PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 16085771-0 2005 The hydroxylamine reaction of sensory rhodopsin II: light-induced conformational alterations with C13=C14 nonisomerizable pigment. Hydroxylamine 4-17 rhodopsin Homo sapiens 38-47 22874131-9 2012 Our results show that with respect to hydroxylamine sensitivity and retinal release, the wild-type echidna rhodopsin displays major differences to all previously characterized mammalian rhodopsins and appears more similar to other nonmammalian vertebrate rhodopsins such as chicken and anole. Hydroxylamine 38-51 rhodopsin Homo sapiens 107-116 21766795-3 2011 We discovered that, while hydroxylamine can enter the retinal binding pocket of light-activated rhodopsin, the modified hydroxylamine compounds o-methylhydroxylamine (mHA), o-ethylhydroxylamine (eHA), o-tert-butylhydroxylamine (t-bHA), and o-(carboxymethyl)hydroxylamine (cmHA) are excluded. Hydroxylamine 26-39 rhodopsin Homo sapiens 96-105 18490656-5 2008 For inactive rhodopsin, it was possible to find a globally minimized arrangement of nitroxide locations that simultaneously satisfied the crystal structure of rhodopsin (Protein Data Bank entry 1GZM), the experimentally measured distance data, and the known rotamers of the nitroxide side chain. Hydroxylamine 84-93 rhodopsin Homo sapiens 13-22 18490656-5 2008 For inactive rhodopsin, it was possible to find a globally minimized arrangement of nitroxide locations that simultaneously satisfied the crystal structure of rhodopsin (Protein Data Bank entry 1GZM), the experimentally measured distance data, and the known rotamers of the nitroxide side chain. Hydroxylamine 84-93 rhodopsin Homo sapiens 159-168 18490656-5 2008 For inactive rhodopsin, it was possible to find a globally minimized arrangement of nitroxide locations that simultaneously satisfied the crystal structure of rhodopsin (Protein Data Bank entry 1GZM), the experimentally measured distance data, and the known rotamers of the nitroxide side chain. Hydroxylamine 274-283 rhodopsin Homo sapiens 13-22 16634635-1 2006 Nitroxide sensors were placed in rhodopsin at sites 140, 227, 250, and 316 to monitor the dynamics and conformation of the receptor at the cytoplasmic surface in solutions of dodecyl maltoside (DM), digitonin, and phospholipid bilayers of two compositions. Hydroxylamine 0-9 rhodopsin Homo sapiens 33-42 17918963-9 2007 However, unlike wild-type rhodopsin, the covalent linkage of the ligand can be attacked by hydroxylamine in the dark. Hydroxylamine 91-104 rhodopsin Homo sapiens 26-35 16085771-3 2005 Similarly to other retinal proteins, sensory rhodopsin II undergoes a bleaching reaction with hydroxylamine in the dark which is markedly catalyzed by light. Hydroxylamine 94-107 rhodopsin Homo sapiens 45-54 11106502-4 2000 Upon absorption of a photon by rhodopsin, the fluorescence intensity increased as much as 20% at acidic pH with an apparent pK(a) of approximately 6.8 at 4 degrees C, and was sensitive to the presence of hydroxylamine. Hydroxylamine 204-217 rhodopsin Homo sapiens 31-40 11747424-1 2001 Double-spin-labeled mutants of rhodopsin were prepared containing a nitroxide side chain at position 316 in the cytoplasmic surface helix H8, and a second nitroxide in the sequence of residues 60-75, which includes the cytoplasmic loop CL1 and cytoplasmic ends of helices TM1 and TM2. Hydroxylamine 68-77 rhodopsin Homo sapiens 31-40 11747424-1 2001 Double-spin-labeled mutants of rhodopsin were prepared containing a nitroxide side chain at position 316 in the cytoplasmic surface helix H8, and a second nitroxide in the sequence of residues 60-75, which includes the cytoplasmic loop CL1 and cytoplasmic ends of helices TM1 and TM2. Hydroxylamine 155-164 rhodopsin Homo sapiens 31-40 11747424-3 2001 In the dark state in solutions of dodecyl maltoside, the interspin distances are found to be consistent with structural models of the nitroxide side chain and rhodopsin, both derived from crystallography. Hydroxylamine 134-143 rhodopsin Homo sapiens 159-168 8110774-2 1994 Approximately 70% of the rhodopsin was depalmitoylated in rod outer segments by a mild hydroxylamine treatment that resulted in minimal bleaching of rhodopsin. Hydroxylamine 87-100 rhodopsin Homo sapiens 25-34 8110774-2 1994 Approximately 70% of the rhodopsin was depalmitoylated in rod outer segments by a mild hydroxylamine treatment that resulted in minimal bleaching of rhodopsin. Hydroxylamine 87-100 rhodopsin Homo sapiens 149-158 8110774-3 1994 Subsequent purification by affinity chromatography could be used to remove hydroxylamine-bleached rhodopsin. Hydroxylamine 75-88 rhodopsin Homo sapiens 98-107 8386638-6 1993 Prior to analysis of the phosphorylation mixture, the phosphorylated form of photoexcited rhodopsin was converted into phospho-opsin by treatment with NH2OH. Hydroxylamine 151-156 rhodopsin Homo sapiens 90-99 1431805-3 1992 Rhodopsin was inactivated by exposure to hydroxylamine and bright light. Hydroxylamine 41-54 rhodopsin Homo sapiens 0-9 1330032-1 1992 Permeation of molecular oxygen in rhodopsin, an integral membrane protein, has been investigated by monitoring the bimolecular collision rate between molecular oxygen and the nitroxide spin label using a pulse electron spin resonance (ESR) T1 method. Hydroxylamine 175-184 rhodopsin Homo sapiens 34-43 2509200-9 1989 Upon treatment of the R*ret-Te complex by a high concentration of hydroxylamine, the retinal can be removed from the rhodopsin. Hydroxylamine 66-79 rhodopsin Homo sapiens 117-126 2914607-4 1989 Experiments using hydroxylamine as an artificial quencher of rhodopsin activity suggest that calcium acts upon rhodopsin kinase and not upon the rate of the GTPase. Hydroxylamine 18-31 rhodopsin Homo sapiens 61-70 2914607-4 1989 Experiments using hydroxylamine as an artificial quencher of rhodopsin activity suggest that calcium acts upon rhodopsin kinase and not upon the rate of the GTPase. Hydroxylamine 18-31 rhodopsin Homo sapiens 111-120 3927920-0 1985 Investigation of rhodopsin catalyzed G-protein GTP-binding using [35S] GTP gamma S--effects of regeneration and hydroxylamine. Hydroxylamine 112-125 rhodopsin Homo sapiens 17-26 13534735-0 1958 Rhodopsin bleaching in the presence of hydroxylamine. Hydroxylamine 39-52 rhodopsin Homo sapiens 0-9