A novel cysteine-rich domain of Sep15 mediates the interaction with UDP-glucose:glycoprotein glucosyltransferase.
about
Deficiency in the 15 kDa selenoprotein inhibits human colon cancer cell growthThe human selenoproteome: recent insights into functions and regulationNMR structures of the selenoproteins Sep15 and SelM reveal redox activity of a new thioredoxin-like family.Structure-function relations, physiological roles, and evolution of mammalian ER-resident selenoproteins.Protein-protein interactions and membrane localization of the human organic solute transporterA large prospective study of SEP15 genetic variation, interaction with plasma selenium levels, and prostate cancer risk and survival.UDP-GlC:glycoprotein glucosyltransferase-glucosidase II, the ying-yang of the ER quality controlSelenoproteins: 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.A role for UDP-glucose glycoprotein glucosyltransferase in expression and quality control of MHC class I moleculesUnderstanding selenoprotein function and regulation through the use of rodent models.Protein folding includes oligomerization - examples from the endoplasmic reticulum and cytosol.Molecular mechanisms by which selenoproteins affect cancer risk and progression.Sep15, a thioredoxin-like selenoprotein, is involved in the unfolded protein response and differentially regulated by adaptive and acute ER stresses.Lectin chaperones help direct the maturation of glycoproteins in the endoplasmic reticulum.Selenium biochemistry and its role for human health.Emerging structural insights into glycoprotein quality control coupled with N-glycan processing in the endoplasmic reticulum.Biochemical characterization of the selenoproteome in Gallus gallus via bioinformatics analysis: structure-function relationships and interactions of binding molecules.Endoplasmic reticulum-resident selenoproteins as regulators of calcium signaling and homeostasis.Regulation of redox signaling by selenoproteins.Evidence for an unusual transmembrane configuration of AGG3, a class C Gγ subunit of Arabidopsis.An atypical heterotrimeric G-protein γ-subunit is involved in guard cell K⁺-channel regulation and morphological development in Arabidopsis thaliana.Comparative analysis of selenocysteine machinery and selenoproteome gene expression in mouse brain identifies neurons as key functional sites of selenium in mammals.The interaction of selenoprotein F (SELENOF) with retinol dehydrogenase 11 (RDH11) implied a role of SELENOF in vitamin A metabolism.Single-particle electron microscopy structure of UDP-glucose:glycoprotein glucosyltransferase suggests a selectivity mechanism for misfolded proteins.Selenoprotein P neutralizes lipopolysaccharide and participates in hepatic cell endoplasmic reticulum stress response.The 811 C/T polymorphism in the 3' untranslated region of the selenoprotein 15-kDa (Sep15) gene and breast cancer in Caucasian women.
P2860
Q24610122-DE73EA1B-EAF7-461D-99E6-99EF5CE0A05EQ24626002-9EE57AB5-5569-4ADD-9488-D9E04B65B506Q27863341-0591E63C-FFE2-4874-8D70-92082FD2AC8EQ27863410-E4F18BC3-41AA-467E-9C12-918D8D4AF84EQ28291028-5B02BD4C-26D8-47E1-BE3F-63828F7A8870Q33566592-483C3B37-A3CE-4BD5-8C87-7E527A032BDBQ33905782-0D5FAA22-927D-4420-A22E-5BF5E7497FFFQ33913069-CA9539EB-C0EB-4183-8188-83D1F199BA2BQ33934875-3334DDB8-39DE-4717-B4BC-680AC3A61B41Q34720949-EE4283C9-D4DD-4F17-A19C-C669E9840A1DQ36129752-977A3BA4-2AAC-481A-B29A-74774EECE8A3Q37235421-3BBDE505-6364-4A0B-907D-1641CFFD9623Q37392350-DAD2BD64-D518-408B-AB2F-2C104C984F71Q37424231-CD5C25DC-D9A0-4B1A-84EA-926DDC93474FQ37627987-E67C2404-E064-4729-BFFC-B23DA0074FC7Q38159453-5183E74A-3967-40F5-8CD7-19A1F3344F3BQ38342650-D0A69DBD-48C1-44D1-90DB-7463CB9B7F5BQ38770040-CFC7D473-4E6D-4904-96D9-49CF465D7F3CQ39307703-D4C2B98C-8263-40A1-A524-9F3A67B3D973Q40030288-CB702E84-AA96-42ED-9964-353BCE3B0B8BQ42175760-ED9E47AA-FB4A-48C2-81E7-6F5297A816B3Q42601056-872556F6-054A-4D51-90D6-6FAA5B109AA2Q46886702-B34861A9-F8C9-490C-92C7-63B519BCFD2CQ48095241-A5082290-A72D-4E61-872D-3C13D59470D6Q48162224-024EA39F-2CC2-45E7-B642-5810AC12F00DQ51320666-C4561448-6EB3-425E-A5BA-84A127095498Q53791912-19360179-6B02-4A9F-B344-64301B761F84
P2860
A novel cysteine-rich domain of Sep15 mediates the interaction with UDP-glucose:glycoprotein glucosyltransferase.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
@zh
2005年學術文章
@zh-hant
name
A novel cysteine-rich domain o ...... coprotein glucosyltransferase.
@en
A novel cysteine-rich domain o ...... coprotein glucosyltransferase.
@nl
type
label
A novel cysteine-rich domain o ...... coprotein glucosyltransferase.
@en
A novel cysteine-rich domain o ...... coprotein glucosyltransferase.
@nl
prefLabel
A novel cysteine-rich domain o ...... coprotein glucosyltransferase.
@en
A novel cysteine-rich domain o ...... coprotein glucosyltransferase.
@nl
P2093
P2860
P356
P1476
A novel cysteine-rich domain o ...... ycoprotein glucosyltransferase
@en
P2093
Andrew D Ferguson
Dmitri E Fomenko
Dolph L Hatfield
Vadim N Gladyshev
Yogarany Chelliah
P2860
P304
37839-37845
P356
10.1074/JBC.M508685200
P407
P577
2005-08-29T00:00:00Z