Type |
Details |
Score |
Genotype |
Symbol: |
Pdgfa/Pdgfa Pdgfc/Pdgfc |
Background: |
involves: 129S1/Sv * 129X1/SvJ |
Zygosity: |
cx |
Has Mutant Allele: |
true |
|
•
•
•
•
•
|
Genotype |
Symbol: |
Myf5/Myf5 |
Background: |
involves: 129S4/SvJae * C57BL/6J |
Zygosity: |
hm |
Has Mutant Allele: |
true |
|
•
•
•
•
•
|
Genotype |
Symbol: |
Myf5/Myf5 |
Background: |
involves: 129S4/SvJae * C57BL/6J |
Zygosity: |
hm |
Has Mutant Allele: |
true |
|
•
•
•
•
•
|
Genotype |
Symbol: |
Pdgfa/Pdgfa<+> Pdgfc/Pdgfc |
Background: |
involves: 129S1/Sv * 129X1/SvJ * C57BL/6 |
Zygosity: |
cx |
Has Mutant Allele: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
729
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
415
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
428
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
378
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
575
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
321
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
628
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
149
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
403
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
722
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
98
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
424
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
173
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
415
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
670
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
663
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
173
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
373
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
373
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
400
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
323
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
437
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
663
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Suriano AR |
Year: |
2005 |
Journal: |
Mol Cell Biol |
Title: |
GCF2/LRRFIP1 represses tumor necrosis factor alpha expression. |
Volume: |
25 |
Issue: |
20 |
Pages: |
9073-81 |
|
•
•
•
•
•
|
Publication |
First Author: |
Dai P |
Year: |
2009 |
Journal: |
J Immunol |
Title: |
Modulation of TLR signaling by multiple MyD88-interacting partners including leucine-rich repeat Fli-I-interacting proteins. |
Volume: |
182 |
Issue: |
6 |
Pages: |
3450-60 |
|
•
•
•
•
•
|
Publication |
First Author: |
Liu J |
Year: |
2005 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
Identification of the Wnt signaling activator leucine-rich repeat in Flightless interaction protein 2 by a genome-wide functional analysis. |
Volume: |
102 |
Issue: |
6 |
Pages: |
1927-32 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
Leucine-rich repeat flightless-interacting protein 1 (LRRFIP1) is a transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'-AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA []. It may control smooth muscle cell proliferation following artery injury through PDGFA repression and may also bind double-stranded RNA. It interacts with the leucine-rich repeat domain of human flightless-I (FliI) protein [].Leucine-rich repeat flightless-interacting protein 2 (LRRFIP2) may function as activator of the canonical Wnt signaling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin []. It positively regulates Toll-like receptor (TLR) signalling in response to agonist probably by competing with the negative FLII regulator for MYD88-binding []. |
|
•
•
•
•
•
|
Publication |
First Author: |
Saba L |
Year: |
2006 |
Journal: |
Mamm Genome |
Title: |
Candidate genes and their regulatory elements: alcohol preference and tolerance. |
Volume: |
17 |
Issue: |
6 |
Pages: |
669-88 |
|
•
•
•
•
•
|
Genotype |
Symbol: |
Pdgfa/Pdgfa Pdgfra/Pdgfra<+> |
Background: |
involves: 129S1/Sv * 129S4/SvJaeSor * 129X1/SvJ * C57BL/6 |
Zygosity: |
cx |
Has Mutant Allele: |
true |
|
•
•
•
•
•
|
Publication |
First Author: |
Ozawa T |
Year: |
2014 |
Journal: |
Cancer Cell |
Title: |
Most human non-GCIMP glioblastoma subtypes evolve from a common proneural-like precursor glioma. |
Volume: |
26 |
Issue: |
2 |
Pages: |
288-300 |
|
•
•
•
•
•
|
Publication |
First Author: |
Hoeman CM |
Year: |
2019 |
Journal: |
Nat Commun |
Title: |
ACVR1 R206H cooperates with H3.1K27M in promoting diffuse intrinsic pontine glioma pathogenesis. |
Volume: |
10 |
Issue: |
1 |
Pages: |
1023 |
|
•
•
•
•
•
|
Publication |
First Author: |
Philip B |
Year: |
2018 |
Journal: |
Cell Rep |
Title: |
Mutant IDH1 Promotes Glioma Formation In Vivo. |
Volume: |
23 |
Issue: |
5 |
Pages: |
1553-1564 |
|
•
•
•
•
•
|
Publication |
First Author: |
Smith JC |
Year: |
2007 |
Journal: |
J Proteome Res |
Title: |
A differential phosphoproteomic analysis of retinoic acid-treated P19 cells. |
Volume: |
6 |
Issue: |
8 |
Pages: |
3174-86 |
|
•
•
•
•
•
|
Publication |
First Author: |
Baguma-Nibasheka M |
Year: |
2021 |
Journal: |
Cells |
Title: |
Regulation of Transplanted Cell Homing by FGF1 and PDGFB after Doxorubicin Myocardial Injury. |
Volume: |
10 |
Issue: |
11 |
|
|
•
•
•
•
•
|
Publication |
First Author: |
Tomita Y |
Year: |
2022 |
Journal: |
Glia |
Title: |
A novel mouse model of diffuse midline glioma initiated in neonatal oligodendrocyte progenitor cells highlights cell-of-origin dependent effects of H3K27M. |
Volume: |
70 |
Issue: |
9 |
Pages: |
1681-1698 |
|
•
•
•
•
•
|
Publication |
First Author: |
Sebastian A |
Year: |
2022 |
Journal: |
Front Immunol |
Title: |
Single-cell RNA-Seq reveals changes in immune landscape in post-traumatic osteoarthritis. |
Volume: |
13 |
|
Pages: |
938075 |
|
•
•
•
•
•
|
Publication |
First Author: |
Habets GG |
Year: |
1992 |
Journal: |
Cytogenet Cell Genet |
Title: |
Sublocalization of an invasion-inducing locus and other genes on human chromosome 7. |
Volume: |
60 |
Issue: |
3-4 |
Pages: |
200-5 |
|
•
•
•
•
•
|
Publication |
First Author: |
Muratoglu SC |
Year: |
2011 |
Journal: |
PLoS One |
Title: |
Macrophage LRP1 suppresses neo-intima formation during vascular remodeling by modulating the TGF-β signaling pathway. |
Volume: |
6 |
Issue: |
12 |
Pages: |
e28846 |
|
•
•
•
•
•
|
Publication |
First Author: |
Ross JL |
Year: |
2021 |
Journal: |
Brain |
Title: |
Platelet-derived growth factor beta is a potent inflammatory driver in paediatric high-grade glioma. |
Volume: |
144 |
Issue: |
1 |
Pages: |
53-69 |
|
•
•
•
•
•
|
Publication |
First Author: |
Yie TA |
Year: |
2023 |
Journal: |
Am J Respir Cell Mol Biol |
Title: |
Hedgehog and Platelet-derived Growth Factor Signaling Intersect during Postnatal Lung Development. |
Volume: |
68 |
Issue: |
5 |
Pages: |
523-536 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
Platelet-derived growth factor (PDGF) [, ]is a potent mitogen for cells ofmesenchymal origin, including smooth muscle cells and glial cells. In both mouse and human, the PDGF signalling network consists of four ligands, PDGFA-D, and two receptors, PDGFRalpha and PDGFRbeta. All PDGFs function as secreted, disulphide-linkedhomodimers, but only PDGFA and B can form functional heterodimers. PDGFRs also function as homo- and heterodimers. All known PDGFs have characteristic `PDGF domains',which include eight conserved cysteines that are involved in inter- and intramolecular bonds.Alternate splicing of the A chain transcript can give rise to two differentforms that differ only in their C-terminal extremity. The transforming proteinof Woolly monkey sarcoma virus (WMSV) (Simian sarcoma virus), encoded by the v-sis oncogene, is derived from the B chain of PDGF.PDGFs are mitogenic during early developmental stages, driving the proliferation of undifferentiated mesenchyme and some progenitor populations. During later maturation stages, PDGF signalling has been implicated in tissue remodelling and cellular differentiation, and in inductive events involved in patterning and morphogenesis. In addition to drivingmesenchymal proliferation, PDGFs have been shown to direct the migration, differentiation and function of a variety of specialised mesenchymal and migratory cell types, both during development and in theadult animal [].PDGF is structurally related to a number of other growth factors which also form disulphide-linked homo- or heterodimers.This domain consists of the N-terminal regions of PGDF A and B. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
Platelet-derived growth factor (PDGF) [, ]is a potent mitogen for cells of mesenchymal origin, including smooth muscle cells and glial cells. In both mouse and human, the PDGF signalling network consists of four ligands, PDGFA-D, and two receptors, PDGFRalpha and PDGFRbeta. All PDGFs function as secreted, disulphide-linked homodimers, but only PDGFA and B can form functional heterodimers. PDGFRs also function as homo- and heterodimers. All known PDGFs have characteristic `PDGF domains', which include eight conserved cysteines that are involved in inter- and intramolecular bonds. Alternate splicing of the A chain transcript can give rise to two different forms that differ only in their C-terminal extremity. The transforming protein of Woolly monkey sarcoma virus (WMSV) (Simian sarcoma virus), encoded by the v-sis oncogene, is derived from the B chain of PDGF.PDGFs are mitogenic during early developmental stages, driving the proliferation of undifferentiated mesenchyme and some progenitor populations. During later maturation stages, PDGF signalling has been implicated in tissue remodelling and cellular differentiation, and in inductive events involved in patterning and morphogenesis. In addition to driving mesenchymal proliferation, PDGFs have been shown to direct the migration, differentiation and function of a variety of specialised mesenchymal and migratory cell types, both during development and in the adult animal [].PDGF is structurally related to a number of other growth factors which also form disulphide-linked homo- or heterodimers.This entry represents the beta subunit of PGDF. |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
241
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
241
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
169
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
219
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
241
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Hannink M |
Year: |
1989 |
Journal: |
Biochim Biophys Acta |
Title: |
Structure and function of platelet-derived growth factor (PDGF) and related proteins. |
Volume: |
989 |
Issue: |
1 |
Pages: |
1-10 |
|
•
•
•
•
•
|
Publication |
First Author: |
Heldin CH |
Year: |
1992 |
Journal: |
EMBO J |
Title: |
Structural and functional studies on platelet-derived growth factor. |
Volume: |
11 |
Issue: |
12 |
Pages: |
4251-9 |
|
•
•
•
•
•
|
Publication |
First Author: |
Hoch RV |
Year: |
2003 |
Journal: |
Development |
Title: |
Roles of PDGF in animal development. |
Volume: |
130 |
Issue: |
20 |
Pages: |
4769-84 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
Platelet-derived growth factor (PDGF) [, , ]is a potent mitogen for cells of mesenchymal origin, including smooth muscle cells and glial cells. In both mouse and human, the PDGF signalling network consists of four ligands, PDGFA-D, and two receptors, PDGFRalpha and PDGFRbeta. All PDGFs function as secreted, disulphide-linkedhomodimers, but only PDGFA and B can form functional heterodimers. PDGFRs also function as homo- and heterodimers. All known PDGFs have characteristic 'PDGF domains', which include eight conserved cysteines that are involved in inter- and intramolecular bonds. Alternate splicing of the A chain transcript can give rise to two different forms that differ only in their C-terminal extremity. The transforming protein of Woolly monkey sarcoma virus (WMSV) (Simian sarcoma virus), encoded by the v-sis oncogene, is derived from the B chain of PDGF.PDGFs are mitogenic during early developmental stages, driving the proliferation of undifferentiated mesenchyme and some progenitor populations. During later maturation stages, PDGF signalling has been implicated in tissue remodelling and cellular differentiation, and in inductive events involved in patterning and morphogenesis. In addition to driving mesenchymal proliferation, PDGFs have been shown to direct the migration, differentiation and function of a variety of specialised mesenchymal and migratory cell types, both during development and in the adult animal [].Other growth factors in this family include vascular endothelial growth factors B and C (VEGF-B, VEGF-C) [, ]which are active in angiogenesis and endothelial cell growth, and placenta growth factor (PlGF) which is also active in angiogenesis []. VEGF is a potent mitogen in embryonic and somatic angiogenesis with a unique specificity for vascular endothelial cells. VEGF forms homodimers and exists in 4 different isoforms. Overall, the VEGF monomer resembles that of PDGF, but its N-terminal segment is helical rather than extended.PDGF is structurally related to a number of other growth factors which also form disulphide-linked homo- or heterodimers. A cysteine knot motif is a common feature of this domain [, , ]. |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
211
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
196
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
211
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
211
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Girolamo F |
Year: |
2019 |
Journal: |
PLoS One |
Title: |
Defining the role of NG2-expressing cells in experimental models of multiple sclerosis. A biofunctional analysis of the neurovascular unit in wild type and NG2 null mice. |
Volume: |
14 |
Issue: |
3 |
Pages: |
e0213508 |
|
•
•
•
•
•
|
Publication |
First Author: |
Oefner C |
Year: |
1992 |
Journal: |
EMBO J |
Title: |
Crystal structure of human platelet-derived growth factor BB. |
Volume: |
11 |
Issue: |
11 |
Pages: |
3921-6 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Conserved_site |
Description: |
Platelet-derived growth factor (PDGF) [, , ]is a potent mitogen for cells of mesenchymal origin, including smooth muscle cells and glial cells. In both mouse and human, the PDGF signalling network consists of four ligands, PDGFA-D, and two receptors, PDGFRalpha and PDGFRbeta. All PDGFs function as secreted, disulphide-linkedhomodimers, but only PDGFA and B can form functional heterodimers. PDGFRs also function as homo- and heterodimers. All known PDGFs have characteristic 'PDGF domains', which include eight conserved cysteines that are involved in inter- and intramolecular bonds. Alternate splicing of the A chain transcript can give rise to two different forms that differ only in their C-terminal extremity. The transforming protein of Woolly monkey sarcoma virus (WMSV) (Simian sarcoma virus), encoded by the v-sis oncogene, is derived from the B chain of PDGF.PDGFs are mitogenic during early developmental stages, driving the proliferation of undifferentiated mesenchyme and some progenitor populations. During later maturation stages, PDGF signalling has been implicated in tissue remodelling and cellular differentiation, and in inductive events involved in patterning and morphogenesis. In addition to driving mesenchymal proliferation, PDGFs have been shown to direct the migration, differentiation and function of a variety of specialised mesenchymal and migratory cell types, both during development and in the adult animal [].Other growth factors in this family include vascular endothelial growth factors B and C (VEGF-B, VEGF-C) [, ]which are active in angiogenesis and endothelial cell growth, and placenta growth factor (PlGF) which is also active in angiogenesis []. VEGF is a potent mitogen in embryonic and somatic angiogenesis with a unique specificity for vascular endothelial cells. VEGF forms homodimers and exists in 4 different isoforms. Overall, the VEGF monomer resembles that of PDGF, but its N-terminal segment is helical rather than extended.PDGF is structurally related to a number of other growth factors which also form disulphide-linked homo- or heterodimers. A cysteine knot motif is a common feature of this domain [, , ].This entry represents a conserved site found in PDGF and VEGF families, amongst others, that includes four of the eight cysteines conserved in the sequences of these proteins. In PDGF, these cysteines are known to be involved in intra and inter-chain disulphide bonds []. |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
158
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
214
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
358
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Olofsson B |
Year: |
1996 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
Vascular endothelial growth factor B, a novel growth factor for endothelial cells. |
Volume: |
93 |
Issue: |
6 |
Pages: |
2576-81 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
207
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
415
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
123
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
208
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
118
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
368
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
392
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
81
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
137
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
64
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
162
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
170
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
158
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Joukov V |
Year: |
1996 |
Journal: |
EMBO J |
Title: |
A novel vascular endothelial growth factor, VEGF-C, is a ligand for the Flt4 (VEGFR-3) and KDR (VEGFR-2) receptor tyrosine kinases. |
Volume: |
15 |
Issue: |
2 |
Pages: |
290-98 |
|
•
•
•
•
•
|
Publication |
First Author: |
Maglione D |
Year: |
1993 |
Journal: |
Oncogene |
Title: |
Two alternative mRNAs coding for the angiogenic factor, placenta growth factor (PlGF), are transcribed from a single gene of chromosome 14. |
Volume: |
8 |
Issue: |
4 |
Pages: |
925-31 |
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•
•
•
•
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Publication |
First Author: |
Muller YA |
Year: |
1997 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
Vascular endothelial growth factor: crystal structure and functional mapping of the kinase domain receptor binding site. |
Volume: |
94 |
Issue: |
14 |
Pages: |
7192-7 |
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•
•
•
•
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Publication |
First Author: |
Westermark B |
Year: |
1993 |
Journal: |
Acta Oncol |
Title: |
Platelet-derived growth factor. Structure, function and implications in normal and malignant cell growth. |
Volume: |
32 |
Issue: |
2 |
Pages: |
101-5 |
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•
•
•
•
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Publication |
First Author: |
Shibuya M |
Year: |
2001 |
Journal: |
Cell Struct Funct |
Title: |
Structure and function of VEGF/VEGF-receptor system involved in angiogenesis. |
Volume: |
26 |
Issue: |
1 |
Pages: |
25-35 |
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•
•
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•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
345
 |
Fragment?: |
false |
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•
•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
370
 |
Fragment?: |
false |
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•
•
•
•
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Publication |
First Author: |
Zhou H |
Year: |
2008 |
Journal: |
J Proteome Res |
Title: |
Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis. |
Volume: |
7 |
Issue: |
9 |
Pages: |
3957-67 |
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•
•
•
•
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Publication |
First Author: |
Sweet SM |
Year: |
2009 |
Journal: |
Mol Cell Proteomics |
Title: |
Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry. |
Volume: |
8 |
Issue: |
5 |
Pages: |
904-12 |
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•
•
•
•
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Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2002 |
|
Title: |
MGC Data curation in Mouse Genome Informatics |
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•
•
•
•
•
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Publication |
First Author: |
Mouse Genome Database and National Center for Biotechnology Information Editorial Staff Collaboration |
Year: |
2001 |
|
Title: |
LocusLink Collaboration |
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•
•
•
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Publication |
First Author: |
Friedel RH |
Year: |
2007 |
Journal: |
Brief Funct Genomic Proteomic |
Title: |
EUCOMM--the European conditional mouse mutagenesis program. |
Volume: |
6 |
Issue: |
3 |
Pages: |
180-5 |
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•
•
•
•
|
Publication |
First Author: |
Park J |
Year: |
2013 |
Journal: |
Mol Cell |
Title: |
SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways. |
Volume: |
50 |
Issue: |
6 |
Pages: |
919-30 |
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•
•
•
•
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Publication |
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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•
•
•
•
•
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Publication |
First Author: |
International Mouse Strain Resource |
Year: |
2014 |
Journal: |
Database Download |
Title: |
MGI download of germline transmission data for alleles from IMSR strain data |
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•
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•
•
•
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Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2003 |
Journal: |
Database Download |
Title: |
Integrating Computational Gene Models into the Mouse Genome Informatics (MGI) Database |
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|
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•
•
•
•
•
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Publication |
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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•
•
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Publication |
First Author: |
Villén J |
Year: |
2007 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
Large-scale phosphorylation analysis of mouse liver. |
Volume: |
104 |
Issue: |
5 |
Pages: |
1488-93 |
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•
•
•
•
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Publication |
First Author: |
Wellcome Trust Sanger Institute |
Year: |
2009 |
Journal: |
MGI Direct Data Submission |
Title: |
Alleles produced for the KOMP project by the Wellcome Trust Sanger Institute |
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•
•
•
•
•
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Publication |
First Author: |
Magdaleno S |
Year: |
2006 |
Journal: |
PLoS Biol |
Title: |
BGEM: an in situ hybridization database of gene expression in the embryonic and adult mouse nervous system. |
Volume: |
4 |
Issue: |
4 |
Pages: |
e86 |
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•
•
•
•
•
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Publication |
First Author: |
Gerhard DS |
Year: |
2004 |
Journal: |
Genome Res |
Title: |
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |
Volume: |
14 |
Issue: |
10B |
Pages: |
2121-7 |
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