PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 32179453-4 2020 Hydrogen is generated in the photocatalytic compartment by a Pt@g-C3N4 photocatalyst embedded into a hydrogen capture material composed of a polymer of intrinsic microporosity (PIM-1). Hydrogen 0-8 Pim-1 proto-oncogene, serine/threonine kinase Homo sapiens 177-182 32179453-4 2020 Hydrogen is generated in the photocatalytic compartment by a Pt@g-C3N4 photocatalyst embedded into a hydrogen capture material composed of a polymer of intrinsic microporosity (PIM-1). Hydrogen 101-109 Pim-1 proto-oncogene, serine/threonine kinase Homo sapiens 177-182 31964938-10 2020 The removal of antibiotics from water by PIM-1 is likely to be governed by both surface and pore-filling adsorption and could be facilitated by electrostatic interactions between the aromatic rings and charged functional groups as well as hydrogen bond formation between the adsorbent and adsorbate. Hydrogen 239-247 Pim-1 proto-oncogene, serine/threonine kinase Homo sapiens 41-46 31228217-3 2019 Here, we create these microstructures via the pyrolysis of a microporous polymer (PIM-1) under low concentrations of hydrogen gas. Hydrogen 117-125 Pim-1 proto-oncogene, serine/threonine kinase Homo sapiens 82-87 31228217-5 2019 The H2 assisted CMS dense membranes show a dramatic increase in p-xylene ideal permeability ( 15 times), with little loss in p-xylene/o-xylene selectivity (18.8 vs. 25.0) when compared to PIM-1 membranes pyrolyzed under a pure argon atmosphere. Hydrogen 4-6 Pim-1 proto-oncogene, serine/threonine kinase Homo sapiens 188-193 17279263-1 2007 A novel triptycene-based polymer of intrinsic microporosity (Trip-PIM) displays enhanced surface area (1065 m2 g(-1)) and reversibly adsorbs 1.65% hydrogen by mass at 1 bar/77 K and 2.71% at 10 bar/77 K. Hydrogen 147-155 Pim-1 proto-oncogene, serine/threonine kinase Homo sapiens 66-69 31066954-0 2019 The Effect of Thermal Treatment on the Hydrogen-Storage Properties of PIM-1. Hydrogen 39-47 Pim-1 proto-oncogene, serine/threonine kinase Homo sapiens 70-75 31066954-3 2019 The synthesised PIM-1 was annealed at different temperatures for varying times and then characterised for hydrogen uptake at both ambient and cryogenic temperatures. Hydrogen 106-114 Pim-1 proto-oncogene, serine/threonine kinase Homo sapiens 16-21 31157332-0 2019 Small-pore CAU-21 and porous PIM-1 in mixed-matrix membranes for improving selectivity and permeability in hydrogen separation. Hydrogen 107-115 Pim-1 proto-oncogene, serine/threonine kinase Homo sapiens 29-34 31046224-5 2019 Such enhanced separation behavior is supposed to stem from the densified membrane microstructure induced by the strong intermolecular interactions between PIM-1 and PDASS (i.e., charge transfer, pi-pi stacking, and hydrogen bonding). Hydrogen 215-223 Pim-1 proto-oncogene, serine/threonine kinase Homo sapiens 155-160 32355363-0 2017 Mechanical characterisation of polymer of intrinsic microporosity PIM-1 for hydrogen storage applications. Hydrogen 76-84 Pim-1 proto-oncogene, serine/threonine kinase Homo sapiens 66-71 32355363-7 2017 It was found that the film is thermally stable at low temperatures, down to -150 C, and decomposition of the material occurs at 350 C. These results suggest that PIM-1 has sufficient elasticity to withstand the elastic deformations occurring within state-of-the-art high-pressure hydrogen storage tanks and sufficient thermal stability to be applied at the range of temperatures necessary for gas storage applications. Hydrogen 282-290 Pim-1 proto-oncogene, serine/threonine kinase Homo sapiens 164-169 26275107-3 2015 Crystallographic analysis of Pim-1 bound to hispidulin reveals a binding mode distinct from that of quercetin, suggesting that the binding potency of flavonoids is determined by their hydrogen-bonding interactions with the hinge region of the kinase. Hydrogen 184-192 Pim-1 proto-oncogene, serine/threonine kinase Homo sapiens 29-34 22733119-6 2012 A cocrystal structure of one metallo-phthalimide with the protein kinase Pim1 confirmed an ATP-competitive binding with the intended hydrogen bonding between the phthalimide moiety and the hinge region of the ATP-binding site. Hydrogen 133-141 Pim-1 proto-oncogene, serine/threonine kinase Homo sapiens 73-77 22854122-7 2012 Structural and molecular interaction studies on the training and test sets suggest that designing novel compounds hydrogen bond with Asp128 in the bioactive region of Pim-1 kinase would result in therapeutic success. Hydrogen 114-122 Pim-1 proto-oncogene, serine/threonine kinase Homo sapiens 167-172 17251021-3 2007 A hydrogen bond matrix involving the Pim-1 inhibitor, two water molecules, and the catalytic core, together with a potential weak hydrogen bond between an aromatic hydrogen on the R(1) phenyl ring and a main-chain carbonyl of Pim-1, accounts for the overall potency of this inhibitor. Hydrogen 130-138 Pim-1 proto-oncogene, serine/threonine kinase Homo sapiens 226-231 17251021-3 2007 A hydrogen bond matrix involving the Pim-1 inhibitor, two water molecules, and the catalytic core, together with a potential weak hydrogen bond between an aromatic hydrogen on the R(1) phenyl ring and a main-chain carbonyl of Pim-1, accounts for the overall potency of this inhibitor. Hydrogen 130-138 Pim-1 proto-oncogene, serine/threonine kinase Homo sapiens 226-231 29670058-3 2018 The chemical structure of C-PIM was characterised by 1H NMR, 13C NMR, FTIR, elemental analysis, UV-Vis, TGA and TGA-MS. Hydrogen 53-55 Pim-1 proto-oncogene, serine/threonine kinase Homo sapiens 28-31 24860196-6 2014 Thus, for the H2/CO2 gas pair, whereas PIM-1 favors CO2, amine-PIM-1 shows permselectivity toward H2, breaking the Robeson 2008 upper bound. Hydrogen 98-100 Pim-1 proto-oncogene, serine/threonine kinase Homo sapiens 63-68 21507633-4 2011 X-ray structures of the inhibitor/Pim-1 binding complex reveal important salt-bridge and hydrogen bond interactions mediated by the compound"s carboxylic acid and amino groups. Hydrogen 89-97 Pim-1 proto-oncogene, serine/threonine kinase Homo sapiens 34-39 18790640-3 2008 Installing a hydroxyl group on the benzene ring of the core has the potential to form a key hydrogen bond interaction to the hinge region of the binding pocket and thus resulted in the most potent inhibitor, 19, with K(i) values at 2.5 and 43.5 nM against Pim-1 and Pim-2, respectively. Hydrogen 92-100 Pim-1 proto-oncogene, serine/threonine kinase Homo sapiens 256-261 17218638-5 2007 Resolution of the crystal structure of PIM1 in complex with quercetagetin or two other flavonoids revealed a spectrum of binding poses and hydrogen-bonding patterns in spite of strong similarity of the ligands. Hydrogen 139-147 Pim-1 proto-oncogene, serine/threonine kinase Homo sapiens 39-43 16302800-2 2005 The three-dimensional structure of PIM-1 is characterized by an unique hinge region which lacks a second hydrogen bond donor and makes it particularly important to determine how inhibitors bind to this kinase. Hydrogen 105-113 Pim-1 proto-oncogene, serine/threonine kinase Homo sapiens 35-40 15808862-5 2005 Pim1 is unique among protein kinases due to the presence of a proline residue at position 123 that precludes the formation of the canonical second hydrogen bond between the hinge backbone and the adenine moiety of ATP. Hydrogen 147-155 Pim-1 proto-oncogene, serine/threonine kinase Homo sapiens 0-4 35490326-7 2022 Binding mode analysis showed that hydrogen bond, hydrophobic and pi-pi stacking interactions dominated the bindings of these compounds to Pim-1. Hydrogen 34-42 Pim-1 proto-oncogene, serine/threonine kinase Homo sapiens 138-143 15525646-7 2005 2) The hinge region has a novel architecture and hydrogen-bonding pattern, which not only expand the ATP pocket but also serve to establish unambiguously the alignment of the Pim-1 hinge region with that of other kinases. Hydrogen 49-57 Pim-1 proto-oncogene, serine/threonine kinase Homo sapiens 175-180 34388430-11 2022 Meanwhile, the fluorescence intensity of PIM declines with the decrease of pH because the Schiff base of PIM is hydrolyzed, which was affirmed by 1H NMR, LC-MS and fluorescence spectra. Hydrogen 146-148 Pim-1 proto-oncogene, serine/threonine kinase Homo sapiens 41-44 34388430-11 2022 Meanwhile, the fluorescence intensity of PIM declines with the decrease of pH because the Schiff base of PIM is hydrolyzed, which was affirmed by 1H NMR, LC-MS and fluorescence spectra. Hydrogen 146-148 Pim-1 proto-oncogene, serine/threonine kinase Homo sapiens 105-108 35346675-5 2022 Secondly, molecular dynamics simulations of heterodimeric STAT3-PIM1 complex with curcumin revealed binding of curcumin on PIM-1 interface of the complex through hydrogen bonds (Asp155) and hydrophobic interactions (Leu13, Phe18, Val21, etc.) Hydrogen 162-170 Pim-1 proto-oncogene, serine/threonine kinase Homo sapiens 64-68 35346675-5 2022 Secondly, molecular dynamics simulations of heterodimeric STAT3-PIM1 complex with curcumin revealed binding of curcumin on PIM-1 interface of the complex through hydrogen bonds (Asp155) and hydrophobic interactions (Leu13, Phe18, Val21, etc.) Hydrogen 162-170 Pim-1 proto-oncogene, serine/threonine kinase Homo sapiens 123-128