Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Eric G.B. Evans"'
Autor:
Eric G.B. Evans, William N. Zagotta
Publikováno v:
Neuron. 109:1245-1247
In this issue of Neuron, Xue et al. report high-resolution structures of the human cGMP-activated ion channel CNGA1 from rod photoreceptors. These structures provide valuable insights into the processes of cGMP-dependent activation and Ca2+ block and
Autor:
Yarra Venkatesh, Eric G.B. Evans, William N. Zagotta, E. James Petersson, Anthony K Nhim, Marium M. Raza, Ryan A. Mehl, Chloe M. Jones, Brandon S Sim, Sharona E. Gordon
Publikováno v:
eLife, Vol 10 (2021)
eLife
eLife
With the recent explosion in high-resolution protein structures, one of the next frontiers in biology is elucidating the mechanisms by which conformational rearrangements in proteins are regulated to meet the needs of cells under changing conditions.
Autor:
William N. Zagotta, E. James Petersson, Anthony K Nhim, Sharona E. Gordon, Marium M. Raza, Eric G.B. Evans, Ryan A. Mehl, Chloe M. Jones, Brandon S Sim, Yarra Venkatesh
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ee49593929eba51bd097fc6dde6d517b
https://doi.org/10.7554/elife.70236.sa2
https://doi.org/10.7554/elife.70236.sa2
Autor:
Eric G.B. Evans, Subhashis Jana, Hyo Sang Jang, Sharona E. Gordon, William N. Zagotta, Ryan A. Mehl, Stefan Stoll
Publikováno v:
Biophysical Journal. 121:406a
Publikováno v:
Proc Natl Acad Sci U S A
Cyclic nucleotide-gated (CNG) ion channels are essential components of mammalian visual and olfactory signal transduction. CNG channels open upon direct binding of cyclic nucleotides (cAMP and/or cGMP), but the allosteric mechanism by which this occu
Publikováno v:
J Biol Chem
Cyclic nucleotide–gated (CNG) channels produce the initial electrical signal in mammalian vision and olfaction. They open in response to direct binding of cyclic nucleotide (cAMP or cGMP) to a cytoplasmic region of the channel. However, the conform
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff6d1998c2786164ea701fa1c63a8db3
https://europepmc.org/articles/PMC6509488/
https://europepmc.org/articles/PMC6509488/
Publikováno v:
Structure (London, England : 1993), vol 24, iss 7
Copper plays a critical role in prion protein (PrP) physiology. Cu(2+) binds with high affinity to the PrP N-terminal octarepeat (OR) domain, and intracellular copper promotes PrP expression. The molecular details of copper coordination within the OR
Autor:
Eric G.B. Evans, Glenn L. Millhauser
The function of the cellular prion protein (PrPC), while still poorly understood, is increasingly linked to its ability to bind physiological metal ions at the cell surface. PrPC binds divalent forms of both copper and zinc through its unstructured N
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8509ced346ca026c39676f10ccd6d09c
https://doi.org/10.1016/bs.pmbts.2017.06.005
https://doi.org/10.1016/bs.pmbts.2017.06.005
Publikováno v:
Biopolymers. 102:273-279
Chemoselective protein labeling remains a significant challenge in chemical biology. Although many selective labeling chemistries have been reported, the practicalities of matching the reaction with appropriately functionalized proteins and labeling
Publikováno v:
Journal of Biological Chemistry. 289:803-813
The cellular form of the prion protein (PrP(C)) is found in both full-length and several different cleaved forms in vivo. Although the precise functions of the PrP(C) proteolytic products are not known, cleavage between the unstructured N-terminal do