(Q27640683)

6

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author name string

Xavi Carpena

1

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Suvit Loprasert

2

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Skorn Mongkolsuk

3

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Jacek Switala

4

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Peter C Loewen

Journal of Molecular Biology

5

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language of work or name

English

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publication date

21 March 2003

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published in

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volume

327

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issue

2

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page(s)

475-89

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cites work

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Effect of Distal Cavity Mutations on the Formation of Compound I in Catalase-Peroxidases

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The 2.0 A crystal structure of catalase-peroxidase from Haloarcula marismortui

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The catalase-peroxidase gene and isoniazid resistance of Mycobacterium tuberculosis

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Crystallization and preliminary X-ray analysis of catalase-peroxidase from the halophilic archaeon Haloarcula marismortui

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Crystallization and preliminary X-ray analysis of the catalase-peroxidase KatG from Burkholderia pseudomallei.

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Crystallization and preliminary X-ray analysis of the hydroperoxidase I C-terminal domain from Escherichia coli

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Inter- and intramolecular domain interactions of the catalase-peroxidase KatG from M. tuberculosis.

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Specific chemical and structural damage to proteins produced by synchrotron radiation

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The 'fingerprint' that X-rays can leave on structures

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Catalase-peroxidase (Mycobacterium tuberculosis KatG) catalysis and isoniazid activation

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The crystal structure of lignin peroxidase at 1.70 A resolution reveals a hydroxy group on the cbeta of tryptophan 171: a novel radical site formed during the redox cycle

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Structure of barley grain peroxidase refined at 1.9-A resolution. A plant peroxidase reversibly inactivated at neutral pH

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New antiviral antibiotics, kistamicins A and B. II. Structure determination

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Two syntheses of the 16- and 17-membered DEF ring systems of chloropeptin and complestatin

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Complete amino acid sequence ofProteus mirabilis PR catalase. Occurrence of a methionine sulfone in the close proximity of the active site

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Structure of the heme d of Penicillium vitale and Escherichia coli catalases.

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Identification of a novel bond between a histidine and the essential tyrosine in catalase HPII of Escherichia coli

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Structural interactions between horseradish peroxidase C and the substrate benzhydroxamic acid determined by X-ray crystallography

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Modification of the NADH of the isoniazid target (InhA) from Mycobacterium tuberculosis

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Action mechanism of antitubercular isoniazid. Activation by Mycobacterium tuberculosis KatG, isolation, and characterization of inha inhibitor

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Site-directed mutagenesis of the katG gene of Mycobacterium tuberculosis: effects on catalase-peroxidase activities and isoniazid resistance

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Comparison of isoniazid oxidation catalyzed by bacterial catalase-peroxidases and horseradish peroxidase

7 January 2021

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Processing of X-ray diffraction data collected in oscillation mode

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AMoRe: an automated package for molecular replacement

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

7 January 2021

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Refinement of macromolecular structures by the maximum-likelihood method

7 January 2021

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Improved methods for building protein models in electron density maps and the location of errors in these models

7 January 2021

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Detection, delineation, measurement and display of cavities in macromolecular structures

7 January 2021

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Mutants that alter the covalent structure of catalase hydroperoxidase II from Escherichia coli

7 January 2021

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SETOR: hardware-lighted three-dimensional solid model representations of macromolecules

7 January 2021

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Crystallization and preliminary X-ray diffraction studies of catalase-peroxidase from Synechococcus PCC 7942.

7 January 2021

1 reference

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inferred from DOI database lookup

7 January 2021

based on heuristic

Bacterial catalase-peroxidases are gene duplicated members of the plant peroxidase superfamily

1 reference

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inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1016/S0022-2836(03)00122-0

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

12628252

1 reference

Consolidated OpenCitations Corpus – April 2017