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Search results 1 to 90 out of 90 for Nifk

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Hits by Strain

Hits by Category

Type Details Score
Gene
509598 | NIFK
Type: gene
Organism: cattle
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Gene
100856252 | NIFK
Type: gene
Organism: dog, domestic
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Gene
424239 | NIFK
Type: gene
Organism: chicken
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Gene
317644 | nifk
Type: gene
Organism: zebrafish
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Gene
697198 | NIFK
Type: gene
Organism: macaque, rhesus
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Gene
448106 | nifk
Type: gene
Organism: frog, western clawed
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Gene
84365 | NIFK
Type: gene
Organism: human
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Gene
246042 | Nifk
Type: gene
Organism: rat
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Gene
459585 | NIFK
Type: gene
Organism: chimpanzee
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Protein Coding Gene
MGI:1915199 | Nifk
Type: protein_coding_gene
Organism: mouse, laboratory
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Gene
401825 | NIFKP1
Type: gene
Organism: human
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Gene
642907 | NIFKP8
Type: gene
Organism: human
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Gene
645398 | NIFKP2
Type: gene
Organism: human
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Gene
100128397 | NIFKP5
Type: gene
Organism: human
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Gene
100128707 | NIFKP4
Type: gene
Organism: human
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Gene
100132796 | NIFKP6
Type: gene
Organism: human
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Gene
100270648 | NIFKP3
Type: gene
Organism: human
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Gene
106480805 | NIFKP9
Type: gene
Organism: human
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Gene
106479049 | NIFKP7
Type: gene
Organism: human
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Gene
254128 | NIFK-AS1
Type: gene
Organism: human
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Publication
11342549 | J:70337
First Author: Takagi M
Year: 2001
Journal: J Biol Chem
Title: A novel nucleolar protein, NIFK, interacts with the forkhead associated domain of Ki-67 antigen in mitosis.
Volume: 276
Issue: 27
Pages: 25386-91
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Protein Coding Gene
MGP_CAROLIEiJ_G0014507 | -
Type: protein_coding_gene
Organism: Mus caroli
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Protein Coding Gene
MGP_129S1SvImJ_G0016390 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AJ_G0016373 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AKRJ_G0016338 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_BALBcJ_G0016333 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C3HHeJ_G0016159 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI_C57BL6J_1915199 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C57BL6NJ_G0016794 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CASTEiJ_G0015740 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CBAJ_G0016132 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_DBA2J_G0016238 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_FVBNJ_G0016237 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_LPJ_G0016309 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_NODShiLtJ_G0016262 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_NZOHlLtJ_G0016830 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_PWKPhJ_G0015526 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_WSBEiJ_G0015802 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_PahariEiJ_G0027743 | -
Type: protein_coding_gene
Organism: Mus pahari
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Protein Coding Gene
MGP_SPRETEiJ_G0015314 | -
Type: protein_coding_gene
Organism: Mus spretus
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Publication
- | J:25000
       
First Author: MGI Nomenclature Committee/Homology Group
Year: 1998
Title: MGI/HUGO Nomenclature Homology Determination
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Publication
- | J:68100
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2001
Title: RIKEN Data Curation in Mouse Genome Informatics
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Publication
- | J:265051
     
First Author: MGI and IMPC
Year: 2018
Journal: Database Release
Title: MGI Load of Endonuclease-Mediated Alleles (CRISPR) from the International Mouse Phenotyping Consortium (IMPC)
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Publication
- | J:155845
     
First Author: Wellcome Trust Sanger Institute
Year: 2010
Journal: MGI Direct Data Submission
Title: Alleles produced for the EUCOMM and EUCOMMTools projects by the Wellcome Trust Sanger Institute
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Publication
- | J:211773
     
First Author: Mouse Genome Informatics and the International Mouse Phenotyping Consortium (IMPC)
Year: 2014
Journal: Database Release
Title: Obtaining and Loading Phenotype Annotations from the International Mouse Phenotyping Consortium (IMPC) Database
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Publication
- | J:342605
       
First Author: GOA curators
Year: 2016
Title: Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
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Publication
11217851 | J:65060
First Author: Kawai J
Year: 2001
Journal: Nature
Title: Functional annotation of a full-length mouse cDNA collection.
Volume: 409
Issue: 6821
Pages: 685-90
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Publication
- | J:23000
       
First Author: MGD Nomenclature Committee
Year: 1995
Title: Nomenclature Committee Use
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Publication
- | J:141210
     
First Author: Mouse Genome Informatics (MGI) and National Center for Biotechnology Information (NCBI)
Year: 2008
Journal: Database Download
Title: Mouse Gene Trap Data Load from dbGSS
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Publication
21677750 | J:173534
First Author: Skarnes WC
Year: 2011
Journal: Nature
Title: A conditional knockout resource for the genome-wide study of mouse gene function.
Volume: 474
Issue: 7351
Pages: 337-42
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Publication
- | J:68900
     
First Author: The Jackson Laboratory Mouse Radiation Hybrid Database
Year: 2004
Journal: Database Release
Title: Mouse T31 Radiation Hybrid Data Load
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Publication
12466851 | J:80000
First Author: Okazaki Y
Year: 2002
Journal: Nature
Title: Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs.
Volume: 420
Issue: 6915
Pages: 563-73
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Publication
- | J:164563
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Title: Human to Mouse ISO GO annotation transfer
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Publication
- | J:157972
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome U74 Array Platform (A, B, C v2).
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Publication
- | J:75000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
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Publication
- | J:161428
       
First Author: Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas
Year: 2010
Title: Annotation inferences using phylogenetic trees
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Publication
- | J:53168
     
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
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Publication
- | J:91388
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
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Publication
- | J:90438
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
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Publication
- | J:155721
     
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
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Publication
- | J:155221
     
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
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Publication
- | J:63103
     
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
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Publication
- | J:262123
     
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
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Publication
- | J:144086
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
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Publication
- | J:85324
     
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
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Publication
- | J:144087
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
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Publication
12798774 | -
First Author: Magnusson C
Year: 2003
Journal: Cell Biol Int
Title: The nifk gene is widely expressed in mouse tissues and is up-regulated in denervated hind limb muscle.
Volume: 27
Issue: 6
Pages: 469-75
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Publication
2644222 | -
First Author: Joerger RD
Year: 1989
Journal: J Bacteriol
Title: Nucleotide sequence and mutational analysis of the structural genes (anfHDGK) for the second alternative nitrogenase from Azotobacter vinelandii.
Volume: 171
Issue: 2
Pages: 1075-86
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Publication
2743980 | -
First Author: Robson RL
Year: 1989
Journal: EMBO J
Title: Structural genes for the vanadium nitrogenase from Azotobacter chroococcum.
Volume: 8
Issue: 4
Pages: 1217-24
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Publication
2388847 | -
First Author: Fallik E
Year: 1990
Journal: Nucleic Acids Res
Title: Completed sequence of the region encoding the structural genes for the vanadium nitrogenase of Azotobacter chroococcum.
Volume: 18
Issue: 15
Pages: 4616
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Protein Domain
IPR014280 | Nase_Fe-Fe_bsu
Type: Family
Description: NNitrogenase, also called dinitrogenase, is the enzyme which catalyses the conversion of molecular nitrogen to ammonia (biological nitrogen fixation). The most widespread and most efficient nitrogenase contains a molybdenum cofactor. This entry, also known as the AnfK family, represents the beta subunit of the iron-only alternative nitrogenase []. It is homologous to NifK and VnfK, of the molybdenum-containing and the vanadium-containing nitrogenases, respectively.
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Protein Domain
IPR014281 | Nase_VnfK
Type: Family
Description: Nitrogenase, also called dinitrogenase, is the enzyme which catalyses the conversion of molecular nitrogen to ammonia (biological nitrogen fixation) [, ]. The most widespread and most efficient nitrogenase contains a molybdenum cofactor. This protein family, VnfK, represents the beta subunit of the vanadium-containing V nitrogenase. It is homologous to NifK and AnfK, of the molybdenum-containing and the iron-only types, respectively.
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Publication
10903367 | -
First Author: Fani R
Year: 2000
Journal: J Mol Evol
Title: Molecular evolution of nitrogen fixation: the evolutionary history of the nifD, nifK, nifE, and nifN genes.
Volume: 51
Issue: 1
Pages: 1-11
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Publication
12823187 | -
First Author: Zehr JP
Year: 2003
Journal: Environ Microbiol
Title: Nitrogenase gene diversity and microbial community structure: a cross-system comparison.
Volume: 5
Issue: 7
Pages: 539-54
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Publication
8226614 | -
First Author: Dean DR
Year: 1993
Journal: J Bacteriol
Title: Nitrogenase metalloclusters: structures, organization, and synthesis.
Volume: 175
Issue: 21
Pages: 6737-44
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Publication
7876209 | -
First Author: Roll JT
Year: 1995
Journal: J Biol Chem
Title: Characteristics of NIFNE in Azotobacter vinelandii strains. Implications for the synthesis of the iron-molybdenum cofactor of dinitrogenase.
Volume: 270
Issue: 9
Pages: 4432-7
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Publication
11913144 | -
 
First Author: Lawson DM
Year: 2002
Journal: Met Ions Biol Syst
Title: Molybdenum nitrogenases: a crystallographic and mechanistic view.
Volume: 39
Pages: 75-119
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Publication
8286368 | -
First Author: Kim J
Year: 1994
Journal: Biochemistry
Title: Nitrogenase and biological nitrogen fixation.
Volume: 33
Issue: 2
Pages: 389-97
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Protein Domain
IPR005971 | Protochlorophyllide_ATP-bd
Type: Family
Description: Synonym: dark protochlorophyllide reductaseProtochlorophyllide reductase catalyzes the reductive formation of chlorophyllide from protochlorophyllide during biosynthesis of chlorophylls and bacteriochlorophylls. Three genes, bchL, bchN and bchB, are involved in light-independent protochlorophyllide reduction in bacteriochlorophyll biosynthesis. In cyanobacteria, algae, and gymnosperms, three similar genes, chlL, chlN and chlB are involved in protochlorophyllide reduction during chlorophylls biosynthesis. BchL/chlL, bchN/chlN and bchB/chlB exhibit significant sequence similarity to the nifH, nifD and nifK subunits of nitrogenase, respectively. Nitrogenase catalyzes the reductive formation of ammonia from dinitrogen []. The light-independent (dark) form of protochlorophyllide reductase plays a key role in the ability of gymnosperms, algae, and photosynthetic bacteria to form chlorophyll in the dark. Genetic and sequence analyses have indicated that dark protochlorophyllide reductase consists of three protein subunits that exhibit significant sequence similarity to the three subunits of nitrogenase, which catalyzes the reductive formation of ammonia from dinitrogen. Dark protochlorophyllide reductase activity was shown to be dependent on the presence of all three subunits, ATP, and the reductant dithionite.The BchL peptide (ChlL in chloroplast and cyanobacteria) is an ATP-binding iron-sulphur protein of the dark form protochlorophyllide reductase, an enzyme similar to nitrogenase [].
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Protein Domain
IPR005977 | Nitrogenase_Fe_NifH
Type: Family
Description: The enzyme responsible for nitrogen fixation, the nitrogenase, shows a high degree of conservation of structure, function, and amino acid sequence across wide phylogenetic ranges. All known Mo-nitrogenases consist of two components, component I (also called dinitrogenase, or Fe-Mo protein), an alpha2beta2 tetramer encoded by the nifD and nifK genes, and component II (dinitrogenase reductase, or Fe protein) a homodimer encoded by the nifH gene [, ]which has an Fe4S4 cluster bound between the subunits and two ATP-binding domains. The Fe protein supplies energy by ATP hydrolysis, and transfers electrons from reduced ferredoxin or flavodoxin to component 1 for the reduction of molecular nitrogen to ammonia [, ]. Nitrogenase contains two unusual rare metal clusters; one of them is the iron molybdenum cofactor (FeMo-co), which is considered to be the site of dinitrogen reduction and whose biosynthesis requires the products of the nifNE operon and of some other nif genes []. It has been proposed that nifNE might serve as a scaffold upon which FeMo-co is built and then inserted into component I [].This entry represents the nitrogenase iron protein (component II), which is encoded by nifH.
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Protein Domain
IPR024564 | Nase_Mo-Fe_CF_bsu_N
Type: Domain
Description: The enzyme responsible for nitrogen fixation, the nitrogenase, shows a high degree of conservation of structure, function, and amino acid sequence across wide phylogenetic ranges. All known Mo-nitrogenases consist of two components, component I (also called dinitrogenase, or Fe-Mo protein), an alpha2beta2 tetramer encoded by the nifD and nifK genes, and component II (dinitrogenase reductase, or Fe protein) a homodimer encoded by the nifH gene [, ]which has an Fe4S4 cluster bound between the subunits and two ATP-binding domains. The Fe protein supplies energy by ATP hydrolysis, and transfers electrons from reduced ferredoxin or flavodoxin to component 1 for the reduction of molecular nitrogen to ammonia [, ]. Nitrogenase contains two unusual rare metal clusters; one of them is the iron molybdenum cofactor (FeMo-co), which is considered to be the site of dinitrogen reduction and whose biosynthesis requires the products of the nifNE operon and of some other nif genes []. It has been proposed that nifNE might serve as a scaffold upon which FeMo-co is built and then inserted into component I [].This entry represents the uncharacterised N-terminal domain of the molybdenum-iron protein beta chain, which is part of the nitrogenase complex that catalyses the key enzymatic reactions in nitrogen fixation.
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Protein Domain
IPR005974 | Nase_asu
Type: Family
Description: The enzyme responsible for nitrogen fixation, thenitrogenase, shows a high degree of conservation of structure, function, and amino acid sequence across wide phylogenetic ranges. All known Mo-nitrogenases consist of two components, component I (also called dinitrogenase, or Fe-Moprotein), an alpha2beta2 tetramer encoded by the nifD and nifK genes, and component II (dinitrogenase reductase, or Fe protein) a homodimer encoded by the nifH gene. Two operons, nifDK and nifEN, encode a tetrameric (alpha2beta2 and N2E2) enzymatic complex. Nitrogenase contains two unusual rare metal clusters; one of them is the iron molybdenum cofactor (FeMo-co), which is considered to be the site of dinitrogen reduction and whose biosynthesis requires the products of nifNE and ofsome other nif genes. It has been proposed that NifNE might serve as a scaffold uponwhich FeMo-co is built and then inserted into component I.This model represents the alpha chains of various forms of the nitrogen-fixing enzyme nitrogenase: vanadium-iron, iron-iron, and molybdenum-iron. Most examples of NifD, the molybdenum-iron type nitrogenase alpha chain, are excluded from this model and described instead by equivalog model .
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Protein Domain
IPR005972 | Nase_Mo-Fe_asu
Type: Family
Description: The enzyme responsible for nitrogen fixation, the nitrogenase, shows a high degree of conservation of structure, function, and amino acid sequence across wide phylogenetic ranges. All known Mo-nitrogenases consist of two components, component I (also called dinitrogenase, or Fe-Mo protein), an alpha2beta2 tetramer encoded by the nifD and nifK genes, and component II (dinitrogenase reductase, or Fe protein) a homodimer encoded by the nifH gene [, ]which has an Fe4S4 cluster bound between the subunits and two ATP-binding domains. The Fe protein supplies energy by ATP hydrolysis, and transfers electrons from reduced ferredoxin or flavodoxin to component 1 for the reduction of molecular nitrogen to ammonia [, ]. Nitrogenase contains two unusual rare metal clusters; one of them is the iron molybdenum cofactor (FeMo-co), which is considered to be the site of dinitrogen reduction and whose biosynthesis requires the products of the nifNE operon and of some other nif genes []. It has been proposed that nifNE might serve as a scaffold upon which FeMo-co is built and then inserted into component I [].This entry refers to the alpha subunit of the MoFe protein (component I) of molybdenum (Mo-) nitrogenase, which is encoded by the nifD gene.
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Protein Domain
IPR005976 | Nase_Mo-Fe_CF_bsu
Type: Family
Description: The enzyme responsible for nitrogen fixation, the nitrogenase, shows a high degree of conservation of structure, function, and amino acid sequence across wide phylogenetic ranges. All known Mo-nitrogenases consist of two components, component I (also called dinitrogenase, or Fe-Mo protein), an alpha2beta2 tetramer encoded by the nifD and nifK genes, and component II (dinitrogenase reductase, or Fe protein) a homodimer encoded by the nifH gene [, ]which has an Fe4S4 cluster bound between the subunits and two ATP-binding domains. The Fe protein supplies energy by ATP hydrolysis, and transfers electrons from reduced ferredoxin or flavodoxin to component 1 for the reduction of molecular nitrogen to ammonia [, ]. Nitrogenase contains two unusual rare metal clusters; one of them is the iron molybdenum cofactor (FeMo-co), which is considered to be the site of dinitrogen reduction and whose biosynthesis requires the products of the nifNE operon and of some other nif genes []. It has been proposed that nifNE might serve as a scaffold upon which FeMo-co is built and then inserted into component I [].This entry represents the molybdenum-iron protein beta chain, encoded by nifK.
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Protein Domain
IPR005973 | NifE
Type: Family
Description: The enzyme responsible for nitrogen fixation, the nitrogenase, shows a high degree of conservation of structure, function, and amino acid sequence across wide phylogenetic ranges. All known Mo-nitrogenases consist of two components, component I (also called dinitrogenase, or Fe-Mo protein), an alpha2beta2 tetramer encoded by the nifD and nifK genes, and component II (dinitrogenase reductase, or Fe protein) a homodimer encoded by the nifH gene [, ]which has an Fe4S4 cluster bound between the subunits and two ATP-binding domains. The Fe protein supplies energy by ATP hydrolysis, and transfers electrons from reduced ferredoxin or flavodoxin to component 1 for the reduction of molecular nitrogen to ammonia [, ]. Nitrogenase contains two unusual rare metal clusters; one of them is the iron molybdenum cofactor (FeMo-co), which is considered to be the site of dinitrogen reduction and whose biosynthesis requires the products of the nifNE operon and of some other nif genes []. It has been proposed that nifNE might serve as a scaffold upon which FeMo-co is built and then inserted into component I [].This entry refers to the nitrogenase MoFe cofactor biosynthesis protein encoded by the gene nifE.
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Publication
7592933 | -
First Author: Allen RM
Year: 1995
Journal: J Biol Chem
Title: Incorporation of iron and sulfur from NifB cofactor into the iron-molybdenum cofactor of dinitrogenase.
Volume: 270
Issue: 45
Pages: 26890-6
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Publication
15728375 | -
First Author: Hu Y
Year: 2005
Journal: Proc Natl Acad Sci U S A
Title: Identification of a nitrogenase FeMo cofactor precursor on NifEN complex.
Volume: 102
Issue: 9
Pages: 3236-41
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Publication
16423898 | -
First Author: Corbett MC
Year: 2006
Journal: Proc Natl Acad Sci U S A
Title: Structural insights into a protein-bound iron-molybdenum cofactor precursor.
Volume: 103
Issue: 5
Pages: 1238-43
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Protein Domain
IPR005975 | Nase_Mo-Fe_CF
Type: Family
Description: The enzyme responsible for nitrogen fixation, the nitrogenase, shows a high degree of conservation of structure, function, and amino acid sequence across wide phylogenetic ranges. All known Mo-nitrogenases consist of two components, component I (also called dinitrogenase, or Fe-Mo protein), an alpha2beta2 tetramer encoded by the nifD and nifK genes, and component II (dinitrogenase reductase, or Fe protein) a homodimer encoded by the nifH gene [, ]which has an Fe4S4 cluster bound between the subunits and two ATP-binding domains. The Fe protein supplies energy by ATP hydrolysis, and transfers electrons from reduced ferredoxin or flavodoxin to component 1 for the reduction of molecular nitrogen to ammonia [, ]. Nitrogenase contains two unusual rare metal clusters; one of them is the iron molybdenum cofactor (FeMo-co), which is considered to be the site of dinitrogen reduction and whose biosynthesis requires the products of the nifNE operon and of some other nif genes []. It has been proposed that nifNE might serve as a scaffold upon which FeMo-co is built and then inserted into component I [].This entry refers to the nitrogenase iron-molybdenum cofactor biosynthesis protein NifN, which forms an alpha2beta2 tetramer with NifE. NifN and NifE are structurally homologous to nitrogenase MoFe protein beta and alpha subunits respectively [][]. NifB-co (an iron and sulfur containing precursor of the FeMoco) from NifB is transferred to the NifEN complex where it is further processed to FeMoco. The nifEN bound precursor of FeMoco has been identified as a molybdenum-free, iron- and sulfur- containing analog of FeMoco. It has been suggested that this nifEN bound precursor also acts as a cofactor precursor in nitrogenase systems which require a cofactor other than FeMoco: i.e. iron-vanadium cofactor (FeVco) or iron only cofactor (FeFeco) [].
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Publication
10811655 | -
First Author: Fujita Y
Year: 2000
Journal: J Biol Chem
Title: Reconstitution of light-independent protochlorophyllide reductase from purified bchl and BchN-BchB subunits. In vitro confirmation of nitrogenase-like features of a bacteriochlorophyll biosynthesis enzyme.
Volume: 275
Issue: 31
Pages: 23583-8
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