Selenoprotein K binds multiprotein complexes and is involved in the regulation of endoplasmic reticulum homeostasis. - Wikidata - wikimedia - TriplyDB

Selenoprotein K binds multiprotein complexes and is involved in the regulation of endoplasmic reticulum homeostasis.

Selenoprotein K binds multiprotein complexes and is involved in the regulation of endoplasmic reticulum homeostasis.

http://www.wikidata.org/entity/Q35604604

about

Selenoprotein K form an intermolecular diselenide bond with unusually high redox potential Selenium cytotoxicity in cancer Selenoprotein T Exerts an Essential Oxidoreductase Activity That Protects Dopaminergic Neurons in Mouse Models of Parkinson's Disease Characterization of mammalian selenoprotein o: a redox-active mitochondrial protein Pro178 and Pro183 of selenoprotein S are essential residues for interaction with p97(VCP) during endoplasmic reticulum-associated degradation.Selenoproteins: molecular pathways and physiological roles.Transcriptional activation of antioxidants may compensate for selenoprotein deficiencies in Amblyomma maculatum (Acari: Ixodidae) injected with selK- or selM-dsRNA.Polymorphisms in thioredoxin reductase and selenoprotein K genes and selenium status modulate risk of prostate cancer.Alternative transcripts and 3'UTR elements govern the incorporation of selenocysteine into selenoprotein S Mechanism-based proteomic screening identifies targets of thioredoxin-like proteins Selenoprotein S Is Highly Expressed in the Blood Vessels and Prevents Vascular Smooth Muscle Cells From Apoptosis.Expression of Selenoprotein Genes Is Affected by Obesity of Pigs Fed a High-Fat Diet.Selenoprotein K and protein palmitoylation.Understanding selenoprotein function and regulation through the use of rodent models.Selenotranscriptomic Analyses Identify Signature Selenoproteins in Brain Regions in a Mouse Model of Parkinson's Disease.Expression and purification of the membrane enzyme selenoprotein K Selenoprotein S-dependent Selenoprotein K Binding to p97(VCP) Protein Is Essential for Endoplasmic Reticulum-associated Degradation Leishmania donovani Encodes a Functional Selenocysteinyl-tRNA Synthase.The intrinsically disordered membrane protein selenoprotein S is a reductase in vitro.Contribution of selenocysteine to the peroxidase activity of selenoprotein S.Progress toward Understanding Protein S-acylation: Prospective in Plants Selenoprotein N in skeletal muscle: from diseases to function.Selenium biochemistry and its role for human health.Selenium and selenoprotein function in brain disorders.Biochemical characterization of the selenoproteome in Gallus gallus via bioinformatics analysis: structure-function relationships and interactions of binding molecules.Biological functions of selenium and its potential influence on Parkinson's disease.Endoplasmic reticulum-resident selenoproteins as regulators of calcium signaling and homeostasis.Deducing the functional characteristics of the human selenoprotein SELK from the structural properties of its intrinsically disordered C-terminal domain.Selenoprotein S is involved in maintenance and transport of multiprotein complexes.The human selenoprotein VCP-interacting membrane protein (VIMP) is non-globular and harbors a reductase function in an intrinsically disordered region.Development of a gene expression database and related analysis programs for evaluation of anticancer compounds.Quantitative Chemical Proteomic Profiling of the in Vivo Targets of Reactive Drug Metabolites.Selenoprotein K Mediates the Proliferation, Migration, and Invasion of Human Choriocarcinoma Cells by Negatively Regulating Human Chorionic Gonadotropin Expression via ERK, p38 MAPK, and Akt Signaling Pathway.Selenoprotein T is a novel OST subunit that regulates UPR signaling and hormone secretion.Modulation of selenium tissue distribution and selenoprotein expression in Atlantic salmon (Salmo salar L.) fed diets with graded levels of plant ingredients.Selenoproteins and cardiovascular stress.

P2860

Q24301898-45926795-AE07-4DB9-8F80-FD19A660D183 Q26865042-16D24C46-0B57-43DB-8A00-80FF9D16CD62 Q28854286-3F3277AC-D1C8-4D67-9C04-DDB16F837744 Q28854578-D605526D-8A53-4BB1-9DAE-76909C9EF4B7 Q33619328-44E6D4B5-1589-44DC-9546-5CF09C8D326E Q33913069-D71FB13F-B33D-4567-9EB3-0B31D7AEFD3D Q33934875-48D09081-ED4B-44FD-AA18-3E0679558411 Q34469841-D7393662-DD02-4174-954D-B40EFECD24E4 Q34685587-BE1453B5-B8A3-4C35-9CF6-401D635E0B38 Q35126677-E2FAD178-0624-485E-AD95-FDD3B4BC120E Q35658636-82F4A237-CBAF-4342-878E-2D570B39796B Q35775167-8D72D481-A21F-491C-9789-9D2D0D60E95B Q36108599-70DAF1E4-F7C3-4B0C-BE46-E6D8D052AF96 Q36129752-08BA8E71-F1C3-487B-BBBF-A5A22F30AE30 Q36140465-767C16BF-1A24-4090-8B8B-8FD203FAD333 Q36354370-0FD0FE3A-C883-4252-8B43-A74E1CF93319 Q36444291-84942EE3-D21F-427E-B26B-F83849043D07 Q36466149-C1E820A5-5CF4-473F-BD3F-8D6474E85D5C Q36909042-385578A7-685D-4078-B5DA-DF7479150B2F Q37259902-25FC515E-33D0-481D-8486-C1825823C7D7 Q37719052-47D6B33B-E59B-4EFA-BCD1-300628AF733A Q38004951-B9138125-E847-4CF4-9871-F57F74FA2468 Q38159453-638239F7-02E0-4539-9413-6E349032A983 Q38199451-3F6F6515-1D58-4B4D-BE95-AA69BE93B6E2 Q38770040-722B5CC1-5B28-485A-A2C9-002F29C5A884 Q38935901-8B60B11D-2930-462F-A2B7-3887DE864EFD Q39307703-2FBE018B-B34A-421E-B1E7-0052F61FF236 Q40139998-A4EBB1C5-24C2-41DA-AC79-A9C1A7B232AF Q41576322-CE94EE9B-8952-4720-B030-DB3EE19101FB Q42252683-612026AC-7365-4796-8F63-90E48C7BEEB7 Q42677922-0E97316A-4CF4-4EF4-8B96-680BBC379DB2 Q46847239-E217B6E7-D709-4833-B005-C3C5B923204A Q47688633-54A32C04-4E36-4AF4-B113-7C6D82E04A1E Q47776155-04F87801-AB47-41FC-8DB5-724AECD36DE2 Q48883387-87E41904-8E58-4760-BCA4-743C5BB81E32 Q50192080-9C74D54F-3A1F-4D5E-9CF2-7BE947AB2BCC

P2860

Selenoprotein K binds multiprotein complexes and is involved in the regulation of endoplasmic reticulum homeostasis.

http://www.wikidata.org/entity/Q35604604

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

Selenoprotein K binds multipro ...... plasmic reticulum homeostasis.

@ast

Selenoprotein K binds multipro ...... plasmic reticulum homeostasis.

@en

type

label

Selenoprotein K binds multipro ...... plasmic reticulum homeostasis.

@ast

Selenoprotein K binds multipro ...... plasmic reticulum homeostasis.

@en

prefLabel

Selenoprotein K binds multipro ...... plasmic reticulum homeostasis.

@ast

Selenoprotein K binds multipro ...... plasmic reticulum homeostasis.

@en

P1433

Q35604604-A5940ACE-8979-448A-BB7F-40460E0BE5A5

P1476

Q35604604-2EB716BA-BEE4-4ABF-AE83-57EDEA9BF96C

P2093

Q35604604-0A99F82C-8A0A-4F5C-8117-500B1D144673

Q35604604-862D6291-BB45-459C-AE59-64718BDFBC49

Q35604604-93769173-F2F4-4A61-80B1-2D5FDFD8B986

Q35604604-99C177F5-DEDC-4A37-9360-D73C1E8E382C

Q35604604-B25092E4-D688-4ACA-B9AA-D02EC17CE3E9

P2860

Q35604604-133659D5-1466-41E6-96D3-E642E46C0023

Q35604604-19FB0B17-B09F-4743-8F57-C715E7B6C28A

Q35604604-1D586D66-8048-41B7-A88D-E4681177F1E4

Q35604604-200A5D68-D5BE-4E9A-A676-DD6CBC624A9B

Q35604604-2CFA4615-268E-4660-9049-FD785265B05D

Q35604604-2FEFAC7C-8DC0-4726-B171-02CF56633BB2

Q35604604-3D3E4113-34D3-4F43-8EF7-E483361BD2F2

Q35604604-3DD59332-706D-4656-BF9A-08948B5A4890

Q35604604-46109DC2-A35E-4DBB-B06C-956CB366FF90

Q35604604-4964F909-A310-4EF8-9770-2EB40D5D8A18

P304

Q35604604-BC388AFC-C31A-4A27-AE37-2A9CA0DBB663

P31

Q35604604-3E0841B0-E5AF-4791-983B-5F3DCED2370D

P356

Q35604604-9ECCB453-0F89-40FB-89B5-35A967EC0DB5

P407

Q35604604-54F9F624-F98B-4D67-B8C5-D1F0D972F81A

P433

Q35604604-2A357366-A6F1-45D1-9153-FCD6479A6DAA

P478

Q35604604-7358520A-9134-4351-BF70-70D16DABC132

P50

Q35604604-E052B57D-7C52-4AC5-A2C3-54F319F681E9

P577

Q35604604-14202DB6-5C14-4150-8C56-9B9D2717F244

P5875

Q35604604-B50D4541-A531-4C97-99AA-D0D925BBCA8F

P698

Q35604604-948AEE02-0ECC-49EE-B0E5-BCC4722149DC

P921

Q35604604-8F2B5883-2479-4606-A949-FD7DBAC05312

P932

Q35604604-E456D79B-B2F5-4452-A7A1-867CD2D12287

P356

JBC.M111.310920

P1433

Journal of Biological Chemistry

P1476

Selenoprotein K binds multipro ...... plasmic reticulum homeostasis.

@en

P2093

Dolph L Hatfield

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

Robert A Everley

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

Vadim N Gladyshev

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

Valentina A Shchedrina

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

Yan Zhang

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

P2860

Evolutionary dynamics of eukaryotic selenoproteomes: large selenoproteomes may associate with aquatic life and small with terrestrial life

Niche of harmful alga Aureococcus anophagefferens revealed through ecogenomics

SelK is a novel ER stress-regulated protein and protects HepG2 cells from ER stress agent-induced apoptosis

A novel protein, Romo1, induces ROS production in the mitochondria

A membrane protein required for dislocation of misfolded proteins from the ER

A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol

Proteomic analysis of mammalian oligosaccharyltransferase reveals multiple subcomplexes that contain Sec61, TRAP, and two potential new subunits

Identification and characterization of selenoprotein K: an antioxidant in cardiomyocytes

Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradation

Defining the human deubiquitinating enzyme interaction landscape

P304

42937-42948

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

P31

scholarly article

P356

10.1074/JBC.M111.310920

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

P407

P433

50

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

P478

286

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

P50

P577

2011-10-20T00:00:00Z

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

P5875

51733089

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

P698

22016385

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

P921

endoplasmic reticulum

P932

3234841

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