PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 32205448-0 2020 A neuroglobin-based hig-affinity ligand trap reverses carbon monoxide-induced mitochondrial poisoning. Carbon Monoxide 54-69 neuroglobin Homo sapiens 2-13 29566507-0 2018 Photoinduced transport in an H64Q neuroglobin antidote for carbon monoxide poisoning. Carbon Monoxide 59-74 neuroglobin Homo sapiens 34-45 29566507-6 2018 This leads to the decrease of the distal pocket volume in H64Q Ngb in comparison to WT Ngb, trapping migrating CO molecules in the distal pocket. Carbon Monoxide 111-113 neuroglobin Homo sapiens 63-66 29566507-6 2018 This leads to the decrease of the distal pocket volume in H64Q Ngb in comparison to WT Ngb, trapping migrating CO molecules in the distal pocket. Carbon Monoxide 111-113 neuroglobin Homo sapiens 87-90 27928027-0 2016 Five-coordinate H64Q neuroglobin as a ligand-trap antidote for carbon monoxide poisoning. Carbon Monoxide 63-78 neuroglobin Homo sapiens 21-32 24914975-2 2014 Neuroglobin belongs to the heterogeneous group of hexacoordinate globins that have evolved in animals, plants and bacteria, endowed with the capability of reversible intramolecular coordination, allowing the binding of small gaseous ligands (O2, NO and CO). Carbon Monoxide 253-255 neuroglobin Homo sapiens 0-11 19852453-1 2009 Neuroglobin (Ngb) belongs to the large family of globular heme proteins capable of binding small gaseous ligands such as O(2), CO, or NO within their active site. Carbon Monoxide 127-129 neuroglobin Homo sapiens 0-11 19852453-1 2009 Neuroglobin (Ngb) belongs to the large family of globular heme proteins capable of binding small gaseous ligands such as O(2), CO, or NO within their active site. Carbon Monoxide 127-129 neuroglobin Homo sapiens 13-16 18778796-2 2008 In this context, particular attention is given to the reactions of small molecules such as dioxygen, carbon monoxide, and nitric oxide with selected hemoproteins (hemoglobin, myoglobin, neuroglobin and cytochrome P450(cam)), as well as to photo-induced electron transfer reactions occurring in hemoproteins (particularly in various types of cytochromes). Carbon Monoxide 101-116 neuroglobin Homo sapiens 186-197 18406335-7 2008 This preliminary result paves the way to experiments aimed at the characterization of pentacoordinate ferrous Ngb, the only species competent in binding external ligands such as O2, CO or NO. Carbon Monoxide 182-184 neuroglobin Homo sapiens 110-113 17701543-4 2007 In recent years, the molecular structures of Ngb with carbon monoxide bound to the heme iron and without an exogenous ligand have been solved, and interesting structural changes have been noticed upon ligand binding. Carbon Monoxide 54-69 neuroglobin Homo sapiens 45-48 23345908-0 2005 A spectroscopic study of structural heterogeneity and carbon monoxide binding in neuroglobin. Carbon Monoxide 54-69 neuroglobin Homo sapiens 81-92 23345908-1 2005 Neuroglobin (Ngb) is a small globular protein that binds diatomic ligands like oxygen, carbon monoxide (CO) and nitric oxide at a heme prosthetic group. Carbon Monoxide 87-102 neuroglobin Homo sapiens 0-11 23345908-1 2005 Neuroglobin (Ngb) is a small globular protein that binds diatomic ligands like oxygen, carbon monoxide (CO) and nitric oxide at a heme prosthetic group. Carbon Monoxide 87-102 neuroglobin Homo sapiens 13-16 23345908-1 2005 Neuroglobin (Ngb) is a small globular protein that binds diatomic ligands like oxygen, carbon monoxide (CO) and nitric oxide at a heme prosthetic group. Carbon Monoxide 104-106 neuroglobin Homo sapiens 0-11 23345908-1 2005 Neuroglobin (Ngb) is a small globular protein that binds diatomic ligands like oxygen, carbon monoxide (CO) and nitric oxide at a heme prosthetic group. Carbon Monoxide 104-106 neuroglobin Homo sapiens 13-16 16201751-3 2005 Picosecond time-resolved resonance Raman (ps-TR3) spectroscopy of transient five-coordinate heme species produced by the photolysis of carbon monoxide (CO) adducts of Cgb and Ngb showed Fe-His stretching (nu(Fe-His)) bands at 229 and 221 cm(-1), respectively. Carbon Monoxide 135-150 neuroglobin Homo sapiens 175-178 21332165-0 2011 Kinetics of carbon monoxide migration and binding in solvated neuroglobin as revealed by molecular dynamics simulations and quantum mechanical calculations. Carbon Monoxide 12-27 neuroglobin Homo sapiens 62-73 21332165-3 2011 In this Article, by using multiple (independent) molecular dynamics trajectories (about 500 ns in total), the migration pathways of photolized carbon monoxide (CO) within solvated Ngb were analyzed, and a quantitative description of CO migration and corresponding kinetics was obtained. Carbon Monoxide 143-158 neuroglobin Homo sapiens 180-183 21332165-3 2011 In this Article, by using multiple (independent) molecular dynamics trajectories (about 500 ns in total), the migration pathways of photolized carbon monoxide (CO) within solvated Ngb were analyzed, and a quantitative description of CO migration and corresponding kinetics was obtained. Carbon Monoxide 160-162 neuroglobin Homo sapiens 180-183 21332165-4 2011 MD results, combined with quantum mechanical calculations on the CO-heme binding-unbinding reaction step in Ngb, allowed construction of a quantitative model representing the relevant steps of CO migration and rebinding. Carbon Monoxide 65-67 neuroglobin Homo sapiens 108-111 19919085-5 2009 We have studied the diffusion of small ligands (CO, NO, and O(2)) in the globin internal cavity network for various states of human Ngb. Carbon Monoxide 48-50 neuroglobin Homo sapiens 132-135 17077295-4 2006 Structural studies revealed that neuroglobin has a typical globin fold, and despite being hexacoordinated, it binds reversibly O2, CO, and NO, undergoing a substantial conformational change of the heme and of the protein. Carbon Monoxide 131-133 neuroglobin Homo sapiens 33-44