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Search results 201 to 300 out of 859 for Palm

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Type Details Score
GXD Expression
GXD Expression
Probe: MGI:3841615
Assay Type: Immunohistochemistry
Annotation Date: 2009-04-28
Strength: Strong
Sex: Not Specified
Emaps: EMAPS:1717120
Pattern: Regionally restricted
Stage: TS20
Assay Id: MGI:3841616
Age: embryonic day 12.5
Image: 1G,I
Note: Intense expression was detected at the vitreal surface of the neural retina.
Specimen Label: 1G,I
Detected: true
Specimen Num: 4
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Publication
11707320 | J:72886
First Author: Andreu N
Year: 2001
Journal: Gene
Title: PALML, a novel paralemmin-related gene mapping on human chromosome 1p21.
Volume: 278
Issue: 1-2
Pages: 33-40
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Publication
16386234 | J:106395
First Author: Basile M
Year: 2006
Journal: Arch Biochem Biophys
Title: Paralemmin interacts with D3 dopamine receptors: implications for membrane localization and cAMP signaling.
Volume: 446
Issue: 1
Pages: 60-8
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Publication
20404157 | J:160326
First Author: Maeda A
Year: 2010
Journal: Proc Natl Acad Sci U S A
Title: Palmitoylation stabilizes unliganded rod opsin.
Volume: 107
Issue: 18
Pages: 8428-33
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Publication
24003143 | J:201159
First Author: Zhou P
Year: 2013
Journal: Proc Natl Acad Sci U S A
Title: Interrogating translational efficiency and lineage-specific transcriptomes using ribosome affinity purification.
Volume: 110
Issue: 38
Pages: 15395-400
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Publication
17114649 | J:187362
First Author: Munton RP
Year: 2007
Journal: Mol Cell Proteomics
Title: Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations.
Volume: 6
Issue: 2
Pages: 283-93
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Publication
14621295 | J:86686
First Author: Okazaki N
Year: 2003
Journal: DNA Res
Title: Prediction of the coding sequences of mouse homologues of KIAA gene: III. the complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries.
Volume: 10
Issue: 4
Pages: 167-80
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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
34321999 | J:313619
 
First Author: Bedogni F
Year: 2021
Journal: Front Mol Neurosci
Title: Cell-Type-Specific Gene Expression in Developing Mouse Neocortex: Intermediate Progenitors Implicated in Axon Development.
Volume: 14
Pages: 686034
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Publication
- | J:136110
     
First Author: Velocigene
Year: 2008
Journal: MGI Direct Data Submission
Title: Alleles produced for the KOMP project by Velocigene (Regeneron Pharmaceuticals)
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Publication
- | J:238766
     
First Author: Shanghai Model Organisms Center
Year: 2017
Journal: MGI Direct Data Submission
Title: Information obtained from the Shanghai Model Organisms Center (SMOC), Shanghai, China
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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:157065
     
First Author: Helmholtz Zentrum Muenchen GmbH
Year: 2010
Journal: MGI Direct Data Submission
Title: Alleles produced for the EUCOMM and EUCOMMTools projects by the Helmholtz Zentrum Muenchen GmbH (Hmgu)
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Publication
- | J:155856
       
First Author: The Gene Ontology Consortium
Year: 2014
Title: Automated transfer of experimentally-verified manual GO annotation data to mouse-rat orthologs
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Publication
- | J:342604
       
First Author: UniProt-GOA
Year: 2012
Title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
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Publication
16141072 | J:99680
First Author: Carninci P
Year: 2005
Journal: Science
Title: The transcriptional landscape of the mammalian genome.
Volume: 309
Issue: 5740
Pages: 1559-63
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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
38355793 | J:345621
First Author: Adams DJ
Year: 2024
Journal: Nature
Title: Genetic determinants of micronucleus formation in vivo.
Volume: 627
Issue: 8002
Pages: 130-136
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Publication
14610273 | J:86696
First Author: Zambrowicz BP
Year: 2003
Journal: Proc Natl Acad Sci U S A
Title: Wnk1 kinase deficiency lowers blood pressure in mice: a gene-trap screen to identify potential targets for therapeutic intervention.
Volume: 100
Issue: 24
Pages: 14109-14
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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
- | J:326541
       
First Author: Cyagen Biosciences Inc.
Year: 2022
Title: Cyagen Biosciences Website.
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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: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: The Gene Ontology Consortium
Year: 2010
Title: Automated transfer of experimentally-verified manual GO annotation data to mouse-human orthologs
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Publication
21267068 | J:153498
First Author: Diez-Roux G
Year: 2011
Journal: PLoS Biol
Title: A high-resolution anatomical atlas of the transcriptome in the mouse embryo.
Volume: 9
Issue: 1
Pages: e1000582
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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: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:57747
     
First Author: MGI Genome Annotation Group and UniGene Staff
Year: 2015
Journal: Database Download
Title: MGI-UniGene Interconnection Effort
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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: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: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:85324
     
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
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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:155221
     
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
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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: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
11015467 | J:64836
First Author: Black TM
Year: 2000
Journal: J Nutr
Title: Palm tocotrienols protect ApoE +/- mice from diet-induced atheroma formation.
Volume: 130
Issue: 10
Pages: 2420-6
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DO Term
DOID:4398 | pustulosis of palm and sole
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Author
Palm K
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Author
Palm NW
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Author
Palm W
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Author
Palm N
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Author
Palm P
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Author
Palm D
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Author
Palm GJ
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Palm F
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Author
Palm JE
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Author
Palm MM
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Author
Palm E
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Author
Palm CJ
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Author
Palm T
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Palm J
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Palm L
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Palm G
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Palm DC
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Palm R
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Protein Domain
IPR028207 | DNA_pol_B_palm_palm
Type: Domain
Description: The catalytic region of DNA polymerase beta is split into three domains. An N-terminal fingers domain, a central palm domain and a C-terminal thumb domain. This entry represents the palm domain [].
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Protein
P51180
Organism: Mus musculus/domesticus
Length: 263  
Fragment?: false
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Protein Domain
IPR043045 | PvsD/AcsD-like_palm_helix
Type: Homologous_superfamily
Description: The achromobactin synthetase protein D (AcsD) monomer can be decomposed into three domains that resemble a cupped hand (thumb domain 1, palm domain 2 and fingers domain 3). The Domain 1 (thumb) is a three helix bundle flanked by a four stranded anti-parallel β-sheet that forms the dimer interface. Domain 2 bridges domain 1 to domain 3 and comprises a four-helix bundle sandwiched between a three-stranded antiparallel β-sheet and a two-stranded antiparallel β-sheet. Domain 3 is connected to domain 1 by a 31-residue extended loop (L4), it comprises 182 residues folded in a twisted eight-stranded antiparallel β-sheet interspersed with five α-helices and extended loops [].This superfamily represents the helix bundle of the vibrioferrin amide bond forming protein PvsD and achromobactin synthetase protein D (AcsD) palm domain. The secondary structure elements of the palm domain are interspersed with long loops, two of which, L9 and L10, point upwards from the palm and contain three absolutely conserved residues H444, N447 and D464 as well as N509 which is found only in type A and B enzymes [].
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Protein Domain
IPR023211 | DNA_pol_palm_dom_sf
Type: Homologous_superfamily
Description: DNA is the biological information that instructs cells how to exist in an ordered fashion: accurate replication is thus one of the most important events in the life cycle of a cell. This function is performed by DNA- directed DNA-polymerases ) by adding nucleotide triphosphate (dNTP) residues to the 5'-end of the growing chain of DNA, using a complementary DNA chain as a template. Small RNA molecules are generally used as primers for chain elongation, although terminal proteins may also be used for the de novo synthesis of a DNA chain. Even though there are 2 different methods of priming, these are mediated by 2 very similar polymerases classes, A and B, with similar methods of chain elongation. A number of DNA polymerases have been grouped under the designation of DNA polymerase family B. Six regions of similarity (numbered from I to VI) are found in all or a subset of the B family polymerases. The most conserved region (I) includes a conserved tetrapeptide with two aspartate residues. Its function is not yet known, however, it has been suggested that it may be involved in binding a magnesium ion. All sequences in the B family contain a characteristic DTDS motif, and possess many functional domains, including a 5'-3' elongation domain, a 3'-5' exonuclease domain [], a DNA binding domain, and binding domains for both dNTP's and pyrophosphate []. The DNA polymerase structure resembles a right hand with fingers, palm, and thumb, with an active site formed by a palm holding the catalytic residues, a thumb that binds the primer:template DNA and fingers interacting with incoming nucleotide, and the N and Exo domains extend from the finger toward the thumb [, , ]. This superfamily represents the palm domain of DNA polymerase B composed of 6-stranded β-sheet flanked by two long α-helices from one side and a short helix from the other.
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Protein Domain
IPR007100 | Birnavirus_RdRp_palm
Type: Domain
Description: RNA-directed RNA polymerase (RdRp) () is an essential protein encoded in the genomes of all RNA containing viruses with no DNA stage [, ]. It catalyses synthesis of the RNA strand complementary to a given RNA template, but the precise molecular mechanism remains unclear.The postulated RNA replication process is a two-step mechanism. First, the initiation step of RNA synthesis begins at or near the 3' end of the RNA template by means of a primer-independent (de novo) mechanism. The de novo initiation consists in the addition of a nucleotide tri-phosphate (NTP) to the 3'-OH of the first initiating NTP. During the following so-called elongation phase, this nucleotidyl transfer reaction is repeated with subsequent NTPs to generate the complementary RNA product []. All the RNA-directed RNA polymerases, and many DNA-directed polymerases, employ a fold whose organisation has been likened to the shape of a right hand with three subdomains termed fingers, palm and thumb []. Only the catalytic palm subdomain, composed of a four-stranded antiparallel β-sheet with two α-helices, is well conserved among all of these enzymes. In RdRp, the palm subdomain comprises three well conserved motifs (A, B and C). Motif A (D-x(4,5)-D) and motif C (GDD) are spatially juxtaposed; the Asp residues of these motifs are implied in the binding of Mg2+ and/or Mn2+. The Asn residue of motif B is involved in selection of ribonucleoside triphosphates over dNTPs and thus determines whether RNA is synthesised rather than DNA [].The domain organisation []and the 3D structure of the catalytic centre of a wide range of RdPp's, even those with a low overall sequence homology, are conserved. The catalytic centre is formed by several motifs containing a number of conserved amino acid residues.There are 4 superfamilies of viruses that cover all RNA containing viruses with no DNA stage:Viruses containing positive-strand RNA or double-strand RNA, except retroviruses and Birnaviridae: viral RNA-directed RNA polymerases including all positive-strand RNA viruses with no DNA stage, double-strand RNA viruses, and the Cystoviridae, Reoviridae, Hypoviridae, Partitiviridae, Totiviridae families.Mononegavirales (negative-strand RNA viruses with non-segmented genomes).Negative-strand RNA viruses with segmented genomes, i.e. Orthomyxoviruses (including influenza A, B, and C viruses, Thogotoviruses, and the infectious salmon anemia virus), Arenaviruses, Bunyaviruses, Hantaviruses, Nairoviruses, Phleboviruses, Tenuiviruses and Tospoviruses.Birnaviridae family of dsRNA viruses.The RNA-directed RNA polymerases in the first of the above superfamilies can be divided into the following three subgroups:All positive-strand RNA eukaryotic viruses with no DNA stage.All RNA-containing bacteriophages -there are two families of RNA-containing bacteriophages: Leviviridae (positive ssRNA phages) and Cystoviridae (dsRNA phages).Reoviridae family of dsRNA viruses.This entry represents the "palm"domain of RdRp from Birnavirus. These proteins lack the highly conserved Gly-Asp-Asp (GDD) sequence, a component of the proposed catalytic site of this enzyme family that exists in the conserved motif VI of the palm domain of other RNA-directed RNA polymerases [, ]. The catalytic motifs are arranged in a permuted order, thus, adopting a unique active site topology [].
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Protein Domain
IPR046812 | Birnavirus_RdRp_palm_sf
Type: Homologous_superfamily
Description: RNA-directed RNA polymerase (RdRp) () is an essential protein encoded in the genomes of all RNA containing viruses with no DNA stage [, ]. It catalyses synthesis of the RNA strand complementary to a given RNA template, but the precise molecular mechanism remains unclear.The postulated RNA replication process is a two-step mechanism. First, the initiation step of RNA synthesis begins at or near the 3' end of the RNA template by means of a primer-independent (de novo) mechanism. The de novo initiation consists in the addition of a nucleotide tri-phosphate (NTP) to the 3'-OH of the first initiating NTP. During the following so-called elongation phase, this nucleotidyl transfer reaction is repeated with subsequent NTPs to generate the complementary RNA product []. All the RNA-directed RNA polymerases, and many DNA-directed polymerases, employ a fold whose organisation has been likened to the shape of a right hand with three subdomains termed fingers, palm and thumb []. Only the catalytic palm subdomain, composed of a four-stranded antiparallel β-sheet with two α-helices, is well conserved among all of these enzymes. In RdRp, the palm subdomain comprises three well conserved motifs (A, B and C). Motif A (D-x(4,5)-D) and motif C (GDD) are spatially juxtaposed; the Asp residues of these motifs are implied in the binding of Mg2+ and/or Mn2+. The Asn residue of motif B is involved in selection of ribonucleoside triphosphates over dNTPs and thus determines whether RNA is synthesised rather than DNA [].The domain organisation []and the 3D structure of the catalytic centre of a wide range of RdPp's, even those with a low overall sequence homology, are conserved. The catalytic centre is formed by several motifs containing a number of conserved amino acid residues.There are 4 superfamilies of viruses that cover all RNA containing viruses with no DNA stage:Viruses containing positive-strand RNA or double-strand RNA, except retroviruses and Birnaviridae: viral RNA-directed RNA polymerases including all positive-strand RNA viruses with no DNA stage, double-strand RNA viruses, and the Cystoviridae, Reoviridae, Hypoviridae, Partitiviridae, Totiviridae families.Mononegavirales (negative-strand RNA viruses with non-segmented genomes).Negative-strand RNA viruses with segmented genomes, i.e. Orthomyxoviruses (including influenza A, B, and C viruses, Thogotoviruses, and the infectious salmon anemia virus), Arenaviruses, Bunyaviruses, Hantaviruses, Nairoviruses, Phleboviruses, Tenuiviruses and Tospoviruses.Birnaviridae family of dsRNA viruses.The RNA-directed RNA polymerases in the first of the above superfamilies can be divided into the following three subgroups:All positive-strand RNA eukaryotic viruses with no DNA stage.All RNA-containing bacteriophages -there are two families of RNA-containing bacteriophages: Leviviridae (positive ssRNA phages) and Cystoviridae (dsRNA phages).Reoviridae family of dsRNA viruses.This superfamily represents the "palm"domain of RdRp from Birnavirus. These proteins lack the highly conserved Gly-Asp-Asp (GDD) sequence, a component of the proposed catalytic site of this enzyme family that exists in the conserved motif VI of the palm domain of other RNA-directed RNA polymerases [, ]. The catalytic motifs are arranged in a permuted order, thus, adopting a unique active site topology []. This domain adopts and α/β structure.
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Protein Domain
IPR043172 | Prp8_domainIV_palm
Type: Homologous_superfamily
Description: Prp8 is the largest and most highly conserved spliceosomal protein and is considered a master regulator of the spliceosome. It forms a salt-stable complex with the Brr2 helicase that is required for spliceosome catalytic activation and disassembly, and with the Snu114 GTPase that regulates Brr2 activity. Prp8 consists of a phylogenetically conserved Rnase H fold along with Prp8-specific elements. The function of this domain is to help assemble and stabilise the spliceosomal catalytic core and coordinate the activities of other splicing factors []. The overall structure of Rnase H is reminiscent of a left-hand mitten, in which a central six-stranded mixed β-sheet and the surrounding α-helices of the N-terminal domain correspond to the palm, an extended β-hairpin of the N-terminal domain comprises the thumb and the α-helical C-terminal domain represents the fingers []. This entry represents the palm region of the Rnase H domain which also includes the β-hairpin thumb.
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GXD Expression
GXD Expression
Probe: MGI:5493267
Assay Type: RNA in situ
Annotation Date: 2013-07-02
Strength: Weak
Sex: Not Specified
Emaps: EMAPS:1742821
Pattern: Regionally restricted
Stage: TS21
Assay Id: MGI:5493271
Age: embryonic day 13.5
Image: 6E
Note: Weak expression in superficial layers in palm and in proximal part of digits excluding digit tips.
Specimen Label: 6E
Detected: true
Specimen Num: 12
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Protein Domain
IPR043503 | PLpro_palm_finger_dom_CoV
Type: Homologous_superfamily
Description: In coronaviruses, papain-like protease (PL(pro)) cleaves the viral replicase polyproteins at different sites releasing non-structural protein NSP1, NSP2, NSP3, and a chymotrypsin-like protease (3CLpro) that cleaves all junctions downstream of NSP4 [].Structurally, coronaviruses papain-like protease consists of a C-terminal catalytic domain containing a right-handed fingers, palm, and thumb domain organisation as well as an N-terminal Ub-like (UBL) domain [, , ].This superfamily represents the palm and finger domains found in papain-like protease from beta and gamma coronaviruses, respectively consisting of 8 and 5 antiparallel β-sheets in MERS-CoV []and 6 and 4 antiparallel β-sheets in SARS-CoV [].
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Publication
1870963 | -
First Author: Ito J
Year: 1991
Journal: Nucleic Acids Res
Title: Compilation and alignment of DNA polymerase sequences.
Volume: 19
Issue: 15
Pages: 4045-57
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Publication
8451181 | -
First Author: Braithwaite DK
Year: 1993
Journal: Nucleic Acids Res
Title: Compilation, alignment, and phylogenetic relationships of DNA polymerases.
Volume: 21
Issue: 4
Pages: 787-802
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Protein Domain
IPR001098 | DNA-dir_DNA_pol_A_palm_dom
Type: Domain
Description: Synonym(s): DNA nucleotidyltransferase (DNA-directed) DNA-directed DNA polymerases() are the key enzymes catalysing the accurate replication of DNA. They require either a small RNA molecule or a protein as a primer for the de novosynthesis of a DNA chain. A number of polymerases belong to this family [, , ].
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Publication
12421558 | -
First Author: Gorbalenya AE
Year: 2002
Journal: J Mol Biol
Title: The palm subdomain-based active site is internally permuted in viral RNA-dependent RNA polymerases of an ancient lineage.
Volume: 324
Issue: 1
Pages: 47-62
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Gene
1828 | DSG1
Type: gene
Organism: human
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Publication
19182782 | -
First Author: Schmelz S
Year: 2009
Journal: Nat Chem Biol
Title: AcsD catalyzes enantioselective citrate desymmetrization in siderophore biosynthesis.
Volume: 5
Issue: 3
Pages: 174-82
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Publication
20591188 | -
 
First Author: Anantharaman V
Year: 2010
Journal: Biol Direct
Title: Presence of a classical RRM-fold palm domain in Thg1-type 3'- 5'nucleic acid polymerases and the origin of the GGDEF and CRISPR polymerase domains.
Volume: 5
Pages: 43
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Publication
16713976 | J:113360
First Author: Czopik AK
Year: 2006
Journal: Immunity
Title: Semaphorin 7A is a negative regulator of T cell responses.
Volume: 24
Issue: 5
Pages: 591-600
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Publication
17149751 | -
First Author: Aid T
Year: 2007
Journal: J Neurosci Res
Title: Mouse and rat BDNF gene structure and expression revisited.
Volume: 85
Issue: 3
Pages: 525-35
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Publication
1729711 | -
First Author: Klenk HP
Year: 1992
Journal: Proc Natl Acad Sci U S A
Title: Component H of the DNA-dependent RNA polymerases of Archaea is homologous to a subunit shared by the three eucaryal nuclear RNA polymerases.
Volume: 89
Issue: 1
Pages: 407-10
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Publication
2110059 | -
First Author: Honka E
Year: 1990
Journal: Eur J Biochem
Title: Properties and primary structure of the L-malate dehydrogenase from the extremely thermophilic archaebacterium Methanothermus fervidus.
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Protein
A0A0J9YTZ6
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Fragment?: true
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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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