Tissue nonspecific alkaline phosphatase is activated via a two-step mechanism by zinc transport complexes in the early secretory pathway - Wikidata - awgldk - TriplyDB

Tissue nonspecific alkaline phosphatase is activated via a two-step mechanism by zinc transport complexes in the early secretory pathway

Tissue nonspecific alkaline phosphatase is activated via a two-step mechanism by zinc transport complexes in the early secretory pathway

http://www.wikidata.org/entity/Q38569070

about

Biochemical characterization of human ZIP13 protein: a homo-dimerized zinc transporter involved in the spondylocheiro dysplastic Ehlers-Danlos syndrome The Functions of Metallothionein and ZIP and ZnT Transporters: An Overview and Perspective Sortilin mediates vascular calcification via its recruitment into extracellular vesicles Essential role of the zinc transporter ZIP9/SLC39A9 in regulating the activations of Akt and Erk in B-cell receptor signaling pathway in DT40 cells Compound heterozygous mutations in SLC30A2/ZnT2 results in low milk zinc concentrations: a novel mechanism for zinc deficiency in a breast-fed infant Cellular function and molecular structure of ecto-nucleotidases.Physiological roles of zinc transporters: molecular and genetic importance in zinc homeostasis.Cooperative functions of ZnT1, metallothionein and ZnT4 in the cytoplasm are required for full activation of TNAP in the early secretory pathway ZnT4 provides zinc to zinc-dependent proteins in the trans-Golgi network critical for cell function and Zn export in mammary epithelial cells.In situ dimerization of multiple wild type and mutant zinc transporters in live cells using bimolecular fluorescence complementation.Molecular and genetic features of zinc transporters in physiology and pathogenesis.Current understanding of ZIP and ZnT zinc transporters in human health and diseases.The Physiological, Biochemical, and Molecular Roles of Zinc Transporters in Zinc Homeostasis and Metabolism.Zinc transporter ZIP13 suppresses beige adipocyte biogenesis and energy expenditure by regulating C/EBP-β expression Dissecting the Process of Activation of Cancer-promoting Zinc-requiring Ectoenzymes by Zinc Metalation Mediated by ZNT Transporters.The PP-motif in luminal loop 2 of ZnT transporters plays a pivotal role in TNAP activation Direct Comparison of Manganese Detoxification/Efflux Proteins and Molecular Characterization of ZnT10 Protein as a Manganese Transporter.Human IAPP-induced pancreatic β cell toxicity and its regulation by autophagy.Drosophila melanogaster Models of Metal-Related Human Diseases and Metal Toxicity.Structural Elements in the Transmembrane and Cytoplasmic Domains of the Metal Transporter SLC30A10 Are Required for Its Manganese Efflux Activity.Understanding the Contribution of Zinc Transporters in the Function of the Early Secretory Pathway.Zinc Transporter Proteins.Properties of Zip4 accumulation during zinc deficiency and its usefulness to evaluate zinc status: a study of the effects of zinc deficiency during lactation.Zinc deficiency causes delayed ATP clearance and adenosine generation in rats and cell culture models Evaluation of the roles of the cytosolic N-terminus and His-rich loop of ZNT proteins using ZNT2 and ZNT3 chimeric mutants

P2860

Q24337896-75FC950C-C690-45C2-B9F8-C3627A254E84 Q26766916-1B4B0FC1-6455-49CA-B49D-35892DBEE92F Q28273951-C48C880F-868F-4C9D-8C53-E321DA112A6F Q28487787-2F8394FE-5F04-4813-A7FE-169130AEF015 Q28533518-ADC6104B-C3F9-492E-B5B0-AA6ACCA0EBA6 Q34031794-40C07C5E-1B12-4712-9C66-DC339008018C Q34550179-581BFC41-B69B-40C8-9BD2-8391361DC461 Q35035248-8C8C0805-0B4D-4953-BFAE-88464A4386B0 Q36175735-CE0685F0-0248-4D3E-B236-8DD19F937E61 Q37635752-865C0979-0E1D-4DB1-A530-2F5173F354FC Q37874950-BED7A20A-4E84-4C40-B351-D1043CAC781C Q38202894-42E57D1C-AC65-4CAA-935E-0AAF2C71AEB4 Q38530500-29900120-E926-43C5-92F6-0E639925763F Q38602160-D2DA96C7-0C41-4141-84D1-C734E702C2A7 Q38724045-B1BAF6FF-0218-43B5-9BB3-FBF167BFB344 Q38764363-E23691AA-0817-413A-9A6D-B610B63D3B9D Q38768341-FBC5E281-73C3-46AA-B751-74E0E90E2D2C Q38974302-1104E1E4-A821-4C6F-853A-702F38D44DA5 Q39419474-2D45C54B-71A8-4FAD-B688-10BD28174E90 Q42395510-449CFD63-09B0-483C-B8B4-19161ECCADA0 Q47163079-40FA4E5A-06FA-4B84-9DCD-4842D63D6DAD Q47291542-7598573F-5BF5-4DC9-8512-09F5AF79F53D Q53237240-D27DE5C6-B941-470A-B08F-57044C7D3B3B Q57132589-E9F34630-958F-4F79-AE15-F4A94102FCAB Q58712633-35CB17D1-6BF6-4E7A-A44B-B3F187772E65

P2860

Tissue nonspecific alkaline phosphatase is activated via a two-step mechanism by zinc transport complexes in the early secretory pathway

http://www.wikidata.org/entity/Q38569070

description

2011 nî lūn-bûn

@nan

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

2011年论文

@zh

2011年论文

@zh-cn

name

Tissue nonspecific alkaline ph ...... in the early secretory pathway

@en

type

label

Tissue nonspecific alkaline ph ...... in the early secretory pathway

@en

prefLabel

Tissue nonspecific alkaline ph ...... in the early secretory pathway

@en

P1433

Q38569070-4E734D28-89B6-4BC4-A1E3-6ECA2487171D

P1476

Q38569070-A34BE300-6871-4FF0-A2E0-CD8E92BD14F0

P2093

Q38569070-09357E4B-15BA-4AE4-BCFF-DC26451DC06C

Q38569070-1A873251-E493-444F-85DE-298F154345EB

Q38569070-34343DF0-69B8-430E-9067-DA192C81C31A

Q38569070-365FFCEB-93B9-44C1-BD55-7F68C585F71E

Q38569070-7AF497EE-7FED-4576-A9C4-8D2C0D3EA2D5

Q38569070-89904AF9-E518-4A78-9F02-FF98666B6535

Q38569070-8DE781D1-347E-4006-930F-A22CCE898A22

Q38569070-D67A3E94-287E-4623-AAA2-D4A5824708D8

Q38569070-EEB370B9-D50F-4497-B436-82D4F64B6524

P2860

Q38569070-076A9AB0-2051-493C-BF88-24027B1AAD2B

Q38569070-0B9CCFD4-C4C6-426F-946C-D478D7A84ED6

Q38569070-221497CA-F58D-4629-896B-6DA69FB036FA

Q38569070-24140EF1-386F-4129-AF79-B267D9908F57

Q38569070-272F4BA7-80B5-4C29-B029-14F1AE74DF70

Q38569070-29379342-A0A3-4909-85B5-F612DE4C5637

Q38569070-2C2CA1A8-6E3E-464D-9CE0-FD83C5047949

Q38569070-3ECDF575-D47D-48B2-BB8A-80903265902C

Q38569070-401F0BE2-3738-4B26-AB7F-667B471494E9

Q38569070-4712D757-D044-4645-B229-C40DD2E70B07

P304

Q38569070-84B730B1-6D1E-4792-89DB-DA1E0B31D423

P31

Q38569070-E9CB6447-100C-43D0-99C5-4C373C4B6F70

P356

Q38569070-55E59887-3830-4793-9999-2A54073812A1

P407

Q38569070-FDD80C81-2B4F-4391-8F97-8A2F5E49AD3B

P433

Q38569070-D82ED6BD-420C-4820-9089-A9BA6D28D27C

P478

Q38569070-27E458CF-6822-44F0-87E9-B43D1B560F0E

P50

Q38569070-605678B4-3ACB-4484-81B3-6011455B25A6

Q38569070-A1DD2E25-B9DF-436F-91D6-1114263A3620

Q38569070-B19D913E-E395-4A50-8A18-F92ED1D1CAA4

P577

Q38569070-C45596E7-A89E-4FB9-B1E6-A681B7BAAE59

P698

Q38569070-71DE7C2F-8A3B-4860-A365-C0D50D42C87A

P932

Q38569070-DD0F203E-5CD2-4429-96D1-B3ED506540F8

P356

JBC.M111.227173

P1433

Journal of Biological Chemistry

P1476

Tissue nonspecific alkaline ph ...... in the early secretory pathway

@en

P2093

Ayako Fukunaka

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

Fumie Teranishi

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

Israel Sekler

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

Kimimitsu Oda

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

Makoto Hiromura

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

Masaya Nagao

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

Seiji Masuda

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

Shuichi Enomoto

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

Yayoi Kurokawa

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

P2860

Crystal structure of the human angiotensin-converting enzyme-lisinopril complex

In vivo expression and functional characterization of the zinc transporter ZnT8 in glucose-induced insulin secretion

Regulation of cellular zinc balance as a potential mechanism of EVER-mediated protection against pathogenesis by cutaneous oncogenic human papillomaviruses

The zinc transporter SLC39A13/ZIP13 is required for connective tissue development; its involvement in BMP/TGF-beta signaling pathways

Constitutive expression of hZnT4 zinc transporter in human breast epithelial cells

Novel proteolytic processing of the ectodomain of the zinc transporter ZIP4 (SLC39A4) during zinc deficiency is inhibited by acrodermatitis enteropathica mutations

One step at a time: endoplasmic reticulum-associated degradation

Zinc and the Msc2 zinc transporter protein are required for endoplasmic reticulum function.

Heteromeric protein complexes mediate zinc transport into the secretory pathway of eukaryotic cells.

Efflux and compartmentalization of zinc by members of the SLC30 family of solute carriers

P304

16363-16373

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

P31

scholarly article

P356

10.1074/JBC.M111.227173

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

P407

P433

18

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

P478

286

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

P50

P577

2011-03-14T00:00:00Z

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

P698

21402707

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

P932

3091242

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