Wilson disease protein ATP7B utilizes lysosomal exocytosis to maintain copper homeostasis. - Wikidata - wikimedia - TriplyDB

Wilson disease protein ATP7B utilizes lysosomal exocytosis to maintain copper homeostasis.

Wilson disease protein ATP7B utilizes lysosomal exocytosis to maintain copper homeostasis.

http://www.wikidata.org/entity/Q41156563

about

Canine Models for Copper Homeostasis Disorders Synthetic fluorescent probes for studying copper in biological systems Copper directs ATP7B to the apical domain of hepatic cells via basolateral endosomes Biphasic regulation of lysosomal exocytosis by oxidative stress Identification of p38 MAPK and JNK as new targets for correction of Wilson disease-causing ATP7B mutants Polarized sorting of the copper transporter ATP7B in neurons mediated by recognition of a dileucine signal by AP-1.TFE3 regulates whole-body energy metabolism in cooperation with TFEB.Copper is an endogenous modulator of neural circuit spontaneous activity.Brief exposure to copper activates lysosomal exocytosis Wilson's disease: a comprehensive review of the molecular mechanisms.Recognition- and reactivity-based fluorescent probes for studying transition metal signaling in living systems.Structural and functional hepatocyte polarity and liver disease.Transition metals activate TFEB in overexpressing cells Gene expression patterns in the progression of canine copper-associated chronic hepatitis.The Menkes and Wilson disease genes counteract in copper toxicosis in Labrador retrievers: a new canine model for copper-metabolism disorders.Review: Insights into molecular mechanisms of disease in neurodegeneration with brain iron accumulation: unifying theories.Targeting drug transport mechanisms for improving platinum-based cancer chemotherapy.Microbial peptide de-coppers mitochondria: implications for Wilson disease.Rational Design of a Water-Soluble, Lipid-Compatible Fluorescent Probe for Cu(I) with Sub-Part-Per-Trillion Sensitivity.Functional analysis and drug response to zinc and D-penicillamine in stable ATP7B mutant hepatic cell lines.ROS and intracellular ion channels.The emerging role of lysosomes in copper homeostasis.The role of insufficient copper in lipid synthesis and fatty-liver disease.Analytical Methods for Imaging Metals in Biology: From Transition Metal Metabolism to Transition Metal Signaling.Prelysosomal Compartments in the Unconventional Secretion of Amyloidogenic Seeds.Orchestration of dynamic copper navigation - new and missing pieces.The P2X4 purinergic receptor impacts liver regeneration after partial hepatectomy in mice through the regulation of biliary homeostasis.ATP7B expression confers multidrug resistance through drug sequestration Organ-specific regulation of ATP7A abundance is coordinated with systemic copper homeostasis.The six metal binding domains in human copper transporter, ATP7B: molecular biophysics and disease-causing mutations.mTORC1 hyperactivation arrests bone growth in lysosomal storage disorders by suppressing autophagy.The mitochondrial metallochaperone SCO1 maintains CTR1 at the plasma membrane to preserve copper homeostasis in the murine heart.Hypothyroidism induced by loss of the manganese efflux transporter SLC30A10 may be explained by reduced thyroxine production.Atp7a and Atp7b regulate copper homeostasis in developing male germ cells in mice.Full-length cellular β-secretase has a trimeric subunit stoichiometry, and its sulfur-rich transmembrane interaction site modulates cytosolic copper compartmentalization.Gene duplication and neo-functionalization in the evolutionary and functional divergence of the metazoan copper transporters Ctr1 and Ctr2.A systems biology approach reveals new endoplasmic reticulum-associated targets for the correction of the ATP7B mutant causing Wilson disease.Production of Wilson Disease Model Rabbits with Homology-Directed Precision Point Mutations in the ATP7B Gene Using the CRISPR/Cas9 System.In Vivo Modeling of the Pathogenic Effect of Copper Transporter Mutations That Cause Menkes and Wilson Diseases, Motor Neuropathy, and Susceptibility to Alzheimer's Disease.Cystinosin-LKG rescues cystine accumulation and decreases apoptosis rate in cystinotic proximal tubular epithelial cells.

P2860

Q26767292-275DB91E-3E61-40AE-8625-27AB43E8C590 Q27008520-80C02310-97CA-40D9-ACDD-EA7461881894 Q27346776-C62E78A4-6F89-4EF4-AD8E-F3A61568B591 Q28392384-9379DF6B-499C-4F73-B29B-FAB8C0C9271B Q28821905-4D5962E9-B0A4-4084-8502-08CA8C15B9D9 Q30615545-8B160E79-A93B-4578-B320-AAFCA87376F6 Q33625901-FFF926D4-5DC0-454F-926A-9CE3F1C13C86 Q34581319-D555DC22-A87D-4924-B063-43E534A114CE Q35187014-FD1B52B0-347C-4E28-90E4-229979BAF8C8 Q35381754-CB691801-20FC-4338-B781-E15498882089 Q35973071-B25615F6-26D6-43B1-9ABF-759FE3868879 Q36090717-63801CF1-20F5-46A1-B38F-6BF654EBFF2E Q36184709-E3A87E0A-1286-4960-B22F-3BDD1FFECF87 Q36359677-6F03D3F6-39ED-416B-BB91-E5CBDEA78502 Q36506584-18C173DA-0855-471F-8E9E-A79CA69C21E8 Q36800670-D6D92A0C-64C0-4FE0-A20D-FBEDE637DC89 Q36841450-9E2AA990-6862-4A8B-A6CF-226EB4020D7D Q37042204-D7C257C7-2A75-44B7-A953-0C6534B108E9 Q37546112-C2181FC4-D09B-4856-A86C-A3E19FF9DE03 Q38774848-9D765852-B96E-482C-BF37-DDD514B73903 Q38781697-E3DC8783-0396-45CD-B867-1CFA9D2A65D6 Q38875182-00F15DB6-9963-47D6-AB03-66EED6F4FDF2 Q38921695-65D694E3-7B56-4A5B-9EC8-1D17422BA0BF Q39038980-E4CBAD55-DC2C-4B04-814F-C645C0BFDCD4 Q39104462-D8C89792-441A-42BC-92A3-E2E7522C07A2 Q39420445-AC908ECD-FC82-4785-A459-51EA57659391 Q39683781-3524118B-487A-44FD-9697-430C96BF6197 Q40997062-0B8CAB36-D1D6-4307-B6F5-61C37548EFE3 Q41697129-AF5FDD89-348D-429B-AF3A-697DC6ACF7DF Q46108156-3F1135B1-EC27-44A3-BA57-B661E1349706 Q47149655-C8955F27-4ED4-4D20-8F39-D75F14DC5679 Q47706161-14DC6A15-C40E-4E2A-8E06-074435CBB501 Q47732317-28C4E47D-90FD-40E6-8AD0-E69380282089 Q47935607-2B4E2CFA-4DFF-41FD-8638-12BD16947D6B Q48059222-0B9932CE-2645-4883-B4C0-77325B2CCAC6 Q48142231-2A686206-2AF3-4281-9716-252CE0EB19B0 Q48673647-51D0486F-8E64-429E-96E7-D15574591B03 Q49417992-46D3D6C9-DF83-4179-90AE-1E0FC2364228 Q50934293-FF64218D-F71E-42E4-A349-116BC5E257D7 Q51475656-C53A6799-947A-440A-BB42-82B20DD714B2

P2860

Wilson disease protein ATP7B utilizes lysosomal exocytosis to maintain copper homeostasis.

http://www.wikidata.org/entity/Q41156563

description

2014 nî lūn-bûn

@nan

2014年の論文

@ja

2014年論文

@yue

2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

@wuu

2014年论文

@zh

2014年论文

@zh-cn

name

Wilson disease protein ATP7B u ...... o maintain copper homeostasis.

@en

type

label

Wilson disease protein ATP7B u ...... o maintain copper homeostasis.

@en

prefLabel

Wilson disease protein ATP7B u ...... o maintain copper homeostasis.

@en

P1433

Q41156563-D13B8468-E852-429D-BFB7-F0892BDFE99A

P1476

Q41156563-C7B9D46B-B625-4C87-9FCE-DC7082A0E200

P2093

Q41156563-05838544-A157-47FA-B49D-3D76F297ED09

Q41156563-283DC20F-A367-4233-B9AF-C8D5B0C3E74A

Q41156563-3816EBD7-508E-468E-BE08-F6EE50497BD8

Q41156563-3E857B5B-41BF-4202-A721-498E288F918E

Q41156563-3F6FEEA3-C910-4B3E-AFEE-77BC4F923EA8

Q41156563-55190FA8-1FC2-4AE1-A32A-7D6284D875CD

Q41156563-57D7673C-D7BB-46AE-8D70-AC381922231B

Q41156563-68D26EA7-1DFD-4F7C-9885-32810A79F603

Q41156563-CE169217-DE4F-4BB4-91B4-36030F0425AD

Q41156563-D81558C7-032B-4920-A4C7-9C97AEEC8229

P2860

Q41156563-0E086DF0-E006-492F-95F6-E69FFCD410A9

Q41156563-0EF5FC3D-8362-4AE6-A92C-B63C73CEF595

Q41156563-12A54F60-CCEF-4DC3-A5FD-4E53F02CD926

Q41156563-1CD795B5-E0E4-4386-B0EB-12B36BFE0013

Q41156563-20689B3C-55A4-4BAB-9F33-45C321ADA09A

Q41156563-2A6123CC-4C2D-4A87-8CCB-43DFEAFADFD7

Q41156563-3CF6B817-EA0B-4F1C-BB2C-D1696D4DB9BD

Q41156563-3D20F1D5-11D0-4DFB-B485-3FF1FE126A94

Q41156563-3E61FC99-9E5A-468D-942E-DBCA44F28923

Q41156563-50193B5F-2362-4CDB-AED8-1A7AC9A270E4

P304

Q41156563-03BEF115-08EE-4269-BEC3-97CC49D53790

P31

Q41156563-794279C0-ACFC-4A83-A0A2-43624B9A3462

P356

Q41156563-0184A82A-407E-415B-A552-B852FF7CF864

P407

Q41156563-096E7BE1-9089-430F-B38C-40155A505526

P433

Q41156563-3D71758E-DAD0-4AF9-B4D2-3E355CABED67

P478

Q41156563-158F106D-DE74-4218-B1DD-B667028B020F

P50

Q41156563-0F553819-0ACF-4317-BE1B-54D1141935D7

Q41156563-211A632F-2B59-4D76-BADE-28955B96F21E

Q41156563-4B8597A9-CF7B-41BE-875B-6FAAC2300FC7

Q41156563-673DDB64-0114-41D6-BEB6-311655EFCA1E

Q41156563-7F1CCDC0-50A5-4EAA-A2D5-8847CCE87181

Q41156563-D2BF51F7-3DD2-4894-9FF4-0A1B5B02ECF0

Q41156563-E2FA2F2C-669B-4E58-8D89-69573CFEA438

Q41156563-FEBA4C57-5D02-4023-9A93-FBFD8CE52B52

P577

Q41156563-7CB22286-D3FA-4F25-BEC4-EE5E0E3B614E

P5875

Q41156563-68D986A2-6175-43A0-9F0E-07CFE6E4B413

P698

Q41156563-E2DCA0D4-E706-4495-B874-E174FADB7A2A

P921

Q41156563-91074BA8-8DEB-479B-853F-43A8251F8118

P932

Q41156563-AE627ED7-FCBC-455B-A8B3-233283BDBE9E

P356

J.DEVCEL.2014.04.033

P1433

Developmental Cell

P1476

Wilson disease protein ATP7B utilizes lysosomal exocytosis to maintain copper homeostasis

@en

P2093

Antonietta Tarallo

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

Christopher J Chang

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

Elena V Polishchuk

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

Francesca Pane

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

Giancarlo Chesi

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

Giancarlo Parenti

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

Jefferson Chan

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

Mafalda Concilli

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

Nunzia Pastore

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

Roman S Polishchuk

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

P2860

The Wilson disease protein ATP7B resides in the late endosomes with Rab7 and the Niemann-Pick C1 protein

ATP7B mediates vesicular sequestration of copper: insight into biliary copper excretion

Copper-dependent interaction of dynactin subunit p62 with the N terminus of ATP7B but not ATP7A

Human copper transporter 2 is localized in late endosomes and lysosomes and facilitates cellular copper uptake

Charting the travels of copper in eukaryotes from yeast to mammals

Trafficking of the copper-ATPases, ATP7A and ATP7B: role in copper homeostasis

NH2-terminal signals in ATP7B Cu-ATPase mediate its Cu-dependent anterograde traffic in polarized hepatic cells

Consequences of copper accumulation in the livers of the Atp7b-/- (Wilson disease gene) knockout mice

Mechanism of constitutive export from the golgi: bulk flow via the formation, protrusion, and en bloc cleavage of large trans-golgi network tubular domains.

Activation of human acid sphingomyelinase through modification or deletion of C-terminal cysteine.

P304

686-700

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

P31

scholarly article

P356

10.1016/J.DEVCEL.2014.04.033

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

P407

P433

6

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

P478

29

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

P50

Simona Paladino

Pasquale Piccolo

Nicola Brunetti-Pierri

Andrea Ballabio

Carmine Settembre

Angela Amoresano

Daniela Baldantoni

P577

2014-06-05T00:00:00Z

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

P5875

262932738

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

P698

24909901

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

P921

P932

4070386

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