Výsledky vyhledávání - "Eswari Gudipati"

Agonist-Induced Transitions of the Acetylcholine Receptor

Autor: Eswari Gudipati, David P. Richman, Mike Y. Lin, Anthony R. Chuang, Mark A. Agius, Brent Y. Hamaoka, Laura Silvian, Robert H. Fairclough, Christopher C. Beltzner

Publikováno v: Annals of the New York Academy of Sciences. 998:101-113

Anti-acetylcholine receptor (AChR) monoclonal antibody 383C binds to the beta-hairpin loop alpha(187-199) of only one of the two Torpedo AChR alpha subunits. The loop recognized is associated with the alpha subunit corresponding to the high-affinity

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::61f3b7432f0f99211cb910e8e98ec252
https://doi.org/10.1196/annals.1254.012

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Differential surface accessibility of α(187–199) in the Torpedo acetylcholine receptor α subunits 1 1Edited by B. Holland

Autor: Mike Y. Lin, George M. Twaddle, David P. Richman, Robert H. Fairclough, Eswari Gudipati

Publikováno v: Journal of Molecular Biology. 282:317-330

We have probed the surface accessibility of residues α187 to α199 of the Torpedo acetylcholine receptor with monoclonal antibody 383C, which binds uniquely to these residues. However, 383C binds to only one of the two α subunits in the membrane-bo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::e5681502d73263449ff4d24ea39115b0
https://doi.org/10.1006/jmbi.1998.2001

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Mapping the mab 383C epitope to α 2 (187–199) of the Torpedo acetylcholine receptor on the three-dimensional model 1 1Edited by B. Holland

Autor: Remington J.S. Stone, Eswari Gudipati, George M. Twaddle, Robert Josephs, David A. Burkwall, Robert H. Fairclough, David P. Richman

Publikováno v: Journal of Molecular Biology. 282:301-315

Monoclonal antibody 383C is an anti-acetylcholine receptor antibody whose binding to the receptor is blocked by alpha-bungarotoxin and by carbamylcholine. Monoclonal antibody 383C binds to the alpha subunit of the Torpedo acetylcholine (ACh) receptor

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::f3aba6b40e35c5019f5c2b7932647e53
https://doi.org/10.1006/jmbi.1998.2000

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A Role for alpha(187-199) in the Conversion of Agonist Binding Energy to the Opening of the Acetylcholine Receptor Ion Channela

Autor: David A. Burkwall, Robert Josephs, David P. Richman, Eswari Gudipati, Mike Y. Lin, George M. Twaddle, Robert H. Fairclough

Publikováno v: Annals of the New York Academy of Sciences. 841:87-92

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1b7a6bdaa7ee131541dbedef062f9739
https://doi.org/10.1111/j.1749-6632.1998.tb10911.x

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Distance between alpha-Cys 192 of the Acetylcholine Receptor and Rhodamine-labeled alpha-Bungarotoxin Complexed to the Receptor

Autor: Robert H. Fairclough, Eswari Gudipati, Viswanatham Katta, Laura Silvian

Publikováno v: Annals of the New York Academy of Sciences. 841:104-107

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::40f36f146a45c0cb5bcb5435cb1a9446
https://doi.org/10.1111/j.1749-6632.1998.tb10915.x

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Entrapment of enzymes using organo-functionalized polysiloxane copolymers

Autor: Eswari Gudipati, Duane L. Venton

Publikováno v: Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1250:117-125

The present study expands previous work [(1984) Biochim. Biophys. Acta. 797, 343-347] by showing that organo-functionalized polysiloxane copolymers could entrap two of the most frequently immobilized enzymes, i.e. urease and invertase with retention

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9ba6ad158ee98c6b953ad1bbffecfbb4
https://doi.org/10.1016/0167-4838(95)00079-a

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Influence of protein on polysiloxane polymer formation: evidence for induction of complementary protein-polymer interactions

Autor: Duane L. Venton, Eswari Gudipati

Publikováno v: Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1250:126-136

Results presented in the companion paper suggested that the protein itself might be actively involved in the polymerization process while being entrapped in polysiloxane polymers. It was speculated that the organo-functional side chains on the silano

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::24e626df341e3822f403822254ced97b
https://doi.org/10.1016/0167-4838(95)00080-e

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