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References from Structural and functional properties of Antarctic fish cytoglobins-1: Cold-reactivity in multi-ligand reactions. Local targets link to admitted publications; unresolved targets remain external evidence.
10.1039/b610236k
10.1039/b610236k · External reference
Isoniazid and rifampicin inhibit allosterically heme binding to albumin and peroxynitrite isomerization by heme albumin
10.1007/s00775-010-0706-2 · 2011 · External reference
Drug binding to Sudlow’s site I impairs allosterically human serum heme-albumin-catalyzed peroxynitrite detoxification
10.1002/iub.381 · 2010 · External reference
Cardiolipin modulates allosterically peroxynitrite detoxification by horse heart cytochrome C
10.1016/j.bbrc.2010.11.091 · 2011 · External reference
Peroxynitrite detoxification by horse heart carboxymethylated cytochrome c is allosterically modulated by cardiolipin
10.1016/j.bbrc.2011.10.094 · 2011 · External reference
Ibuprofen impairs allosterically peroxynitrite isomerization by ferric human serum heme-albumin
10.1074/jbc.m109.010736 · 2009 · External reference
Peroxynitrite-An ugly biofactor?
10.1002/biof.103 · 2010 · External reference
Abacavir modulates peroxynitrite-mediated oxidation of ferrous nitrosylated human serum heme–albumin
10.1016/j.bbrc.2006.12.041 · 2007 · External reference
Cardiolipin modulates allosterically the nitrite reductase activity of horse heart cytochrome c
10.1007/s00775-014-1175-9 · 2014 · External reference
The nitrite reductase activity of ferrous human hemoglobin: haptoglobin 1–1 and 2–2 complexes
10.1016/j.jinorgbio.2018.07.005 · 2018 · External reference
Warfarin modulates the nitrite reductase activity of ferrous human serum heme–albumin
10.1007/s00775-013-1040-2 · 2013 · External reference
Coupling of disulfide bond and distal histidine dissociation in human ferrous cytoglobin regulates ligand binding
10.1016/j.febslet.2015.01.010 · 2015 · External reference
Engineered chimeras reveal the structural basis of hexacoordination in globins: a case study of neuroglobin and myoglobin
2015 · External reference
10.1021/bc900130f
10.1021/bc900130f · External reference
High pressure reveals structural determinants for globin hexacoordination: neuroglobin and myoglobin cases
10.1002/prot.22297 · 2009 · External reference
Unresolved reference
External reference
Molecular ecophysiology of Antarctic notothenioid fishes
10.1098/rstb.2006.1946 · 2007 · External reference
10.1002/iub.138
10.1002/iub.138 · External reference
3.0: A tool for the analysis of transport pathways in dynamic protein structures
10.1371/journal.pcbi.1002708 · 2012 · External reference
Kinetic evidence for the existence of a rate-limiting step in the reaction of ferric hemoproteins with anionic ligands
10.1111/j.1432-1033.1996.00049.x · 1996 · External reference
Genome evolution in the cold: Antarctic icefish muscle transcriptome reveals selective duplications increasing mitochondrial function
10.1093/gbe/evs108 · 2013 · External reference
10.1016/j.niox.2015.12.004
10.1016/j.niox.2015.12.004 · External reference
Inhibition of the activation of hepatic stellate cells by arundic acid via the induction of cytoglobin
10.1016/j.bbrc.2012.07.126 · 2012 · External reference
10.1016/j.jinorgbio.2017.04.025
10.1016/j.jinorgbio.2017.04.025 · External reference
Crystal structure of cytoglobin: the fourth globin type discovered in man displays heme hexa-coordination
10.1016/j.jmb.2003.12.063 · 2004 · External reference
10.1016/j.bbrc.2004.03.007
10.1016/j.bbrc.2004.03.007 · External reference
Antarctic fishes survive exposure to carbon-monoxide
10.1007/bf01928166 · 1992 · External reference
The Ross Sea and its rich life: research on molecular adaptive evolution of stenothermal and eurythermal Antarctic organisms and the Italian contribution Hydrobiologia
2015 · External reference
Unresolved reference
1993 · External reference
10.1107/s0907444905036693
10.1107/s0907444905036693 · External reference
Allosteric regulation and temperature dependence of oxygen binding in human neuroglobin and cytoglobin. Molecular mechanisms and physiological significance
10.1074/jbc.m407126200 · 2004 · External reference
Temperature-dependent enthalpy of oxygenation in Antarctic fish hemoglobins
10.1016/s0305-0491(97)00160-0 · 1997 · External reference
10.1074/jbc.m402011200
10.1074/jbc.m402011200 · External reference
10.1016/j.bbrc.2005.08.271
10.1016/j.bbrc.2005.08.271 · External reference
CO rebinding kinetics and molecular dynamics simulations highlight dynamic regulation of internal cavities in human cytoglobin
10.1371/journal.pone.0049770 · 2013 · External reference
Biophysical characterisation of neuroglobin of the icefish, a natural knockout for hemoglobin and myoglobin Comparison with human neuroglobin
10.1371/journal.pone.0044508 · 2012 · External reference
“Cool” adaptations to cold environments: globins in Notothenioidei Hydrobiologia
2015 · External reference
The chemistry of peroxynitrite: implications for biological activity
10.1016/s0076-6879(08)36004-2 · 2008 · External reference
10.1074/jbc.m705222200
10.1074/jbc.m705222200 · External reference
10.1074/jbc.m808231200
10.1074/jbc.m808231200 · External reference
10.1074/jbc.m309396200
10.1074/jbc.m309396200 · External reference
Neuroglobin and cytoglobin in search of their role in the vertebrate globin family
10.1016/j.jinorgbio.2004.11.009 · 2005 · External reference
Functional differentiation of myoglobin isoforms in hypoxia-tolerant carp indicates tissue-specific protective roles
10.1152/ajpregu.00501.2011 · 2012 · External reference
10.1074/jbc.m313732200
10.1074/jbc.m313732200 · External reference
Mechanistic studies of the isomerization of peroxynitrite to nitrate catalyzed by distal histidine metmyoglobin mutants
10.1021/ja0493300 · 2004 · External reference
Metmyoglobin and methemoglobin catalyze the isomerization of peroxynitrite to nitrate
10.1021/bi0350349 · 2003 · External reference
The reaction between nitrite and deoxyhemoglobin. Reassessment of reaction kinetics and stoichiometry
10.1074/jbc.m501496200 · 2005 · External reference
10.1172/jci24650
10.1172/jci24650 · External reference
10.1107/s0907444909047337
10.1107/s0907444909047337 · External reference
Characterization of a stellate cell activation-associated protein (STAP) with peroxidase activity found in rat hepatic stellate cells
10.1074/jbc.m102630200 · 2001 · External reference
Cytoglobin conformations and disulfide bond formation
2010 · External reference
Cytoglobin up-regulated by hydrogen peroxide plays a protective role in oxidative stress
10.1007/s11064-007-9317-x · 2007 · External reference
Characterization of the mechanism and magnitude of cytoglobin-mediated nitrite reduction and Nitric Oxide generation under anaerobic conditions
10.1074/jbc.m112.342378 · 2012 · External reference
10.1002/prot.22711
10.1002/prot.22711 · External reference
Cytoglobin regulates blood pressure and vascular tone through nitric oxide metabolism in the vascular wall
10.1038/ncomms14807 · 2017 · External reference
Characterization of the function of cytoglobin as an oxygen-dependent regulator of nitric oxide concentration
10.1021/bi300291h · 2012 · External reference
Differences in oxygen-dependent nitric oxide metabolism by cytoglobin and myoglobin account for their differing functional roles
10.1111/febs.12352 · 2013 · External reference
10.1002/prot.22950
10.1002/prot.22950 · External reference
10.1016/j.jinorgbio.2005.12.009
10.1016/j.jinorgbio.2005.12.009 · External reference
10.1107/s0021889807021206
10.1107/s0021889807021206 · External reference
10.1107/s0907444996012255
10.1107/s0907444996012255 · External reference
Cytoglobin, a novel member of the globin family, protects kidney fibroblasts against oxidative stress under ischemic conditions
10.1016/j.ajpath.2010.11.011 · 2011 · External reference
Cytoglobin: biochemical, functional and clinical perspective of the newest member of the globin family
10.1007/s00018-011-0764-9 · 2011 · External reference
Cytoglobin has bimodal: tumour suppressor and oncogene functions in lung cancer cell lines
10.1093/hmg/ddt174 · 2013 · External reference
10.1002/bies.201000124
10.1002/bies.201000124 · External reference
10.1016/s0969-2126(03)00166-7
10.1016/s0969-2126(03)00166-7 · External reference
Reactions of ferrous neuroglobin and cytoglobin with nitrite under anaerobic conditions
10.1016/j.jinorgbio.2008.05.008 · 2008 · External reference
Oxygen binding to heme proteins in solution, encapsulated in silica gels, and in the crystalline state
10.1016/s0076-6879(07)37016-x · 2008 · External reference
Characterization of the heme environmental structure of cytoglobin, a fourth globin in humans
10.1021/bi027067e · 2003 · External reference
10.1152/jappl.1997.82.1.86
10.1152/jappl.1997.82.1.86 · External reference
Cytoglobin is a respiratory protein in connective tissue and neurons, which is up-regulated by hypoxia
10.1074/jbc.m310540200 · 2004 · External reference
MDpocket: Open-source cavity detection and characterization on molecular dynamics trajectories
10.1093/bioinformatics/btr550 · 2011 · External reference
10.1161/01.res.0000260171.52224.6b
10.1161/01.res.0000260171.52224.6b · External reference
10.1242/jeb.02091
10.1242/jeb.02091 · External reference
10.1073/pnas.94.7.3420
10.1073/pnas.94.7.3420 · External reference
Plant and cyanobacterial hemoglobins reduce nitrite to nitric oxide under anoxic conditions
10.1021/bi2004312 · 2011 · External reference
Promotion of liver and lung tumorigenesis in DEN-treated cytoglobin-deficient mice
10.1016/j.ajpath.2011.05.006 · 2011 · External reference
Human neuroglobin functions as a redox-regulated nitrite reductase
10.1074/jbc.m110.159541 · 2011 · External reference
Nitrite reductase activity of nonsymbiotic hemoglobins from Arabidopsis thaliana
10.1021/bi300570v · 2012 · External reference
A ubiquitously expressed human hexa-coordinate hemoglobin
10.1074/jbc.m201934200 · 2002 · External reference
10.1021/ja803363p
10.1021/ja803363p · External reference
Role of PheE15 gate in ligand entry and nitric oxide detoxification function of Mycobacterium tuberculosis truncated hemoglobin N
10.1371/journal.pone.0049291 · 2012 · External reference
10.1016/j.bbapap.2013.04.009
10.1016/j.bbapap.2013.04.009 · External reference
10.1073/pnas.0710825105
10.1073/pnas.0710825105 · External reference
10.1002/cphc.201200608
10.1002/cphc.201200608 · External reference
