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Search results 1 to 69 out of 69 for Pdf

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Categories

Hits by Strain

Hits by Category

Type Details Score
Gene
64146 | PDF
Type: gene
Organism: human
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Gene
690214 | Pdf
Type: gene
Organism: rat
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Gene
610955 | PDF
Type: gene
Organism: dog, domestic
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Gene
788473 | PDF
Type: gene
Organism: cattle
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Gene
619248 | pdf
Type: gene
Organism: zebrafish
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Gene
100427223 | PDF
Type: gene
Organism: macaque, rhesus
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Gene
448425 | pdf
Type: gene
Organism: frog, western clawed
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Gene
107968879 | PDF
Type: gene
Organism: chimpanzee
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Protein Coding Gene
MGI:1915273 | Pdf
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CAROLIEiJ_G0031528 | -
Type: protein_coding_gene
Organism: Mus caroli
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Protein Coding Gene
MGP_129S1SvImJ_G0034093 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AJ_G0034073 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AKRJ_G0033999 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_BALBcJ_G0034066 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C3HHeJ_G0033778 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI_C57BL6J_1915273 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C57BL6NJ_G0034586 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CASTEiJ_G0033105 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CBAJ_G0033751 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_DBA2J_G0033906 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_FVBNJ_G0033851 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_LPJ_G0033997 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_NODShiLtJ_G0033896 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_NZOHlLtJ_G0034604 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_PWKPhJ_G0032806 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_WSBEiJ_G0033220 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_PahariEiJ_G0023128 | -
Type: protein_coding_gene
Organism: Mus pahari
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Protein Coding Gene
MGP_SPRETEiJ_G0032646 | -
Type: protein_coding_gene
Organism: Mus spretus
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Publication
- | J:223507
     
First Author: Li Y
Year: 2015
Journal: MGI Direct Data Submission
Title: Direct data submission for endonuclease mediated alleles from the Institute of Neuroscience, Chinese Academy of Sciences
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Publication
- | J:237616
     
First Author: MGI and IMPC
Year: 2017
Journal: MGI Direct Data Submission
Title: MGI Curation of Endonuclease-Mediated Alleles (CRISPR) from the International Mouse Phenotyping Consortium (IMPC)
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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
- | J:85000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2003
Title: MGI Sequence Curation Reference
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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:60000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2000
Title: Gene Ontology Annotation by electronic association of SwissProt Keywords with GO terms
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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: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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Author
Guns PDF
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Publication
21170725 | J:339031
First Author: Izumi H
Year: 2011
Journal: Brain Struct Funct
Title: Bioluminescence imaging of Arc expression enables detection of activity-dependent and plastic changes in the visual cortex of adult mice.
Volume: 216
Issue: 2
Pages: 91-104
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GO Term
GO:0042586 | peptide deformylase activity
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Publication
29528383 | J:330118
First Author: Shakeri H
Year: 2018
Journal: Cardiovasc Res
Title: Neuregulin-1 attenuates stress-induced vascular senescence.
Volume: 114
Issue: 7
Pages: 1041-1051
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Publication
33989083 | J:330106
First Author: Shakeri H
Year: 2021
Journal: Am J Physiol Heart Circ Physiol
Title: Neuregulin-1 compensates for endothelial nitric oxide synthase deficiency.
Volume: 320
Issue: 6
Pages: H2416-H2428
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Publication
34206322 | J:311312
 
First Author: Hendrickx JO
Year: 2021
Journal: Int J Mol Sci
Title: Serum Corticosterone and Insulin Resistance as Early Biomarkers in the hAPP23 Overexpressing Mouse Model of Alzheimer's Disease.
Volume: 22
Issue: 13
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Publication
- | J:241489
     
First Author: Mouse Genome Informatics Software and Curation Teams
Year: 2017
Journal: Database Release
Title: MGI Literature Triage Load
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Publication
22714332 | J:232622
First Author: Barrios R
Year: 2012
Journal: Opt Express
Title: Exponentiated Weibull distribution family under aperture averaging for Gaussian beam waves.
Volume: 20
Issue: 12
Pages: 13055-64
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Publication
25046436 | J:214226
First Author: Yu JW
Year: 2014
Journal: Lab Invest
Title: MicroRNA-29b inhibits peritoneal fibrosis in a mouse model of peritoneal dialysis.
Volume: 94
Issue: 9
Pages: 978-90
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Publication
31579944 | J:283757
First Author: Shi Y
Year: 2020
Journal: J Pathol
Title: Genetic or pharmacologic blockade of enhancer of zeste homolog 2 inhibits the progression of peritoneal fibrosis.
Volume: 250
Issue: 1
Pages: 79-94
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Protein
S4R2K0
Organism: Mus musculus/domesticus
Length: 231  
Fragment?: false
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Publication
8845003 | -
First Author: Meinnel T
Year: 1996
Journal: J Mol Biol
Title: A new subclass of the zinc metalloproteases superfamily revealed by the solution structure of peptide deformylase.
Volume: 262
Issue: 3
Pages: 375-86
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Publication
9665852 | -
First Author: Dardel F
Year: 1998
Journal: J Mol Biol
Title: Solution structure of nickel-peptide deformylase.
Volume: 280
Issue: 3
Pages: 501-13
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Publication
9846875 | -
First Author: Becker A
Year: 1998
Journal: Nat Struct Biol
Title: Iron center, substrate recognition and mechanism of peptide deformylase.
Volume: 5
Issue: 12
Pages: 1053-8
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Publication
9565550 | -
First Author: Becker A
Year: 1998
Journal: J Biol Chem
Title: Structure of peptide deformylase and identification of the substrate binding site.
Volume: 273
Issue: 19
Pages: 11413-6
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Publication
12823970 | -
First Author: Kreusch A
Year: 2003
Journal: J Mol Biol
Title: Structure analysis of peptide deformylases from Streptococcus pneumoniae, Staphylococcus aureus, Thermotoga maritima and Pseudomonas aeruginosa: snapshots of the oxygen sensitivity of peptide deformylase.
Volume: 330
Issue: 2
Pages: 309-21
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Publication
12126617 | -
First Author: Guilloteau JP
Year: 2002
Journal: J Mol Biol
Title: The crystal structures of four peptide deformylases bound to the antibiotic actinonin reveal two distinct types: a platform for the structure-based design of antibacterial agents.
Volume: 320
Issue: 5
Pages: 951-62
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Publication
11738381 | -
First Author: Giglione C
Year: 2001
Journal: Trends Plant Sci
Title: Organellar peptide deformylases: universality of the N-terminal methionine cleavage mechanism.
Volume: 6
Issue: 12
Pages: 566-72
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Publication
10931273 | -
First Author: Giglione C
Year: 2000
Journal: Mol Microbiol
Title: Peptide deformylase as a target for new generation, broad spectrum antimicrobial agents.
Volume: 36
Issue: 6
Pages: 1197-205
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Protein Domain
IPR036821 | Peptide_deformylase_sf
Type: Homologous_superfamily
Description: Peptide deformylase (PDF) is an essential metalloenzyme required for the removal of the formyl group at the N terminus of nascent polypeptide chains in eubacteria: []. The enzyme acts as a monomer and binds a single metal ion, catalysing the reaction:N-formyl-L-methionine + H2O = formate + methionyl peptideCatalytic efficiency strongly depends on the identity of the bound metal []. These enzymes utilize Fe(II) as the catalytic metal ion, which can be replaced with a nickel or cobalt ion with no loss of activity. There are two types of peptide deformylases, types I and II, which differ in structure only in the outer surface of the domain. Because these enzymes are essential only in prokaryotes (although eukaryotic gene sequences have been found), they are a target for a new class of antibacterial agents [, , , ].The structure of these enzymes is known [, ]. PDF, a zinc metalloenzyme from the mitochondrion, comprises an active core domain of 147 residues and a C-terminal tail of 21 residue. The 3D fold of the catalytic core has been determined by X-ray crystallography and NMR. Overall, the structure contains a series of anti-parallel β-strands that surround two perpendicular α-helices. The C-terminal helix contains the characteristic HEXXH motif of metalloenzymes, which is crucial for activity. The helical arrangement, and the way the histidine residues bind the zinc ion, is reminiscent of metalloproteases such as thermolysin or metzincins. However, the arrangement of secondary and tertiary structures of PDF, and the positioning of its third zinc ligand (a cysteine residue), are quite different. These discrepancies, together with notable biochemical differences, suggest that PDF constitutes a new class of zinc-metalloenzymes [].
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Protein Domain
IPR023635 | Peptide_deformylase
Type: Family
Description: Peptide deformylase (PDF) is an essential metalloenzyme required for the removal of the formyl group at the N terminus of nascent polypeptide chains in eubacteria: []. The enzyme acts as a monomer and binds a single metal ion, catalysing the reaction:N-formyl-L-methionine + H2O = formate + methionyl peptideCatalytic efficiency strongly depends on the identity of the bound metal []. These enzymes utilize Fe(II) as the catalytic metal ion, which can be replaced with a nickel or cobalt ion with no loss of activity. There are two types of peptide deformylases, types I and II, which differ in structure only in the outer surface of the domain. Because these enzymes are essential only in prokaryotes (although eukaryotic gene sequences have been found), they are a target for a new class of antibacterial agents [, , , ].The structure of these enzymes is known [, ]. PDF, a zinc metalloenzyme from the mitochondrion, comprises an active core domain of 147 residues and a C-terminal tail of 21 residue. The 3D fold of the catalytic core has been determined by X-ray crystallography and NMR. Overall, the structure contains a series of anti-parallel β-strands that surround two perpendicular α-helices. The C-terminal helix contains the characteristic HEXXH motif of metalloenzymes, which is crucial for activity. The helical arrangement, and the way the histidine residues bind the zinc ion, is reminiscent of metalloproteases such as thermolysin or metzincins. However, the arrangement of secondary and tertiary structures of PDF, and the positioning of its third zinc ligand (a cysteine residue), are quite different. These discrepancies, together with notable biochemical differences, suggest that PDF constitutes a new class of zinc-metalloenzymes [].
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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