YTH: A new domain in nuclear proteins

Peter Stoilov; Ilona Rafalska; Stefan Stamm

doi:10.1016/S0968-0004(02)02189-8

YTH: A new domain in nuclear proteins

Peter Stoilov
, Ilona Rafalska
, Stefan Stamm

Research output: Contribution to journal › Short survey › peer-review

168 Scopus citations

Abstract

A novel 100-150-residue domain has been identified in the human splicing factor YT521-B and its Drosophila and yeast homologues. Homology searches show that the domain is typical for the eukaryotes and is particularly abundant in plants. It is predicted to adopt a mixed α-helix-β-sheet fold and to bind to RNA. We propose the name YTH (for YT521-B homology) for the domain.

Original language	English
Pages (from-to)	495-497
Number of pages	3
Journal	Trends in Biochemical Sciences
Volume	27
Issue number	10
DOIs	https://doi.org/10.1016/S0968-0004(02)02189-8
State	Published - Oct 1 2002

ASJC Scopus subject areas

Biochemistry
Molecular Biology

Access to Document

10.1016/S0968-0004(02)02189-8

Cite this

@article{5a864cb94d4843ea9dc8d3b9d48354f7,

title = "YTH: A new domain in nuclear proteins",

abstract = "A novel 100-150-residue domain has been identified in the human splicing factor YT521-B and its Drosophila and yeast homologues. Homology searches show that the domain is typical for the eukaryotes and is particularly abundant in plants. It is predicted to adopt a mixed α-helix-β-sheet fold and to bind to RNA. We propose the name YTH (for YT521-B homology) for the domain.",

author = "Peter Stoilov and Ilona Rafalska and Stefan Stamm",

year = "2002",

month = oct,

day = "1",

doi = "10.1016/S0968-0004(02)02189-8",

language = "English",

volume = "27",

pages = "495--497",

number = "10",

}

TY - JOUR

T1 - YTH

T2 - A new domain in nuclear proteins

AU - Stoilov, Peter

AU - Rafalska, Ilona

AU - Stamm, Stefan

PY - 2002/10/1

Y1 - 2002/10/1

N2 - A novel 100-150-residue domain has been identified in the human splicing factor YT521-B and its Drosophila and yeast homologues. Homology searches show that the domain is typical for the eukaryotes and is particularly abundant in plants. It is predicted to adopt a mixed α-helix-β-sheet fold and to bind to RNA. We propose the name YTH (for YT521-B homology) for the domain.

AB - A novel 100-150-residue domain has been identified in the human splicing factor YT521-B and its Drosophila and yeast homologues. Homology searches show that the domain is typical for the eukaryotes and is particularly abundant in plants. It is predicted to adopt a mixed α-helix-β-sheet fold and to bind to RNA. We propose the name YTH (for YT521-B homology) for the domain.

UR - https://www.scopus.com/pages/publications/0036805371

UR - https://www.scopus.com/pages/publications/0036805371#tab=citedBy

U2 - 10.1016/S0968-0004(02)02189-8

DO - 10.1016/S0968-0004(02)02189-8

M3 - Short survey

C2 - 12368078

AN - SCOPUS:0036805371

SN - 0968-0004

VL - 27

SP - 495

EP - 497

JO - Trends in Biochemical Sciences

JF - Trends in Biochemical Sciences

IS - 10

ER -

YTH: A new domain in nuclear proteins

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this