The pleiotropic functions of the Y-box-binding protein, YB-1
โ Scribed by Kimitoshi Kohno; Hiroto Izumi; Takeshi Uchiumi; Megumi Ashizuka; Michihiko Kuwano
- Publisher
- John Wiley and Sons
- Year
- 2003
- Tongue
- English
- Weight
- 215 KB
- Volume
- 25
- Category
- Article
- ISSN
- 0265-9247
No coin nor oath required. For personal study only.
โฆ Synopsis
Abstract
The Yโboxโbinding protein (YBโ1) represents the most evolutionary conserved nucleicโacidโbinding protein currently known. YBโ1 is a member of the coldโshock domain (CSD) protein superfamily. It performs a wide variety of cellular functions, including transcriptional regulation, translational regulation, DNA repair, drug resistance and stress responses to extracellular signals. As a result, YBโ1 expression is closely associated with cell proliferation. In this review, we will begin by briefly describing the characteristics of YBโ1 and will then summarize the pleiotropic functions brought about via DNAโRNA transaction and proteinโprotein interactions. In addition, we will discuss the diverse range of potential physiological and pathological functions of YBโ1. BioEssays 25:691โ698, 2003. ยฉ 2003 Wiley Periodicals, Inc.
๐ SIMILAR VOLUMES
## BACKGROUND. Nuclear expression of Y box-binding protein (YB-1), a member of the DNA binding protein family, has been reported to be much more highly concentrated in cisplatin-resistant cell lines than in their parental counterparts, suggesting an ability to limit cisplatin sensitivity. Moreover,
## Abstract For Abstract see ChemInform Abstract in Full Text.
The complex sensation of vision begins with the relatively simple photoisomerization of the visual pigment chromophore 11-cis-retinal to its all-trans configuration. This event initiates a series of biochemical reactions that are collectively referred to as phototransduction, which ultimately lead t