Zobrazeno 1 - 10
of 33
pro vyhledávání: '"Zachary M. James"'
Publikováno v:
Journal of General Physiology. 150:625-635
KCNH voltage-gated potassium channels (EAG, ERG, and ELK) play significant roles in neuronal and cardiac excitability. They contain cyclic nucleotide-binding homology domains (CNBHDs) but are not directly regulated by cyclic nucleotides. Instead, the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3f6e6de7d1871c2ba83d60e3d1b2b04e
https://doi.org/10.1085/jgp.201711989
https://doi.org/10.1085/jgp.201711989
Publikováno v:
Journal of Magnetic Resonance. 262:50-56
We have applied a bifunctional spin label and EPR spectroscopy to determine membrane protein structural topology in magnetically-aligned bicelles, using monomeric phospholamban (PLB) as a model system. Bicelles are a powerful tool for studying membra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3ddea20d822929aac05d39578cb7666a
https://doi.org/10.1016/j.jmr.2015.12.005
https://doi.org/10.1016/j.jmr.2015.12.005
Publikováno v:
Biophysical journal. 114(11)
We have used site-directed spin labeling and electron paramagnetic resonance (EPR) to map interactions between the transmembrane (TM) domains of the sarcoplasmic reticulum Ca(2+)-ATPase (SERCA) and phospholamban (PLB) as affected by PLB phosphorylati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::95018cd83ae36d0e72749486c01b968b
https://pubmed.ncbi.nlm.nih.gov/29874608
https://pubmed.ncbi.nlm.nih.gov/29874608
Publikováno v:
Journal of Magnetic Resonance. 250:71-75
We have optimized the magnetic alignment of phospholipid bilayered micelles (bicelles) for EPR spectroscopy, by varying lipid composition and temperature. Bicelles have been extensively used in NMR spectroscopy for several decades, in order to obtain
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fe472999f7cdd548bf3e739c5a92b446
https://doi.org/10.1016/j.jmr.2014.09.026
https://doi.org/10.1016/j.jmr.2014.09.026
Autor:
Félix A. Rey, Marija Backovic, David Veesler, Zachary M. James, Mark H. Ginsberg, Andrew J. Borst, Frank DiMaio, William N. Zagotta
Publikováno v:
Structure
Structure, Elsevier (Cell Press), 2017, 25 (11), pp.1732-1739.e5. ⟨10.1016/j.str.2017.09.007⟩
Structure, 2017, 25 (11), pp.1732-1739.e5. ⟨10.1016/j.str.2017.09.007⟩
Structure, Elsevier (Cell Press), 2017, 25 (11), pp.1732-1739.e5. ⟨10.1016/j.str.2017.09.007⟩
Structure, 2017, 25 (11), pp.1732-1739.e5. ⟨10.1016/j.str.2017.09.007⟩
International audience; The LM609 antibody specifically recognizes αVβ3 integrin and inhibits angiogenesis, bone resorption, and viral infections in an arginine-glycine-aspartate-independent manner. LM609 entered phase II clinical trials for the tr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::38090c90585f95553dd457680131dd28
https://hal-pasteur.archives-ouvertes.fr/pasteur-01632900
https://hal-pasteur.archives-ouvertes.fr/pasteur-01632900
Autor:
William N. Zagotta, Zachary M. James
Publikováno v:
The Journal of General Physiology
James and Zagotta discuss how recent cryoEM structures inform our understanding of cyclic nucleotide–binding domain channels.
Cyclic nucleotide-binding domain (CNBD) channels are a family of ion channels in the voltage-gated K+ channel superfa
Cyclic nucleotide-binding domain (CNBD) channels are a family of ion channels in the voltage-gated K+ channel superfa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::353d0beaffb1a3229567bf272938ed96
https://pubmed.ncbi.nlm.nih.gov/29233886
https://pubmed.ncbi.nlm.nih.gov/29233886
Autor:
Andrew J, Borst, Zachary M, James, William N, Zagotta, Mark, Ginsberg, Felix A, Rey, Frank, DiMaio, Marija, Backovic, David, Veesler
Publikováno v:
Structure (London, England : 1993). 25(11)
The LM609 antibody specifically recognizes αVβ3 integrin and inhibits angiogenesis, bone resorption, and viral infections in an arginine-glycine-aspartate independent manner. LM609 entered phase II clinical trials for the treatment of several cance
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::1bea9580edc36978ca3f22658118616a
https://pubmed.ncbi.nlm.nih.gov/29033288
https://pubmed.ncbi.nlm.nih.gov/29033288
Autor:
William N. Zagotta, Brandon Frenz, Andrew J. Borst, David Veesler, Yoni Haitin, Frank DiMaio, Zachary M. James
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 114(17)
Cyclic nucleotide-gated (CNG) and hyperpolarization-activated cyclic nucleotide-regulated (HCN) ion channels play crucial physiological roles in phototransduction, olfaction, and cardiac pace making. These channels are characterized by the presence o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5c45e4e6c8f81552e75be6ebf91630aa
https://pubmed.ncbi.nlm.nih.gov/28396445
https://pubmed.ncbi.nlm.nih.gov/28396445
Publikováno v:
Biophysical Journal. 103:1370-1378
We have used electron paramagnetic resonance (EPR) to probe the homo- and heterooligomeric interactions of reconstituted sarcoplasmic reticulum Ca-ATPase (SERCA) and its regulator phospholamban (PLB). SERCA is responsible for restoring calcium to the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::74d10c5bdf5fa19fd6262e10a643e683
https://doi.org/10.1016/j.bpj.2012.08.032
https://doi.org/10.1016/j.bpj.2012.08.032
Publikováno v:
Proceedings of the National Academy of Sciences. 108:12729-12733
We have used site-directed spin labeling and pulsed electron paramagnetic resonance to resolve a controversy concerning the structure of the utrophin–actin complex, with implications for the pathophysiology of muscular dystrophy. Utrophin is a homo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::36b26c7bec048c06ee18d59dcdd28472
https://doi.org/10.1073/pnas.1106453108
https://doi.org/10.1073/pnas.1106453108