Zobrazeno 1 - 10 of 27 pro vyhledávání: '"S O, Smith"'
1
Fourier transform infrared spectroscopy and site-directed isotope labeling as a probe of local secondary structure in the transmembrane domain of phospholamban
Autor: Xiao-Mei Liu, Kenneth J. Rothschild, S. Aimoto, M. S. Rothman, Donald M. Engelman, Parshuram Rath, S. O. Smith, Isaiah T. Arkin, Cheryl F.C. Ludlam
Publikováno v: Biophysical Journal. 70:1728-1736
Phospholamban is a 52-amino acid residue membrane protein that regulates Ca(2+)-ATPase activity in the sarcoplasmic reticulum of cardiac muscle cells. The hydrophobic C-terminal 28 amino acid fragment of phospholamban (hPLB) anchors the protein in th
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::567ad2f7d9be37e9567258e5f71838f4
https://doi.org/10.1016/s0006-3495(96)79735-7
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2
Helical structure of phospholamban in membrane bilayers
Autor: S O, Smith, T, Kawakami, W, Liu, M, Ziliox, S, Aimoto
Publikováno v: Journal of molecular biology. 313(5)
The regulation of calcium levels across the membrane of the sarcoplasmic reticulum involves the complex interplay of several membrane proteins. Phospholamban is a 52 residue integral membrane protein that is involved in reversibly inhibiting the Ca(2
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::bc404685a8effb8ed7fa402fc6e093c6
https://pubmed.ncbi.nlm.nih.gov/11700069
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3
Structural models of the bovine papillomavirus E5 protein
Autor: T, Surti, O, Klein, K, Aschheim, D, DiMaio, S O, Smith
Publikováno v: Proteins. 33(4)
The bovine papillomavirus E5 protein is thought to be a type II integral membrane protein that exists as a disulfide-linked homodimer in transformed cells. Polarized-infrared measurements show that the E5 dimer in membrane bilayers is largely alpha-h
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::8034731d2776d83c038e80e9af74f1fa
https://pubmed.ncbi.nlm.nih.gov/9849943
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4
Functional interaction of transmembrane helices 3 and 6 in rhodopsin. Replacement of phenylalanine 261 by alanine causes reversion of phenotype of a glycine 121 replacement mutant
Autor: M, Han, S W, Lin, M, Minkova, S O, Smith, T P, Sakmar
Publikováno v: The Journal of biological chemistry. 271(50)
Replacement of a highly conserved glycine residue on transmembrane (TM) helix 3 of bovine rhodopsin (Gly121) by amino acid residues with larger side chains causes a progressive blue-shift in the lambdamax value of the pigment, a decrease in thermal s
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::dd02c0b0334642759e2c42672e1dd3b1
https://pubmed.ncbi.nlm.nih.gov/8943296
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5
Factors affecting erythropoietin production and correction of anemia in kidney transplant recipients
Autor: L W, Moore, S O, Smith, R P, Winsett, S R, Acchiardo, A O, Gaber
Publikováno v: Clinical transplantation. 8(4)
Anemia does not correct in many kidney transplant recipients, probably due to iron deficiency or inadequate erythropoietin (Epo) production. We evaluated effects of iron (Fe) availability on correction of anemia in renal transplant recipients and sou
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::34a9bb8915be18e165ebea40b27c4858
https://pubmed.ncbi.nlm.nih.gov/7949539
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7
Iterative fitting of magic-angle-spinning NMR spectra
Autor: C. Winkel, Robert G. Griffin, S. O. Smith, J Lugtenburgt, J. M. L. Courtin, A.C Kolbert, H. J. M. de Groot, Judith Herzfeld
Publikováno v: Journal of Magnetic Resonance, 91(1), 30-38
An approach for the analysis of magic-angle-spinning NMR spectra which combines nonlinear iterative and linear analytical procedures for fitting sideband spectra is presented. Parameter values, as well as statistical errors, are extracted from the ex
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5387ae401d1cee1c3de68264958d07d4
https://hdl.handle.net/1887/3465960
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8
Solid-state NMR studies of mechanism of the opsin shift in the visual pigment rhodopsin
Autor: J. Lugtenburg, M. E. Miley, Robert G. Griffin, I. Palings, H. J. M. de Groot, S. O. Smith, J. M. L. Courtin, Richard A. Mathies
Publikováno v: Biochemistry, 29(35), 8158-8164. AMER CHEMICAL SOC
Solid-state 13C NMR spectra have been obtained of bovine rhodopsin and isorhodopsin regenerated with retinal selectively 13C labeled along the polyene chain. In rhodopsin, the chemical shifts for 13C-5, 13C-6, 13C-7, 13C-14, and 13C-15 correspond clo
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3eb4c051914bed2c1aa041dff4ada4c2
https://hdl.handle.net/1887/3281790
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9
Solid-state 13C and 15N NMR study of the low pH forms of bacteriorhodopsin
Autor: H J, de Groot, S O, Smith, J, Courtin, E, van den Berg, C, Winkel, J, Lugtenburg, R G, Griffin, J, Herzfeld
Publikováno v: Biochemistry. 29(29)
The visible absorption of bacteriorhodopsin (bR) is highly sensitive to pH, the maximum shifting from 568 nm (pH 7) to approximately 600 nm (pH 2) and back to 565 nm (pH 0) as the pH is decreased further with HCl. Blue membrane (lambda max greater th
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::f60acdc62bc5ca2a75212dca2d3a0dbf
https://pubmed.ncbi.nlm.nih.gov/2168744
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