(Q27643141)

2

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John S. Olson

object named as

John S Olson

7

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author name string

Masaki Unno

1

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Grace C Chu

3

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Tadashi Yoshida

5

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Denis L Rousseau

6

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Masao Ikeda-Saito

Journal of Biological Chemistry

8

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language of work or name

English

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publication date

14 May 2004

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published in

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volume

279

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issue

20

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page(s)

21055-61

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cites work

The heme oxygenase system: a regulator of second messenger gases

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

Heme oxygenase 1 is required for mammalian iron reutilization

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

NPAS2: a gas-responsive transcription factor

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

The heme oxygenase-carbon monoxide system: a regulator of hepatobiliary function

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

The mechanism of heme oxygenase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

Autocatalytic radical reactions in physiological prosthetic heme modification

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

Bacterial heme sources: the role of heme, hemoprotein receptors and hemophores

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

Emerging strategies in microbial haem capture.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

Utilization of host iron sources by Corynebacterium diphtheriae: identification of a gene whose product is homologous to eukaryotic heme oxygenases and is required for acquisition of iron from heme and hemoglobin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

Heme degradation as catalyzed by a recombinant bacterial heme oxygenase (Hmu O) from Corynebacterium diphtheriae.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

The heme complex of Hmu O, a bacterial heme degradation enzyme from Corynebacterium diphtheriae. Structure of the catalytic site.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

The crystal structures of the ferric and ferrous forms of the heme complex of HmuO, a heme oxygenase of Corynebacterium diphtheriae

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

Degradation of heme in gram-negative bacteria: the product of the hemO gene of Neisseriae is a heme oxygenase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

Crystal structure of heme oxygenase from the gram-negative pathogen Neisseria meningitidis and a comparison with mammalian heme oxygenase-1

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

Heme-Containing Oxygenases

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

Crystal structure of rat apo-heme oxygenase-1 (HO-1): mechanism of heme binding in HO-1 inferred from structural comparison of the apo and heme complex forms

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

Crystal structure of human heme oxygenase-1.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

Catalytic mechanism of heme oxygenase through EPR and ENDOR of cryoreduced oxy-heme oxygenase and its Asp 140 mutants

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

Crystal structures of the ferric, ferrous, and ferrous-NO forms of the Asp140Ala mutant of human heme oxygenase-1: catalytic implications

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

Processing of X-ray diffraction data collected in oscillation mode

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

The CCP4 suite: programs for protein crystallography

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

Stabilizing bound O2 in myoglobin by valine68 (E11) to asparagine substitution

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

Controlling ligand binding in myoglobin by mutagenesis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

High resolution crystal structures of the deoxy, oxy, and aquomet forms of cobalt myoglobin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

Molecular cloning and characterization of TPP36 and its isoform TPP32, novel substrates of Abl tyrosine kinase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

Crystal structures of myoglobin-ligand complexes at near-atomic resolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

The catalytic pathway of cytochrome p450cam at atomic resolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

The catalytic pathway of horseradish peroxidase at high resolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

A role for highly conserved carboxylate, aspartate-140, in oxygen activation and heme degradation by heme oxygenase-1.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

Stereoselectivity of each of the three steps of the heme oxygenase reaction: hemin to meso-hydroxyhemin, meso-hydroxyhemin to verdoheme, and verdoheme to biliverdin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

The structure of deoxy- and oxy-leghaemoglobin from lupin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

Characterization of recombinant soybean leghemoglobin a and apolar distal histidine mutants

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

The structure of Ascaris hemoglobin domain I at 2.2 A resolution: molecular features of oxygen avidity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

Distal pocket polarity in ligand binding to myoglobin: structural and functional characterization of a threonine68(E11) mutant

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

Formation of two hydrogen bonds from the globin to the heme-linked oxygen molecule in Ascaris hemoglobin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

Preferred orientation of imidazole ligands in metalloporphyrins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

Oxygen and one reducing equivalent are both required for the conversion of alpha-hydroxyhemin to verdoheme in heme oxygenase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

The Oxygen and Carbon Monoxide Reactions of Heme Oxygenase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

Folding of cytochrome c initiated by submillisecond mixing

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

The Ferrous Dioxygen Complex of the Oxygenase Domain of Neuronal Nitric-oxide Synthase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

Further additions to MolScript version 1.4, including reading and contouring of electron-density maps

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

Rates of reaction of Ascaris haemoglobins with ligands.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

Kinetic isotope effects on the rate-limiting step of heme oxygenase catalysis indicate concerted proton transfer/heme hydroxylation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200

Myoglobin discriminates between O2, NO, and CO by electrostatic interactions with the bound ligand

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400491200