Peropsin modulates transit of vitamin A from retina to retinal pigment epithelium

Autor: Shannan Eddington, Jeremy Nathans, Roxana A. Radu, Hui Sun, Jeremy D. Cook, Sze Yin Ng, Marcia Lloyd, Dean Bok, Gabriel H. Travis

Publikováno v: Cook, JD; Ng, SY; Lloyd, M; Eddington, S; Sun, H; Nathans, J; et al.(2017). Peropsin modulates transit of vitamin A from retina to retinal pigment epithelium. JOURNAL OF BIOLOGICAL CHEMISTRY, 292(52), 21407-21416. doi: 10.1074/jbc.M117.812701. UCLA: Retrieved from: http://www.escholarship.org/uc/item/6zp1h80n
The Journal of biological chemistry, vol 292, iss 52

Peropsin is a non-visual opsin in both vertebrate and invertebrate species. In mammals, peropsin is present in the apical microvilli of retinal pigment epithelial (RPE) cells. These structures interdigitate with the outer segments of rod and cone pho

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e9e5f402ae6586db70c58c6de2a857c
http://www.escholarship.org/uc/item/6zp1h80n

Identification of DES1 as a Vitamin A Isomerase in Müller Glial Cells of the Retina

Autor: Joanna J. Kaylor, Shanta Sarfare, C Nathaniel Roybal, Paul Kim, Tongzhou Xu, Samer Habib, Gabriel H. Travis, Steven Nusinowitz, Jeremy D. Cook, Anita Kim, Anh Miu, Quan Yuan, Jacob Makshanoff

Publikováno v: Nature chemical biology
Nature chemical biology, vol 9, iss 1

Absorption of a light particle by an opsin-pigment causes photoisomerization of its retinaldehyde chromophore. Restoration of light sensitivity to the resulting apo-opsin requires chemical re-isomerization of the photobleached chromophore. This is ca

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aa782a01339f755f730b12ac2f3086e6
http://europepmc.org/articles/PMC3522777

Structural studies on Na0.75CoO2 thermoelectric material at high pressures

Autor: D. Prabhakaran, Eunja Kim, Jeremy D. Cook, Mark R. Chance, Sandeep Rekhi, Timothy L. Stemmler, Maddury Somayazulu, Ravhi S. Kumar, Andrew T. Boothroyd, Andrew Cornelius

Publikováno v: Solid State Communications. 149:1712-1716

The crystal structure of Na0.75CoO2 was studied at ambient and low temperatures down to 10 K at pressures up to 40 GPa using synchrotron x-rays and a diamond cell in angle dispersion geometry. A reduction in the c / a ratio was observed at both condi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ca96b003ff586bfd488dcd0b0ffbbe79
https://doi.org/10.1016/j.ssc.2009.06.012

Circular dichroism (CD) spectroscopy of the assembly and disassembly of SNAREs: The proteins involved in membrane fusion in cells

Autor: Timothy L. Stemmler, Bhanu P. Jena, Jeremy D. Cook, Won Jin Cho

Publikováno v: Chemical Physics Letters. 462:6-9

In this study, we report for the first time that both t-SNAREs and v-SNARE and their complexes in buffered suspension, exhibit defined peaks at CD signals of 208 and 222 nm wavelengths, consistent with a higher degree of helical secondary structure.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::810cade370a4530894b924b0a6d4b172
https://doi.org/10.1016/j.cplett.2008.07.043

Molecular details of the yeast frataxin-Isu1 interaction during mitochondrial Fe-S cluster assembly

Autor: Andrew Dancis, William C. Childs, Kalyan C. Kondapalli, Jeremy D. Cook, Yogapriya Murugesan, Swati Rawat, Timothy L. Stemmler

Publikováno v: Biochemistry. 49(40)

Frataxin, a conserved nuclear-encoded mitochondrial protein, plays a direct role in iron-sulfur cluster biosynthesis within the ISC assembly pathway. Humans with frataxin deficiency have Friedreich's ataxia, a neurodegenerative disorder characterized

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::873f23ad02022e0584ab07db6c055815
https://pubmed.ncbi.nlm.nih.gov/20815377