno v:
Proceedings of the National Academy of Sciences. 108:4328-4333
Allosteric proteins use energy derived from ligand binding to promote a global change in conformation. The “gating” equilibrium constant of acetylcholine receptor-channels (AChRs) is influenced by ligands, mutations, and membrane voltage. We engi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8a78e67f5330bb874cfa1bb9a3df1f90
https://doi.org/10.1073/pnas.1016617108
https://doi.org/10.1073/pnas.1016617108
Autor:
David F. Smith, Robert J. Woods, Matthew B. Tessier, John Glushka, Jamie Heimburg-Molinaro, Oliver C. Grant, Snehal Jadey, Susan L. Deutscher, Kate Rittenhouse-Olson, Andrew M. Gulick
Publikováno v:
PLoS ONE
PLoS ONE, Vol 8, Iss 1, p e54874 (2013)
PLoS ONE, Vol 8, Iss 1, p e54874 (2013)
Recombinant antibodies are of profound clinical significance; yet, anti-carbohydrate antibodies are prone to undesirable cross-reactivity with structurally related-glycans. Here we introduce a new technology called Computational Carbohydrate Grafting
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b72b85b82958f3a643134228c22f1555
http://hdl.handle.net/10379/14140
http://hdl.handle.net/10379/14140
Publikováno v:
Biophysical Journal. 96(3)
The M2 helix of each of the five acetylcholine receptor (AChR) subunit forms the narrow region of the ion conduction pathway. As part of an overall project of trying to understand the mechanisms that underlie two reactions - the C(losed)↔O(pen) con
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::157058df921029e389333f687597d455
Autor:
Snehal Jadey, Anthony Auerbach
Publikováno v:
Biophysical Journal. 102(3):119a-120a
For many years drug action on membrane receptors has been conceptualized as occurring in two distinct steps, initially termed ‘affinity’ and ‘intrinsic activity’. In ligand-gated ion channels these stages of activation are called ‘binding
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::593d4c39e4c20785ba8eea49be00c71f
Publikováno v:
Biophysical Journal. 106:339a
Occupancy of an AChR binding site by an agonist (A) shifts a pre-existing equilibrium from the Closed-channel towards the Open-channel conformation. We estimated energy changes in adult mouse A2C↔A2O gating (adult mouse) from single-channels. Mutat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fbf14500cec664286ccd3a8066c681dd
https://doi.org/10.1016/j.bpj.2013.11.1939
https://doi.org/10.1016/j.bpj.2013.11.1939
Publikováno v:
Biophysical Journal. 98:132a
Acetylcholine receptors (AChRs) are ligand-gated ion channels involved in vertebrate neuromuscular transmission. Binding of acetylcholine (ACh, the endogenous neurotransmitter) increases the equilibrium constant of the ‘gating’ isomerization and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3ad47bd1614f9db4606b4cf8595871e7
https://doi.org/10.1016/j.bpj.2009.12.714
https://doi.org/10.1016/j.bpj.2009.12.714
Publikováno v:
Biophysical Journal. (3):131a-132a
Nicotinic acetylcholine receptors (AChRs) isomerize (‘gate’) between a low affinity/non-conducting (R) and a high affinity/ion-conducting (R∗) conformation. Many different residues in this large, heteropentameric membrane protein have been show
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be02823dc3fb450c8cb1c616b31d85a0