PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 16331986-7 2005 Together, these data show that nitrosoalkanes are a novel class of heme-based sGC activators and suggest that heme ligation is a general requirement for YC-1 synergism. Heme 110-114 RNA binding motif single stranded interacting protein 1 Homo sapiens 153-157 20459051-6 2010 In contrast, addition of YC-1 to either the 1-NO or xsNO forms alters the RR spectrum significantly, indicating a protein-induced change in the heme geometry. Heme 144-148 RNA binding motif single stranded interacting protein 1 Homo sapiens 25-29 20353168-4 2010 YC-1 also shifts the RR intensity of the nu(FeC) and nu(CO) bands from 473 and 1985 cm(-1) to 487 and 1969 cm(-1), respectively, and induces an additional nu(FeC) band, at 521 cm(-1), assigned to five-coordinate heme-CO. Site-directed variants in the proximal heme pocket (P118A) or in the distal heme pocket (V5Y and I149Y) reduce the extent of YC-1 activation, along with the 473 cm(-1) band intensity. Heme 212-216 RNA binding motif single stranded interacting protein 1 Homo sapiens 0-4 20353168-4 2010 YC-1 also shifts the RR intensity of the nu(FeC) and nu(CO) bands from 473 and 1985 cm(-1) to 487 and 1969 cm(-1), respectively, and induces an additional nu(FeC) band, at 521 cm(-1), assigned to five-coordinate heme-CO. Site-directed variants in the proximal heme pocket (P118A) or in the distal heme pocket (V5Y and I149Y) reduce the extent of YC-1 activation, along with the 473 cm(-1) band intensity. Heme 260-264 RNA binding motif single stranded interacting protein 1 Homo sapiens 0-4 20353168-4 2010 YC-1 also shifts the RR intensity of the nu(FeC) and nu(CO) bands from 473 and 1985 cm(-1) to 487 and 1969 cm(-1), respectively, and induces an additional nu(FeC) band, at 521 cm(-1), assigned to five-coordinate heme-CO. Site-directed variants in the proximal heme pocket (P118A) or in the distal heme pocket (V5Y and I149Y) reduce the extent of YC-1 activation, along with the 473 cm(-1) band intensity. Heme 260-264 RNA binding motif single stranded interacting protein 1 Homo sapiens 0-4 20353168-7 2010 Specifically, YC-1 binding alters the heme geometry via peripheral nonbonded contacts and also relieves an intrinsic electronic effect that weakens FeCO backbonding in the native, YC-1 responsive protein. Heme 38-42 RNA binding motif single stranded interacting protein 1 Homo sapiens 14-18 31566566-3 2019 NO and the sGC-specific stimulator YC-1 induce a 71 rotation of the heme-binding beta H-NOX and PAS domains. Heme 69-73 RNA binding motif single stranded interacting protein 1 Homo sapiens 35-39 27364190-7 2016 Docking of YC-1, a classic heme-dependent stimulator, to all frames of representative trajectories of "inactive" and "active" conformations, followed by calculation of absolute binding free energies with the linear interaction energy (LIE) method, revealed a potential high-affinity binding site on the "active" structure. Heme 27-31 RNA binding motif single stranded interacting protein 1 Homo sapiens 11-15 16534188-1 2006 BACKGROUND: The indazole derivative YC-1 has been characterized as a nitric oxide (NO)-independent and heme dependent soluble guanylate cyclase (sGC) activator, which also sensitizes sGC to NO. Heme 103-107 RNA binding motif single stranded interacting protein 1 Homo sapiens 36-40 9920755-6 1999 It is, therefore, a reasonable inference that ligand binding at the heme iron atom is intimately connected with enzyme activation, a hypothesis that would have been difficult to maintain if the earlier report, that YC-1 has no effect on CO binding, were correct. Heme 68-72 RNA binding motif single stranded interacting protein 1 Homo sapiens 215-219 12540839-2 2003 Here we report the action of YC-1 on the coordination of CO- and NO-hemes in the enzyme and correlate the events with the activation of enzyme catalysis. Heme 68-73 RNA binding motif single stranded interacting protein 1 Homo sapiens 29-33 12540839-4 2003 To explore the affect of YC-1 on the NO-heme coordination, the six-coordinate NO complex of the enzyme was stabilized by dibromodeuteroheme substitution. Heme 40-44 RNA binding motif single stranded interacting protein 1 Homo sapiens 25-29 12540839-5 2003 Using the dibromodeuteroheme enzyme, YC-1 converted the six-coordinate NO-heme to a five-coordinate NO-heme with a characteristic EPR signal that differed from that in the absence of YC-1. Heme 24-28 RNA binding motif single stranded interacting protein 1 Homo sapiens 37-41 12540839-5 2003 Using the dibromodeuteroheme enzyme, YC-1 converted the six-coordinate NO-heme to a five-coordinate NO-heme with a characteristic EPR signal that differed from that in the absence of YC-1. Heme 24-28 RNA binding motif single stranded interacting protein 1 Homo sapiens 183-187 12540839-5 2003 Using the dibromodeuteroheme enzyme, YC-1 converted the six-coordinate NO-heme to a five-coordinate NO-heme with a characteristic EPR signal that differed from that in the absence of YC-1. Heme 74-78 RNA binding motif single stranded interacting protein 1 Homo sapiens 37-41 12540839-6 2003 These results revealed that YC-1 facilitated cleavage of the proximal His-iron bond and caused geometrical distortion of the five-coordinate NO-heme. Heme 144-148 RNA binding motif single stranded interacting protein 1 Homo sapiens 28-32 15023055-4 2004 In the presence of NO, YC-1 synergistically increases the catalytic activity of sGC by enhancing the affinity of NO for the heme. Heme 124-128 RNA binding motif single stranded interacting protein 1 Homo sapiens 23-27 9443939-8 1998 Together, our results indicate that YC-1 increases the maximal catalytic rate and sensitizes the enzyme toward its gaseous activators by binding to an allosteric site on sGC molecules, thereby reducing the ligand dissociation rate from the heme group. Heme 240-244 RNA binding motif single stranded interacting protein 1 Homo sapiens 36-40 9646941-4 1998 Carbon monoxide (CO) binds to the heme to form a 6-coordinate complex, but only activates the enzyme 5-fold, YC-1 is a recently discovered compound that relaxes vascular smooth muscle by stimulating sGC. Heme 34-38 RNA binding motif single stranded interacting protein 1 Homo sapiens 109-113 9646941-11 1998 In the presence of YC-1, maximal activation of sGC by CO is achieved by formation of a 6-coordinate complex between CO and the heme indicating that cleavage of the Fe-His bond is not required for maximal activation of sGC. Heme 127-131 RNA binding motif single stranded interacting protein 1 Homo sapiens 19-23