Mutations in FKBP10 cause recessive osteogenesis imperfecta and Bruck syndrome - Wikidata - wikimedia - TriplyDB

Mutations in FKBP10 cause recessive osteogenesis imperfecta and Bruck syndrome

Mutations in FKBP10 cause recessive osteogenesis imperfecta and Bruck syndrome

http://www.wikidata.org/entity/Q35229875

about

Mutations in SERPINF1 cause osteogenesis imperfecta type VI Recent developments in osteogenesis imperfecta Osteogenesis imperfecta due to mutations in non-collagenous genes: lessons in the biology of bone formation Bisphosphonate therapy in pediatric patients Bone collagen: new clues to its mineralization mechanism from recessive osteogenesis imperfecta New genes in bone development: what's new in osteogenesis imperfecta Structure of human peptidyl-prolylcis-transisomerase FKBP22 containing two EF-hand motifs Endoplasmic reticulum stress in chondrodysplasias caused by mutations in collagen types II and X Novel mutations in FKBP10 and PLOD2 cause rare Bruck syndrome in Chinese patients Prolyl 3-hydroxylase-1 null mice exhibit hearing impairment and abnormal morphology of the middle ear bone joints.Integration of zebrafish fin regeneration genes with expression data of human tumors in silico uncovers potential novel melanoma markers.The ever-expanding conundrum of primary osteoporosis: aetiopathogenesis, diagnosis, and treatment.The swaying mouse as a model of osteogenesis imperfecta caused by WNT1 mutations Recent advances in osteogenesis imperfecta.Connective tissue alterations in Fkbp10-/- mice.Mutations in FKBP10 can cause a severe form of isolated Osteogenesis imperfecta.Mutations in FKBP14 cause a variant of Ehlers-Danlos syndrome with progressive kyphoscoliosis, myopathy, and hearing loss First mouse model for combined osteogenesis imperfecta and Ehlers-Danlos syndrome.Chaperoning osteogenesis: new protein-folding disease paradigms.A transgenic mouse model of OI type V supports a neomorphic mechanism of the IFITM5 mutation HSP47 and FKBP65 cooperate in the synthesis of type I procollagen.Peptidyl 3-hydroxyproline binding properties of type I collagen suggest a function in fibril supramolecular assembly Osteogenesis Imperfecta: A Review with Clinical Examples.Osteoblastic differentiation of bone marrow mesenchymal stromal cells in Bruck Syndrome FK506-Binding Protein 10, a Potential Novel Drug Target for Idiopathic Pulmonary Fibrosis Absence of FKBP10 in recessive type XI osteogenesis imperfecta leads to diminished collagen cross-linking and reduced collagen deposition in extracellular matrix.Comparison of bone tissue properties in mouse models with collagenous and non-collagenous genetic mutations using FTIRI.Genetic epidemiology, prevalence, and genotype-phenotype correlations in the Swedish population with osteogenesis imperfecta.Mutations in FKBP10, which result in Bruck syndrome and recessive forms of osteogenesis imperfecta, inhibit the hydroxylation of telopeptide lysines in bone collagen.Next-generation sequencing for disorders of low and high bone mineral density.Disentangling mechanisms involved in collagen pyridinoline cross-linking: The immunophilin FKBP65 is critical for dimerization of lysyl hydroxylase 2 Kuskokwim syndrome, a recessive congenital contracture disorder, extends the phenotype of FKBP10 mutations.Deficiency for the ER-stress transducer OASIS causes severe recessive osteogenesis imperfecta in humans.New perspectives on osteogenesis imperfecta Recessive osteogenesis imperfecta: clinical, radiological, and molecular findings.Functional diversity and pharmacological profiles of the FKBPs and their complexes with small natural ligands.Osteogenesis imperfecta: diagnosis and treatment.Lysyl Hydroxylase 2 Is Secreted by Tumor Cells and Can Modify Collagen in the Extracellular Space.IFITM5 mutations and osteogenesis imperfecta.Heat shock protein 47 and 65 KDa FK506 binding protein weakly but synergistically interact during collagen folding in the endoplasmic reticulum.

P2860

Q24629521-D6768DF4-7FAF-4073-BC3D-9B63F4FEB4B8 Q26781674-AE06EB84-BDCB-49DA-B976-10BF02B3BC59 Q26824200-A6080843-BB48-41F0-8C53-200F68F0F51E Q26830702-129F4CFC-995C-4C2B-9D6F-235AE8854431 Q26862184-1CD48167-A46D-40EE-B472-B39BC78B8885 Q26864752-059C3011-E094-4730-B46A-3513BD730816 Q27680678-55B5876B-3D1C-440E-8C1A-59ADB5037364 Q28073452-929119E3-23D8-4745-9F24-F9A1627C1EA9 Q28543099-F3C65A42-89C9-44F6-8507-F6DC0032B49C Q30445165-E1AE57D4-E7A6-4E7D-93DE-A75EF3B113C9 Q31133977-68227D27-016F-4950-9AC2-E770F8B82693 Q33781943-A86AF33F-1CE0-4A30-B416-F333FCCA1BCD Q33847609-819E7CE4-7863-46B5-AB06-AA5592C0D60E Q34031264-83EF82CC-0951-498A-A236-758A76F8BBBF Q34074505-C9134EB2-0CD8-4695-80E5-520641F0EC1F Q34080220-A63070AB-8B67-4919-AAA2-8E8298353A6F Q34248693-52B807CE-896A-4548-A523-A1E629D94A8E Q34398977-146166B5-F2BF-41BB-AA84-194794DE94E6 Q34672644-89ABCF3A-4B4A-4D78-91E5-922E5FCAF7BA Q35096701-3C703574-4765-4928-AD8F-BDC9C5321652 Q35163465-E1CDDD93-9FE6-473E-97EE-F68D69C22B92 Q35858452-F018675B-D5E5-4B0C-9791-B57717F0D0A9 Q35932671-9C0CA5F7-9D04-46E1-84E4-5272C9B4F432 Q36008701-2B57B753-3B4B-4380-93B9-C6FE0EAD180D Q36128503-2F595DCA-5F56-4F4A-A471-A7BC22E50241 Q36315415-3DD0D8FF-97FC-40F7-8E9D-4313AB6D01E7 Q36642684-686D8553-7D45-42DB-B3F4-2F7C4DAF28D7 Q36695362-9F3878AE-5D2E-4399-8B27-0688EE400593 Q36709687-E40C5936-B05F-4EB8-9CCF-6696561A4B80 Q37004612-E4DE3C10-70FA-4F37-9D53-2CD0DF979B69 Q37065130-B7917815-AC6F-48D8-AC7B-51742B4886BD Q37164274-35FC300D-A463-4583-9851-88E205C60B1C Q37363516-DE9FE5BA-0E26-4512-99F7-F3AF2D115730 Q37889113-F037D5CF-4062-409A-B712-0FFDCAF537EB Q38025998-BE096FFF-2DB4-4B33-B860-DB132CA0E5FF Q38065993-6952F825-6F92-4FD0-808D-6BA2F0CD00D4 Q38223208-E7A7E201-0279-4E64-87A1-A36B332AE137 Q38435130-97ED455D-3AD4-4BDC-9B3D-12D6A7032708 Q38511204-C14AE463-9E46-40A1-979B-9C905301AE89 Q38599183-778CD726-3BF4-4573-BB0B-54EDE6DF4634

P2860

Mutations in FKBP10 cause recessive osteogenesis imperfecta and Bruck syndrome

http://www.wikidata.org/entity/Q35229875

description

2011 nî lūn-bûn

@nan

2011 թուականի Մարտին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի մարտին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

Mutations in FKBP10 cause recessive osteogenesis imperfecta and Bruck syndrome

@ast

Mutations in FKBP10 cause recessive osteogenesis imperfecta and Bruck syndrome

@en

type

label

Mutations in FKBP10 cause recessive osteogenesis imperfecta and Bruck syndrome

@ast

Mutations in FKBP10 cause recessive osteogenesis imperfecta and Bruck syndrome

@en

prefLabel

Mutations in FKBP10 cause recessive osteogenesis imperfecta and Bruck syndrome

@ast

Mutations in FKBP10 cause recessive osteogenesis imperfecta and Bruck syndrome

@en

P1433

Q35229875-EAC0F986-617E-4812-9488-F152BC2B64A4

P1476

Q35229875-85583FB6-92D3-49F2-A20D-16035E59CCA0

P2093

Q35229875-1F7540AE-2CD0-4679-8111-DE1376677C96

Q35229875-232C6C63-6E52-4DF7-A370-DCCF4C573A70

Q35229875-682E147B-F4A3-4D7E-ADB7-4D201E1A6C3B

Q35229875-790C2780-952D-4D5B-8D4E-102D5022624D

Q35229875-84A3349E-06C1-4E85-B958-D746B7437CD8

Q35229875-8C1807E2-F8C6-4F3B-80BA-9F08926AB90A

Q35229875-8ECAACC3-54C1-4C04-B356-ABCF723460C9

Q35229875-A2506FEA-743C-4E5E-9E2C-1A945C667783

Q35229875-A7DE0897-468E-414F-8B7B-8BE86821EBDC

Q35229875-BB215C76-A22C-486B-94A8-A18984DEDAC2

P2860

Q35229875-0487B530-7372-4752-8EE6-6D740F5A06FB

Q35229875-1DEB4FBB-4FE2-44F9-B81A-66C77257A8EB

Q35229875-23C6A1DC-1CBF-4240-86DB-32BC4E326893

Q35229875-3B1445BA-D775-47F6-9F83-8703F7615297

Q35229875-565B3F95-FC95-4F08-8B8E-81E20DDD5FC7

Q35229875-66F72F81-4952-4E13-A194-9A97888DFA95

Q35229875-6D87943D-BB13-4ED2-807F-073727059610

Q35229875-6E332C94-CDEC-42BC-813D-21D35D407118

Q35229875-71583327-9FD0-4E3D-A4EF-1EC2CB9A5287

Q35229875-86EE5908-7CAA-4F32-B0F5-A9BB2383E97D

P304

Q35229875-FB09F937-0BC2-4111-9A20-95B92A3B3FDB

P31

Q35229875-79EB5C23-8A33-40BE-AEDE-FBB5C4945AC6

P356

Q35229875-282D8840-BF14-4EE8-818C-FACA07D282DD

P433

Q35229875-71B5DECE-93CC-426D-A560-E392DD0D0797

P478

Q35229875-949A5495-D605-4F9A-BD1D-C6546EB0B374

P50

Q35229875-0B223B13-E6C7-41C5-8E9C-5B8A01762008

Q35229875-57ADF762-6C25-4E05-A55F-E1F757D25367

Q35229875-9A0CAA3D-8A99-449E-B677-686ED67BC8E2

Q35229875-AE6A0B9B-3855-4B81-B5E9-63D6BE9312CC

Q35229875-CB166E88-9430-46F0-A6A2-C0331EFB35FB

P577

Q35229875-9A04336E-7C8F-4A1F-A16B-6B32A33D3E17

P5875

Q35229875-4B5F6C24-C3EC-4B7F-8126-6D71080D5B16

P698

Q35229875-334DB5DB-4DD7-4E28-8B70-471F60D6F467

P921

Q35229875-C077E1BB-1306-4FD6-BC88-CF61E1711948

P932

Q35229875-76F2F0BD-41A1-4C68-B766-E694D53DA1B9

P356

P1433

Journal of Bone and Mineral Research

P1476

Mutations in FKBP10 cause recessive osteogenesis imperfecta and Bruck syndrome

@en

P2093

Andy Willaert

http://www.w3.org/2001/XMLSchema#string

Brendan Lee

http://www.w3.org/2001/XMLSchema#string

Brian P Kelley

http://www.w3.org/2001/XMLSchema#string

Deborah Krakow

http://www.w3.org/2001/XMLSchema#string

Dobrawa Napierala

http://www.w3.org/2001/XMLSchema#string

Dustin Baldridge

http://www.w3.org/2001/XMLSchema#string

Erica Homan

http://www.w3.org/2001/XMLSchema#string

Luisa Bonafe

http://www.w3.org/2001/XMLSchema#string

Nursel Elcioglu

http://www.w3.org/2001/XMLSchema#string

Peter Beighton

http://www.w3.org/2001/XMLSchema#string

P2860

A missense mutation in the SERPINH1 gene in Dachshunds with osteogenesis imperfecta

Null mutations in LEPRE1 and CRTAP cause severe recessive osteogenesis imperfecta

Homozygosity for a missense mutation in SERPINH1, which encodes the collagen chaperone protein HSP47, results in severe recessive osteogenesis imperfecta

CRTAP and LEPRE1 mutations in recessive osteogenesis imperfecta

CRTAP is required for prolyl 3- hydroxylation and mutations cause recessive osteogenesis imperfecta

Defective collagen crosslinking in bone, but not in ligament or cartilage, in Bruck syndrome: indications for a bone-specific telopeptide lysyl hydroxylase on chromosome 17.

Mutations in the gene encoding the RER protein FKBP65 cause autosomal-recessive osteogenesis imperfecta.

Consortium for osteogenesis imperfecta mutations in the helical domain of type I collagen: regions rich in lethal mutations align with collagen binding sites for integrins and proteoglycans.

Bruck syndrome: congenital joint contractures with bone fragility.

Identification of PLOD2 as telopeptide lysyl hydroxylase, an important enzyme in fibrosis.

P304

666-672

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1002/JBMR.250

http://www.w3.org/2001/XMLSchema#string

P433

3

http://www.w3.org/2001/XMLSchema#string

P478

26

http://www.w3.org/2001/XMLSchema#string

P50

Andrea Superti-Furga

Lionel Van Maldergem

Fransiska Malfait

Christine Verellen-Dumoulin

P577

2011-03-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

46257213

http://www.w3.org/2001/XMLSchema#string

P698

20839288

http://www.w3.org/2001/XMLSchema#string

P921

osteogenesis imperfecta

P932

3179293

http://www.w3.org/2001/XMLSchema#string