Cellular mechanisms of connexin32 mutations associated with CNS manifestations. - Wikidata - wikimedia - TriplyDB

Cellular mechanisms of connexin32 mutations associated with CNS manifestations.

Cellular mechanisms of connexin32 mutations associated with CNS manifestations.

http://www.wikidata.org/entity/Q44059866

about

Mutations in the gene encoding gap junction protein alpha 12 (connexin 46.6) cause Pelizaeus-Merzbacher-like disease Gap junctions couple astrocytes and oligodendrocytes Human oligodendrocytes express Cx31.3: function and interactions with Cx32 mutants Loss-of-function GJA12/Connexin47 mutations cause Pelizaeus-Merzbacher-like disease Gap junctions in inherited human disorders of the central nervous system.The delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiology Systemic inflammation disrupts oligodendrocyte gap junctions and induces ER stress in a model of CNS manifestations of X-linked Charcot-Marie-Tooth disease.Cx32 and Cx47 mediate oligodendrocyte:astrocyte and oligodendrocyte:oligodendrocyte gap junction coupling.Connexin32 mutations cause loss of function in Schwann cells and oligodendrocytes leading to PNS and CNS myelination defects Phenotypes and cellular effects of GJB1 mutations causing CMT1X in a cohort of 226 Chinese CMT families.Classification and diagnosis of the inherited neuropathies.A novel missense mutation in the connexin30 causes nonsyndromic hearing loss.The role of gap junction channels during physiologic and pathologic conditions of the human central nervous system Properties of human connexin 31, which is implicated in hereditary dermatological disease and deafness.Gap junction communication in myelinating glia Connexinopathies: a structural and functional glimpse How do mutations in GJB1 cause X-linked Charcot-Marie-Tooth disease?Clinical and electrophysiological aspects of Charcot-Marie-Tooth disease.Molecular genetics of X-linked Charcot-Marie-Tooth disease.Molecular diagnostics of Charcot-Marie-Tooth disease and related peripheral neuropathies.Functional requirement for a highly conserved charged residue at position 75 in the gap junction protein connexin 32.Resetting translational homeostasis restores myelination in Charcot-Marie-Tooth disease type 1B mice Mutation Analysis of Gap Junction Protein Beta 1 and Genotype-Phenotype Correlation in X-linked Charcot-Marie-Tooth Disease in Chinese Patients Update on Charcot-Marie-Tooth disease.Conformational maturation and post-ER multisubunit assembly of gap junction proteins.Exome sequencing identification of a GJB1 missense mutation in a kindred with X-linked spinocerebellar ataxia (SCA-X1).Loss of Coupling Distinguishes GJB1 Mutations Associated with CNS Manifestations of CMT1X from Those Without CNS Manifestations.Degradation of connexins and gap junctions.Key functions for gap junctions in skin and hearing.Molecular connexin partner remodeling orchestrates connexin traffic: from physiology to pathophysiology.GJB1-associated X-linked Charcot-Marie-Tooth disease, a disorder affecting the central and peripheral nervous systems.Intraneural GJB1 gene delivery improves nerve pathology in a model of X-linked Charcot-Marie-Tooth disease.Cx29 and Cx32, two connexins expressed by myelinating glia, do not interact and are functionally distinct.Functional heterotypic interactions between astrocyte and oligodendrocyte connexins.Unusual features of central nervous system involvement in CMTX associated with a novel mutation of GJB1 gene.Gap junction pathology in multiple sclerosis lesions and normal-appearing white matter.Golgi-retained Cx32 mutants interfere with gene addition therapy for CMT1X.Identification of mutations in members of the connexin gene family as a cause of nonsyndromic deafness in Taiwan.What's the Function of Connexin 32 in the Peripheral Nervous System?

P2860

Q24534074-D33C07E7-38ED-46DF-92B9-C2EC9EE8B4C8 Q24645936-2385410F-47E9-476C-BB1D-6F0B2BDD848A Q24655300-5B7C82A3-7743-45BA-8F5B-1347B8E8C51B Q24682835-F01C5EEC-A96E-498A-A99C-C0E0EBFC10D0 Q26823332-4BDF6FCA-2675-41C2-938A-A67188A7CF6E Q27015793-324F47C3-1FB2-4CC1-9AED-FC77701657FC Q27316720-0284ABEB-3A30-4A95-9A8F-37ED18C28D45 Q30449325-E6788E30-5CBF-484F-94F3-C319DA497CA4 Q30485962-FE8736A3-F1D4-406C-ACED-D802DAA2B5F5 Q32186771-AA3FAD8A-3F61-46D1-8DB5-1E59255CB59A Q33616045-5C20F12D-2E8D-4554-BCFD-D5D097F6C58F Q33952479-66B618A9-132A-4364-844A-1AC39F02B712 Q34262821-4241E8B8-48AD-4310-AC9E-45718418D3E4 Q34597107-E7B8979B-C026-4E65-815D-D57A7B440436 Q35760051-BD2932C4-1182-4C35-93D1-CC2347B0E8D2 Q36031035-6D55E6A4-554C-41CA-89E1-B1A6561731C0 Q36368553-6F1277C4-B3BF-461B-8EC3-33E5CF5D0DA1 Q36507132-A5C2F4F4-6759-4316-A0DD-4153F1B9160C Q36507155-25926821-A6BD-4AD6-B1A6-1040FF314984 Q36507186-9AA03651-E4A6-4EA0-A890-041DCFAAF096 Q36579629-25D84F91-F951-4DFB-A2DF-0211A1E1A53A Q36750041-8EED0CCE-0086-41A8-BF42-3A2FA891EBED Q36856529-C38ADE8B-2B0B-4E1A-8FEA-2243D5E816DE Q36937164-31B720DA-5BA7-4E3B-908B-B5F0B5A9C5AE Q37175399-CC57781F-598E-4952-B35D-8E2387B04959 Q37220682-C6673A24-5560-418D-B80F-6627496C0948 Q37576096-BB90E913-8E93-449D-8F4D-E3DB39E3A172 Q37707273-58722587-596E-45D3-8712-93C9BC5E4C59 Q37915593-562BAA0F-1EE8-4049-A57F-E4674192830A Q38007019-94735495-A246-4995-A0A7-8BAE3FFA7E67 Q38265030-87EA3AF8-EF5C-4EF6-AE7E-28F4210F0C75 Q39002760-AD5DF87B-AAB8-4ED9-93EF-4EB09F92C888 Q42089141-6DEC7488-1B36-4D8E-ABC8-ED68F0E68EF3 Q42574030-1641C568-4163-46D6-98A7-90C1BEDCCB3B Q43510700-A6A7B18A-AAFD-4C7C-B516-349DEB5E3E7C Q48579102-97624F6B-4DF1-41D7-88D3-C20366BFD2D7 Q51089613-A473D8F3-5B41-4E8B-B62D-B52928BBEBEF Q51995942-BB8D3DC8-74DD-41B2-B2A8-2518AF42EAEA Q57176565-C323BE0E-A6DC-462A-A9A3-2A92C445365B

P2860

Cellular mechanisms of connexin32 mutations associated with CNS manifestations.

http://www.wikidata.org/entity/Q44059866

description

2002 nî lūn-bûn

@nan

2002年の論文

@ja

2002年学术文章

@wuu

2002年学术文章

@zh-cn

2002年学术文章

@zh-hans

2002年学术文章

@zh-my

2002年学术文章

@zh-sg

2002年學術文章

@yue

2002年學術文章

@zh

2002年學術文章

@zh-hant

name

Cellular mechanisms of connexin32 mutations associated with CNS manifestations.

@en

Cellular mechanisms of connexin32 mutations associated with CNS manifestations.

@nl

type

label

Cellular mechanisms of connexin32 mutations associated with CNS manifestations.

@en

Cellular mechanisms of connexin32 mutations associated with CNS manifestations.

@nl

prefLabel

Cellular mechanisms of connexin32 mutations associated with CNS manifestations.

@en

Cellular mechanisms of connexin32 mutations associated with CNS manifestations.

@nl

P1433

Q44059866-4CB99CD6-CBF2-4415-AD11-A231499A6504

P1476

Q44059866-FFC98BEA-7DA2-4C97-BA80-8ED6DBA5BA5B

P2093

Q44059866-2E08A23D-EA8F-45E4-B42B-9B507F2C979A

Q44059866-BCCF3DB8-A05C-4053-8BCC-5F85A86D7DE5

Q44059866-D348218B-E7CF-4FFC-80DC-EED5C8015F4B

P2860

Q44059866-02FB75EE-D9FE-4D5E-81FC-02CBD6E0FFD5

Q44059866-151422C1-CF90-42E2-9469-52C948398EFB

Q44059866-188FEEA8-4303-496F-BD79-FAA53C0D7510

Q44059866-1A3397EA-B0FA-4947-B6F2-0543020AA138

Q44059866-24DF50C2-8616-46E5-90D1-4D2E0B04FDE2

Q44059866-315237C0-92EA-4EC9-87FB-5950452C26AE

Q44059866-3549876C-EA2B-495B-86EB-E0695453ABB4

Q44059866-3D8F8842-A785-4DB7-A5B2-1F0FF315D8EE

Q44059866-3FC1F3DD-493F-4ADA-8498-ADA81F508F29

Q44059866-423E9AA3-0B65-46E7-A39B-24DD82B453C7

P304

Q44059866-51D43D28-C9FB-4B93-AD42-27C2E4AC4A47

P31

Q44059866-B3DDFF36-D5CE-4247-B1FE-48E9AAEDD2DD

P356

Q44059866-137B3EB4-5832-4D5A-8E39-CF30734B7214

P433

Q44059866-D72C5B7D-F3D1-439F-B766-54D902C30C61

P478

Q44059866-19FD9C78-C2D6-40BB-9CFC-B55DA945AFC5

P577

Q44059866-48F70BDF-C5E3-42D3-91B2-7AD447056FB0

P5875

Q44059866-DEA87B31-3787-4EB8-8B1F-9AA568B7AB9B

P698

Q44059866-59D1E8D4-EF51-415B-90CA-C84BB7DAB71C

P356

P1433

Journal of Neuroscience Research

P1476

Cellular mechanisms of connexin32 mutations associated with CNS manifestations.

@en

P2093

Kleopas A Kleopa

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

Sabrina W Yum

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

Steven S Scherer

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

P2860

Glial growth factors are alternatively spliced erbB2 ligands expressed in the nervous system

Connexin mutations in X-linked Charcot-Marie-Tooth disease

Connexin32 and X-linked Charcot-Marie-Tooth disease

Aggresomes: a cellular response to misfolded proteins

Analysis of gap junction assembly using mutated connexins detected in Charcot-Marie-Tooth X-linked disease

Central visual, acoustic, and motor pathway involvement in a Charcot-Marie-Tooth family with an Asn205Ser mutation in the connexin 32 gene.

On the molecular architecture of myelinated fibers.

Differential aggregation of the Trembler and Trembler J mutants of peripheral myelin protein 22

Multisubunit assembly of an integral plasma membrane channel protein, gap junction connexin43, occurs after exit from the ER.

Intracellular transport, assembly, and degradation of wild-type and disease-linked mutant gap junction proteins.

P304

522-534

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

P31

scholarly article

P356

10.1002/JNR.10255

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

P433

5

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

P478

68

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

P577

2002-06-01T00:00:00Z

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

P5875

11266439

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

P698

12111842

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