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2014
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UNIPROT ID/AC
9823.ENSSSCP00000000410
(1)
9823.ENSSSCP00000000606
(1)
9823.ENSSSCP00000000717
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9823.ENSSSCP00000001244
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9823.ENSSSCP00000002108
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9823.ENSSSCP00000003829
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9823.ENSSSCP00000003865
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9823.ENSSSCP00000007309
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9823.ENSSSCP00000008216
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9823.ENSSSCP00000009166
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9823.ENSSSCP00000009732
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9823.ENSSSCP00000011053
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9823.ENSSSCP00000011561
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9823.ENSSSCP00000014399
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9823.ENSSSCP00000016046
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9823.ENSSSCP00000019489
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9823.ENSSSCP00000019566
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9823.ENSSSCP00000019793
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Superficial cells are self-renewing chondrocyte progenitors, which form the articular cartilage in juvenile mice.
Not available
S-EPMC5295727
|
biostudies-literature
Cite
Revisiting the Endoscopic Third Ventriculostomy Success Score using machine learning: can we do better?
Not available
S-EPMC12551986
|
biostudies-literature
Cite
Autosomal recessive disorder otospondylomegaepiphyseal dysplasia is associated with loss-of-function mutations in the COL11A2 gene.
Not available
S-EPMC1288089
|
biostudies-literature
Cite
Mutations in LRP5 cause primary osteoporosis without features of OI by reducing Wnt signaling activity.
Not available
S-EPMC3374890
|
biostudies-literature
Cite
S.scrofa - Synovial fluid, iBAQ (Bennikeetal,jproteomeres2014)
abundance based on iBAQ, Interaction consistency score: 4.7, Coverage: 2
ORGANISM(S):
9823
2014-00-00
|
2274773369
|
PAXDB
Cite
Lethal skeletal dysplasia in mice and humans lacking the golgin GMAP-210.
Not available
S-EPMC3108191
|
biostudies-literature
Cite
Splicing mutations of 54-bp exons in the COL11A1 gene cause Marshall syndrome, but other mutations cause overlapping Marshall/Stickler phenotypes.
Not available
S-EPMC1288268
|
biostudies-literature
Cite
Loss-of-function mutations in PTPN11 cause metachondromatosis, but not Ollier disease or Maffucci syndrome.
Not available
S-EPMC3077396
|
biostudies-literature
Cite
Mutations in the transmembrane natriuretic peptide receptor NPR-B impair skeletal growth and cause acromesomelic dysplasia, type Maroteaux.
Not available
S-EPMC1182004
|
biostudies-literature
Cite
Recurrent dominant mutations affecting two adjacent residues in the motor domain of the monomeric kinesin KIF22 result in skeletal dysplasia and joint laxity.
Not available
S-EPMC3234368
|
biostudies-literature
Cite
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