PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2547609-3 1989 Our sequence data shows that the histidine at residue 47 of ADH beta 2 is encoded by CAC. Histidine 33-42 potassium calcium-activated channel subfamily M regulatory beta subunit 2 Homo sapiens 64-70 3622513-8 1987 Residue 47 is His in beta 2 and Arg in the beta 1, gamma 1, and gamma 2 subunits, and in horse liver alcohol dehydrogenase. Histidine 14-17 potassium calcium-activated channel subfamily M regulatory beta subunit 2 Homo sapiens 21-27 3022799-3 1986 Transverse 1H NMR relaxation measurements have been used to investigate the interaction of SL-Phe with hemoglobin molecules by use of the resonances assigned to the C2 protons of the beta 2 His, the beta 143 His, and the beta 146 or beta 97 His residues as intrinsic probes. Histidine 190-193 potassium calcium-activated channel subfamily M regulatory beta subunit 2 Homo sapiens 183-189 3022799-4 1986 Distance calculations using the paramagnetically induced relaxation data suggest that the SL-Phe binding site is approximately 12-16 A away from the C2 protons of the beta 2 His and the beta 146 or beta 97 His residues in the (carbonmonoxy)hemoglobin tetramer; for deoxyhemoglobin, the distances are approximately 14-17 A between the SL-Phe binding site and the C2 protons of the beta 2 His, the beta 143 His, and the beta 146 His residues. Histidine 174-177 potassium calcium-activated channel subfamily M regulatory beta subunit 2 Homo sapiens 167-173 3893464-6 1985 The structural analysis showed that beta 2-Bern differs at only one position from beta 1: Arg-47 in beta 1 is substituted for His-47 in beta 2-Bern. Histidine 126-129 potassium calcium-activated channel subfamily M regulatory beta subunit 2 Homo sapiens 36-42 3893464-6 1985 The structural analysis showed that beta 2-Bern differs at only one position from beta 1: Arg-47 in beta 1 is substituted for His-47 in beta 2-Bern. Histidine 126-129 potassium calcium-activated channel subfamily M regulatory beta subunit 2 Homo sapiens 136-142 6378668-5 1984 Thus, Arg-47 in beta 1 is substituted by His in beta 2-Bern. Histidine 41-44 potassium calcium-activated channel subfamily M regulatory beta subunit 2 Homo sapiens 48-54 6374651-3 1984 Here, the beta 2 form has a histidine residue, while, in common with other characterized mammalian liver alcohol dehydrogenases, the beta 1 form has an arginine residue. Histidine 28-37 potassium calcium-activated channel subfamily M regulatory beta subunit 2 Homo sapiens 10-16 6374651-5 1984 The histidine/arginine-47 mutational replacement corresponds to a position that binds the pyrophosphate group of the coenzyme NAD(H); this explains the functional differences between the beta 1 beta 1 and beta 2 beta 2 isozymes, including both a lower pH optimum and higher turnover number of beta 2 beta 2, which is likely to be the mutant form. Histidine 4-13 potassium calcium-activated channel subfamily M regulatory beta subunit 2 Homo sapiens 205-211 6374651-5 1984 The histidine/arginine-47 mutational replacement corresponds to a position that binds the pyrophosphate group of the coenzyme NAD(H); this explains the functional differences between the beta 1 beta 1 and beta 2 beta 2 isozymes, including both a lower pH optimum and higher turnover number of beta 2 beta 2, which is likely to be the mutant form. Histidine 4-13 potassium calcium-activated channel subfamily M regulatory beta subunit 2 Homo sapiens 212-218 6374651-5 1984 The histidine/arginine-47 mutational replacement corresponds to a position that binds the pyrophosphate group of the coenzyme NAD(H); this explains the functional differences between the beta 1 beta 1 and beta 2 beta 2 isozymes, including both a lower pH optimum and higher turnover number of beta 2 beta 2, which is likely to be the mutant form. Histidine 4-13 potassium calcium-activated channel subfamily M regulatory beta subunit 2 Homo sapiens 212-218 6374651-5 1984 The histidine/arginine-47 mutational replacement corresponds to a position that binds the pyrophosphate group of the coenzyme NAD(H); this explains the functional differences between the beta 1 beta 1 and beta 2 beta 2 isozymes, including both a lower pH optimum and higher turnover number of beta 2 beta 2, which is likely to be the mutant form. Histidine 4-13 potassium calcium-activated channel subfamily M regulatory beta subunit 2 Homo sapiens 212-218 6547932-0 1984 The characterization of hemoglobin Manitoba or alpha (2)102(G9)Ser----Arg beta 2 and hemoglobin Contaldo or alpha (2)103(G10)His----Arg beta 2 by high performance liquid chromatography. Histidine 125-128 potassium calcium-activated channel subfamily M regulatory beta subunit 2 Homo sapiens 74-113 6256747-6 1980 When the temperature or the hemoglobin concentration was increased (i) several additional histidine resonances in sickle hemoglobin solutions had larger T1-1 values than the corresponding ones in normal hemoglobin and (ii) the differences between the T1-1 values (sickle versus normal hemoglobin) of these histidine resonances as well as that of the beta 2 histidine resonance gradually increased. Histidine 90-99 potassium calcium-activated channel subfamily M regulatory beta subunit 2 Homo sapiens 350-356 7410379-3 1980 Proton nuclear magnetic resonance measurements indicate that in the peptide beta (1-55) from hemoglobin S this residue is the histidine at beta 2. Histidine 126-135 potassium calcium-activated channel subfamily M regulatory beta subunit 2 Homo sapiens 139-145 478976-0 1979 Hemoglobin Sunshine Seth - alpha 2 (94 (G1) Asp replaced by His) beta 2. Histidine 60-63 potassium calcium-activated channel subfamily M regulatory beta subunit 2 Homo sapiens 65-71 393-2 1975 Hemoglobin Deer Lodge is an abnormal human hemoglobin with arginine substituted for histidine at the beta 2 position. Histidine 84-93 potassium calcium-activated channel subfamily M regulatory beta subunit 2 Homo sapiens 101-107 4430367-0 1974 A resonance Raman study on Hb M Iwate (alpha87His leads to Tyr beta)2, and Hb Zurich (alpha beta 63 His-Arg). Histidine 46-49 potassium calcium-activated channel subfamily M regulatory beta subunit 2 Homo sapiens 63-69 25617389-2 2015 The usefulness of the morpholinopropanesulfonic acid (MOPS)-histidine buffer in detecting beta2-transferrin, which is only found in the cerebrospinal fluid, was compared with the standard barbital buffer. Histidine 60-69 potassium calcium-activated channel subfamily M regulatory beta subunit 2 Homo sapiens 90-95 21486062-4 2011 Vibrational bands are assigned by comparison to histidine, phenylalanine, tyrosine, tryptophan, and 3-methylindole model compound data and by isotopic labeling of histidine in the beta2 subunit. Histidine 163-172 potassium calcium-activated channel subfamily M regulatory beta subunit 2 Homo sapiens 180-185 10026163-5 1999 This difference is consistent with preferential binding of Cu(II) in Hb A0 to a high affinity site involving His-beta2, which is ineffective in promoting electron exchange between Cu(II) and the beta heme iron. Histidine 109-112 potassium calcium-activated channel subfamily M regulatory beta subunit 2 Homo sapiens 113-118 9425070-0 1998 Conformational fluctuations in deoxy hemoglobin revealed as a major contributor to anionic modulation of function through studies of the oxygenation and oxidation of hemoglobins A0 and Deer Lodge beta2(NA2)His --> Arg. Histidine 206-209 potassium calcium-activated channel subfamily M regulatory beta subunit 2 Homo sapiens 196-201 8201622-5 1994 A naturally occurring variant of beta 1 alcohol dehydrogenase, found in approximately 50% of the Asian population, possesses a His at position 47 (beta 2 or beta 47H) and was crystallized in a complex with NAD+ and the inhibitor 4-iodopyrazole. Histidine 127-130 potassium calcium-activated channel subfamily M regulatory beta subunit 2 Homo sapiens 147-153 8357536-7 1993 The histidines beta 2 and beta 143 of the two beta-chains form hydrogen bonds with the phosphates. Histidine 4-14 potassium calcium-activated channel subfamily M regulatory beta subunit 2 Homo sapiens 15-21 1512262-5 1992 In the R-state, His-97 beta 2 is positioned between Thr-38 alpha 1 and Thr-41 alpha 1, whereas in transition to the T-state His 97 beta 2 must "jump" a turn in the alpha 1 C helix to form nonpolar contacts with Thr-41 alpha 1 and Pro-44 alpha 1. Histidine 16-19 potassium calcium-activated channel subfamily M regulatory beta subunit 2 Homo sapiens 23-29 1512262-5 1992 In the R-state, His-97 beta 2 is positioned between Thr-38 alpha 1 and Thr-41 alpha 1, whereas in transition to the T-state His 97 beta 2 must "jump" a turn in the alpha 1 C helix to form nonpolar contacts with Thr-41 alpha 1 and Pro-44 alpha 1. Histidine 16-19 potassium calcium-activated channel subfamily M regulatory beta subunit 2 Homo sapiens 131-137 1512262-5 1992 In the R-state, His-97 beta 2 is positioned between Thr-38 alpha 1 and Thr-41 alpha 1, whereas in transition to the T-state His 97 beta 2 must "jump" a turn in the alpha 1 C helix to form nonpolar contacts with Thr-41 alpha 1 and Pro-44 alpha 1. Histidine 124-127 potassium calcium-activated channel subfamily M regulatory beta subunit 2 Homo sapiens 23-29 1512262-5 1992 In the R-state, His-97 beta 2 is positioned between Thr-38 alpha 1 and Thr-41 alpha 1, whereas in transition to the T-state His 97 beta 2 must "jump" a turn in the alpha 1 C helix to form nonpolar contacts with Thr-41 alpha 1 and Pro-44 alpha 1. Histidine 124-127 potassium calcium-activated channel subfamily M regulatory beta subunit 2 Homo sapiens 131-137 1512262-7 1992 In the R2-state, His-97 beta 2 simply rotates away from threonines 38 alpha 1 and 41 alpha 1, breaking contact with these residues and allowing water access to the center of the alpha 1 beta 2 interface. Histidine 17-20 potassium calcium-activated channel subfamily M regulatory beta subunit 2 Homo sapiens 24-30 1512262-7 1992 In the R2-state, His-97 beta 2 simply rotates away from threonines 38 alpha 1 and 41 alpha 1, breaking contact with these residues and allowing water access to the center of the alpha 1 beta 2 interface. Histidine 17-20 potassium calcium-activated channel subfamily M regulatory beta subunit 2 Homo sapiens 186-192 1512262-8 1992 With the switch region in an open position in the R2-state, His-97 beta 2 should be able to move by Thr-41 alpha 1 and make the transition to the T-state with a steric barrier that is less than that for the R-T transition. Histidine 60-63 potassium calcium-activated channel subfamily M regulatory beta subunit 2 Homo sapiens 67-73 1428951-0 1992 Hb Ethiopia or alpha 2(140)(HC2)Tyr----His beta 2. Histidine 39-42 potassium calcium-activated channel subfamily M regulatory beta subunit 2 Homo sapiens 43-49 1718750-2 1991 One peptide, His-Gly-Arg-Val-Gly-Ile-Tyr-Phe-Gly-Met-Lys (peptide 11; Ile, isoleucine) is antigenic and binds with a high affinity to a monoclonal antibody that recognizes the native beta 2 subunit. Histidine 13-16 potassium calcium-activated channel subfamily M regulatory beta subunit 2 Homo sapiens 183-189