PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 12221079-2 2002 Incubation of the purified His-tagged ROMK1 protein with PKC and radiolabeled ATP resulted in (32)P incorporation into ROMK1 detected by autoradiography. Adenosine Triphosphate 78-81 potassium inwardly rectifying channel subfamily J member 1 Homo sapiens 38-43 12381730-0 2002 Localization of the ATP/phosphatidylinositol 4,5 diphosphate-binding site to a 39-amino acid region of the carboxyl terminus of the ATP-regulated K+ channel Kir1.1. Adenosine Triphosphate 20-23 potassium inwardly rectifying channel subfamily J member 1 Homo sapiens 157-163 12381730-1 2002 Intracellular ATP and membrane-associated phosphatidylinositol phospholipids, like PIP(2) (PI(4,5)P(2)), regulate the activity of ATP-sensitive K(+) (K(ATP)) and Kir1.1 channels by direct interaction with the pore-forming subunits of these channels. Adenosine Triphosphate 14-17 potassium inwardly rectifying channel subfamily J member 1 Homo sapiens 162-168 12381730-1 2002 Intracellular ATP and membrane-associated phosphatidylinositol phospholipids, like PIP(2) (PI(4,5)P(2)), regulate the activity of ATP-sensitive K(+) (K(ATP)) and Kir1.1 channels by direct interaction with the pore-forming subunits of these channels. Adenosine Triphosphate 130-133 potassium inwardly rectifying channel subfamily J member 1 Homo sapiens 162-168 12381730-3 2002 In addition, PIP(2) competed for TNP-ATP binding on the COOH termini of Kir1.1 and Kir6.x channels, providing a mechanism that can account for PIP(2) antagonism of ATP inhibition of these channels. Adenosine Triphosphate 37-40 potassium inwardly rectifying channel subfamily J member 1 Homo sapiens 72-78 12381730-3 2002 In addition, PIP(2) competed for TNP-ATP binding on the COOH termini of Kir1.1 and Kir6.x channels, providing a mechanism that can account for PIP(2) antagonism of ATP inhibition of these channels. Adenosine Triphosphate 164-167 potassium inwardly rectifying channel subfamily J member 1 Homo sapiens 72-78 12381730-4 2002 To localize the ATP-binding site within the COOH terminus of Kir1.1, we produced and purified maltose-binding protein (MBP) fusion proteins containing truncated and/or mutated Kir1.1 COOH termini and examined the binding of TNP-ATP and competition by PIP(2). Adenosine Triphosphate 16-19 potassium inwardly rectifying channel subfamily J member 1 Homo sapiens 61-67 12381730-11 2002 These studies suggest that the first 39 COOH-terminal amino acid residues form an ATP-PIP(2) binding domain in Kir1.1 and possibly the Kir6.x ATP-sensitive K(+) channels. Adenosine Triphosphate 82-85 potassium inwardly rectifying channel subfamily J member 1 Homo sapiens 111-117 12589089-3 2003 Mutations in the bumetanide-sensitive Na-K-2Cl cotransporter (NKCC2) and ATP-sensitive inwardly rectifying potassium channel (ROMK) of the thick ascending limb of Henle"s loop have been identified in the antenatal Bartter syndrome. Adenosine Triphosphate 73-76 potassium inwardly rectifying channel subfamily J member 1 Homo sapiens 126-130 12221079-2 2002 Incubation of the purified His-tagged ROMK1 protein with PKC and radiolabeled ATP resulted in (32)P incorporation into ROMK1 detected by autoradiography. Adenosine Triphosphate 78-81 potassium inwardly rectifying channel subfamily J member 1 Homo sapiens 119-124 11956191-6 2002 The affinities for TNP-ATP binding to K(ATP) COOH termini of Kir1.1, Kir6.1, and Kir6.2 were similar. Adenosine Triphosphate 23-26 potassium inwardly rectifying channel subfamily J member 1 Homo sapiens 61-67 11956191-9 2002 Competition of TNP-ATP binding to the Kir1.1 COOH terminus by MgATP was complex with both Mg(2+) and MgATP effects. Adenosine Triphosphate 19-22 potassium inwardly rectifying channel subfamily J member 1 Homo sapiens 38-44 11956191-9 2002 Competition of TNP-ATP binding to the Kir1.1 COOH terminus by MgATP was complex with both Mg(2+) and MgATP effects. Adenosine Triphosphate 62-67 potassium inwardly rectifying channel subfamily J member 1 Homo sapiens 38-44 11956191-9 2002 Competition of TNP-ATP binding to the Kir1.1 COOH terminus by MgATP was complex with both Mg(2+) and MgATP effects. Adenosine Triphosphate 101-106 potassium inwardly rectifying channel subfamily J member 1 Homo sapiens 38-44 31441846-2 2019 We present 1 case with Bartter syndrome, due to a novel compound heterozygous mutation in the KCNJ1 gene encoding the ATP-sensitive inward rectifier potassium channel in the thick ascending limb of the loop of Henle. Adenosine Triphosphate 118-121 potassium inwardly rectifying channel subfamily J member 1 Homo sapiens 94-99 10600928-5 1999 This notion is supported by recent reports showing that cystic fibrosis transmembrane conductance regulator (CFTR) and A kinase anchoring proteins (AKAP) interact with the ROMK channels to restore the response to ATP sensitivity and protein kinase A stimulation. Adenosine Triphosphate 213-216 potassium inwardly rectifying channel subfamily J member 1 Homo sapiens 172-176 8770158-3 1996 Additionally, ROMK1 contains a putative carboxy-terminal ATP-binding site. Adenosine Triphosphate 57-60 potassium inwardly rectifying channel subfamily J member 1 Homo sapiens 14-19 8770158-4 1996 Although ROMK1 channel activity could be reactivated by cytosolic Mg-ATP after rundown, the role of nucleotides in channel gating was less certain. Adenosine Triphosphate 66-72 potassium inwardly rectifying channel subfamily J member 1 Homo sapiens 9-14 8770158-6 1996 Differences in the amino terminus of ROMK isoforms alters the sensitivity of the channel-gating mechanism to ATP. Adenosine Triphosphate 109-112 potassium inwardly rectifying channel subfamily J member 1 Homo sapiens 37-41 8621594-0 1996 Phosphorylation of the ATP-sensitive, inwardly rectifying K+ channel, ROMK, by cyclic AMP-dependent protein kinase. Adenosine Triphosphate 23-26 potassium inwardly rectifying channel subfamily J member 1 Homo sapiens 70-74 11880626-4 2002 We have shown that maltose-binding fusion proteins (MBP) containing the COOH termini of K(ATP) channels (Kir1.1, Kir6.1, and Kir6.2) form functional tetramers that directly bind at least two ATP molecules with negative cooperativity. Adenosine Triphosphate 90-93 potassium inwardly rectifying channel subfamily J member 1 Homo sapiens 105-111 11880626-7 2002 A role for head group charge was supported by polycations (neomycin, spermine, and polylysine) reversing the effect of PIP2 on TNP-ATP binding to the Kir1.1 channel COOH terminal fusion protein. Adenosine Triphosphate 131-134 potassium inwardly rectifying channel subfamily J member 1 Homo sapiens 150-156 9620703-3 1998 The channel is only 38% identical to its closest relative, Kir1.3 (Kir1-ATP-regulated inward rectifier K+ [ROMK] family) and displays none of the functional properties unique to the ROMK class. Adenosine Triphosphate 72-75 potassium inwardly rectifying channel subfamily J member 1 Homo sapiens 107-111 9391167-6 1997 When bathed in electrolyte solution that contained the catalytic subunit of protein kinase A and 0.1 mM ATP (conditions that activate the native ion channel), we found stochastically occurring height fluctuations in the ROMK1 molecule. Adenosine Triphosphate 104-107 potassium inwardly rectifying channel subfamily J member 1 Homo sapiens 220-225 9374837-1 1997 The ATP-sensitive, inwardly rectifying K+ channel, ROMK, has been suggested to be the low-conductance ATP-sensitive K+ channel identified in apical membranes of mammalian renal thick ascending limb (TAL) and cortical collecting duct (CCD). Adenosine Triphosphate 4-7 potassium inwardly rectifying channel subfamily J member 1 Homo sapiens 51-55 8710944-12 1996 This change (which was reversible) suggests that ATP induces a structural change in the ROMK1 protein. Adenosine Triphosphate 49-52 potassium inwardly rectifying channel subfamily J member 1 Homo sapiens 88-93 20179498-6 2010 It had no effect on the closely related, adenosine triphosphate (ATP)-regulated Kir1.1 channel and failed to activate an ATP-insensitive mutant version of Kir6.2. Adenosine Triphosphate 65-68 potassium inwardly rectifying channel subfamily J member 1 Homo sapiens 80-86 17326663-5 2007 Examination of the intracellular domains revealed key structural differences between Kir1.1 and Kir6.2 which may explain the difference in channel inhibition by ATP. Adenosine Triphosphate 161-164 potassium inwardly rectifying channel subfamily J member 1 Homo sapiens 85-91