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Literature DB >> 22218948

New mammalian selenium-containing protein V: the search for protein partners.

E G Varlamova¹, S V Novoselov, V I Novoselov, E E Fesenko.

Abstract

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Year: 2012 PMID： 22218948 DOI： 10.1134/S1607672911060056

Source DB: PubMed Journal: Dokl Biochem Biophys ISSN： 1607-6729 Impact factor: 0.788

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10 in total

1. Phosphorylation and glycosylation of nucleoporins.

Authors: M W Miller; M R Caracciolo; W K Berlin; J A Hanover
Journal: Arch Biochem Biophys Date: 1999-07-01 Impact factor: 4.013

2. SelT, SelW, SelH, and Rdx12: genomics and molecular insights into the functions of selenoproteins of a novel thioredoxin-like family.

Authors: Alexander Dikiy; Sergey V Novoselov; Dmitri E Fomenko; Aniruddha Sengupta; Bradley A Carlson; Ronald L Cerny; Krzysztof Ginalski; Nick V Grishin; Dolph L Hatfield; Vadim N Gladyshev
Journal: Biochemistry Date: 2007-05-16 Impact factor: 3.162

3. Dynamic interplay between O-glycosylation and O-phosphorylation of nucleocytoplasmic proteins: alternative glycosylation/phosphorylation of THR-58, a known mutational hot spot of c-Myc in lymphomas, is regulated by mitogens.

Authors: Kazuo Kamemura; Bradley K Hayes; Frank I Comer; Gerald W Hart
Journal: J Biol Chem Date: 2002-03-19 Impact factor: 5.157

1 in total

1. Protein Partners of Selenoprotein SELM and the Role of Selenium Compounds in Regulation of Its Expression in Human Cancer Cells.

Authors: E G Varlamova; M V Goltyaev; E E Fesenko
Journal: Dokl Biochem Biophys Date: 2019-11-25 Impact factor: 0.788

1 in total

New mammalian selenium-containing protein V: the search for protein partners.

1. Phosphorylation and glycosylation of nucleoporins.

2. SelT, SelW, SelH, and Rdx12: genomics and molecular insights into the functions of selenoproteins of a novel thioredoxin-like family.

3. Dynamic interplay between O-glycosylation and O-phosphorylation of nucleocytoplasmic proteins: alternative glycosylation/phosphorylation of THR-58, a known mutational hot spot of c-Myc in lymphomas, is regulated by mitogens.

4. RNA polymerase II is a glycoprotein. Modification of the COOH-terminal domain by O-GlcNAc.

5. Reciprocity between O-GlcNAc and O-phosphate on the carboxyl terminal domain of RNA polymerase II.

6. Reduced O glycosylation of Sp1 is associated with increased proteasome susceptibility.

7. Glycosylation of the c-Myc transactivation domain.

8. Roles of the tetratricopeptide repeat domain in O-GlcNAc transferase targeting and protein substrate specificity.

9. Characterization of mammalian selenoproteomes.

10. Expression of testis specific ankyrin repeat and SOCS box-containing 17 gene.

1. Protein Partners of Selenoprotein SELM and the Role of Selenium Compounds in Regulation of Its Expression in Human Cancer Cells.