Functional expression of the Wilson disease protein reveals mislocalization and impaired copper-dependent trafficking of the common H1069Q mutation.
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The Wilson disease protein ATP7B resides in the late endosomes with Rab7 and the Niemann-Pick C1 proteinCopper binding to the N-terminal metal-binding sites or the CPC motif is not essential for copper-induced trafficking of the human Wilson protein (ATP7B)Solution structure of the N-domain of Wilson disease protein: distinct nucleotide-binding environment and effects of disease mutationsMissense mutations in the copper transporter gene ATP7A cause X-linked distal hereditary motor neuropathyMolecular pathogenesis of Wilson and Menkes disease: correlation of mutations with molecular defects and disease phenotypesInteraction of the copper chaperone HAH1 with the Wilson disease protein is essential for copper homeostasisOTOF mutations revealed by genetic analysis of hearing loss families including a potential temperature sensitive auditory neuropathy alleleCopper directs ATP7B to the apical domain of hepatic cells via basolateral endosomesFunctional characterization of missense mutations in ATP7B: Wilson disease mutation or normal variant?The molecular basis of oculocutaneous albinism type 1 (OCA1): sorting failure and degradation of mutant tyrosinases results in a lack of pigmentationSupplying copper to the cuproenzyme peptidylglycine alpha-amidating monooxygenaseDefective localization of the Wilson disease protein (ATP7B) in the mammary gland of the toxic milk mouse and the effects of copper supplementationDefective copper-induced trafficking and localization of the Menkes protein in patients with mild and copper-treated classical Menkes diseaseIdentification of p38 MAPK and JNK as new targets for correction of Wilson disease-causing ATP7B mutantsThe Lys1010-Lys1325 fragment of the Wilson's disease protein binds nucleotides and interacts with the N-terminal domain of this protein in a copper-dependent manner.Modifying factors and phenotypic diversity in Wilson's diseaseDiverse functional properties of Wilson disease ATP7B variants.A conditional mutation affecting localization of the Menkes disease copper ATPase. Suppression by copper supplementation.Hepatocellular transport proteins and their role in liver disease.Hepatic transport systems.Clusterin (apolipoprotein J), a molecular chaperone that facilitates degradation of the copper-ATPases ATP7A and ATP7B.Difference in stability of the N-domain underlies distinct intracellular properties of the E1064A and H1069Q mutants of copper-transporting ATPase ATP7B.Laser ablation inductively coupled plasma mass spectrometry imaging of metals in experimental and clinical Wilson's disease.Clusterin and COMMD1 independently regulate degradation of the mammalian copper ATPases ATP7A and ATP7BPrevalence of ATP7B Gene Mutations in Iranian Patients With Wilson Disease.5'-adenosine monophosphate mediated cooling treatment enhances ΔF508-Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) stability in vivo.Molecular events initiating exit of a copper-transporting ATPase ATP7B from the trans-Golgi networkCopper transportion of WD protein in hepatocytes from Wilson disease patients in vitroCurrently Clinical Views on Genetics of Wilson's DiseaseATP7B expression in human breast epithelial cells is mediated by lactational hormones.Delivery of the Cu-transporting ATPase ATP7B to the plasma membrane in Xenopus oocytes.Intestinal expression of metal transporters in Wilson's disease.Predicting subcellular localization via protein motif co-occurrence.Distinct phenotype of a Wilson disease mutation reveals a novel trafficking determinant in the copper transporter ATP7B.Golgi in copper homeostasis: a view from the membrane trafficking field.Population screening for Wilson's disease.The role of GMXCXXC metal binding sites in the copper-induced redistribution of the Menkes protein.Trafficking defects of a novel autosomal recessive distal renal tubular acidosis mutant (S773P) of the human kidney anion exchanger (kAE1).The distinct roles of the N-terminal copper-binding sites in regulation of catalytic activity of the Wilson's disease protein.The role of the invariant His-1069 in folding and function of the Wilson's disease protein, the human copper-transporting ATPase ATP7B.
P2860
Q24293217-A6661AA6-8854-4CCC-8D29-E2DF3245E2B6Q24300903-E9900E51-1450-42AF-A998-D887E5968FD2Q24310820-6C73C351-8B97-4F3D-B4FC-E2D7DBC5DE30Q24632623-8BBC39B0-451E-4E44-9BF9-5FFE332F2A93Q24647056-27C7C08F-0ABA-44CC-88DB-CFB96E2594ACQ24650387-0F717783-88AC-4455-8537-5CB28C2D669AQ24651350-FBCCB070-0B37-4635-AEFA-5F29DB7C8359Q27346776-A9DDEFD9-6DDA-4BC7-A2A6-72C396C52B0DQ28118944-6334EB33-EFEC-44D6-939A-65CE2B0EEA5AQ28361790-B686D5C4-CDC2-4941-8EA4-D102F0FDE466Q28577544-49F3FB30-8FBC-462B-B6E7-DD348C199B36Q28592976-53ACB5E8-639C-4086-8BEE-7116B06C8DB9Q28609317-D063C1B8-EA96-4230-A592-A039393D8319Q28821905-DB12FE73-C12E-4E61-8613-DC6E9FE5340DQ31504267-725D168E-B373-461C-894F-5FE9ACB864EFQ33851780-D319B239-0FB5-4418-94B8-F530D2E0965CQ34125926-3270CA53-AE9F-4AD2-BE80-B47140124E8CQ34148762-441D924B-1F9E-47F0-BA0B-791349896868Q34512014-8EB6805D-5BC4-4B2E-8E50-3E67F9998380Q34631359-7D397E34-C091-488F-A5BB-7EB44607EAF7Q34695507-773E8EA6-6ADF-4955-8122-9201EF76D50BQ34963655-3A3234E7-7526-4486-95D9-5AB87F0A677DQ35391010-56607430-7197-4882-96CD-8177BBC8F4D9Q35709894-8BBAC693-B492-4FE2-8A81-12E394726525Q35714770-51F5F559-5F43-439F-B904-BD75F65D0AB5Q36024047-FE4E8C17-D75D-4DFB-A06A-DEFBE8C8141BQ36332811-961E2786-8438-4D9F-A396-AFD8123A2E52Q36415720-FE821546-C2F4-4112-9664-ABFFD3161743Q36523123-AA86A697-5626-4468-A54D-367006A9BAA0Q36574299-E9C71C82-6F81-4B4F-A1B9-0D666D39F07FQ36662522-6DAB7D22-B8DD-40E7-A014-E8EDD8887BACQ37302290-EDA9B52D-7597-4BF5-83A2-5CED5C5A3525Q37593051-13CA8311-F16E-40B2-93D1-469BB31AF192Q37702034-338CEA53-FB87-437E-A7CE-7FEBDCCBDE05Q38121020-F91F3E39-3C53-4E03-A305-829D82942BF4Q38204501-7CE7462D-C848-4282-B464-E982B908FB6FQ38326201-E7C4B3E4-B542-4A56-B93B-E8F262AAB0DAQ38338952-95634C17-0446-4C1B-AEC4-8F0B81E90398Q38353817-DB6F3BBA-E131-4BF8-890D-9598E43B3210Q38358304-BCB96C8D-77E7-46E0-8C3B-47415203D0C6
P2860
Functional expression of the Wilson disease protein reveals mislocalization and impaired copper-dependent trafficking of the common H1069Q mutation.
description
1998 nî lūn-bûn
@nan
1998 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Functional expression of the W ...... of the common H1069Q mutation.
@ast
Functional expression of the W ...... of the common H1069Q mutation.
@en
Functional expression of the W ...... of the common H1069Q mutation.
@nl
type
label
Functional expression of the W ...... of the common H1069Q mutation.
@ast
Functional expression of the W ...... of the common H1069Q mutation.
@en
Functional expression of the W ...... of the common H1069Q mutation.
@nl
prefLabel
Functional expression of the W ...... of the common H1069Q mutation.
@ast
Functional expression of the W ...... of the common H1069Q mutation.
@en
Functional expression of the W ...... of the common H1069Q mutation.
@nl
P2093
P2860
P356
P1476
Functional expression of the W ...... of the common H1069Q mutation.
@en
P2093
P2860
P304
10854-10859
P356
10.1073/PNAS.95.18.10854
P407
P577
1998-09-01T00:00:00Z