Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Editor

Personal info

View

About

Terms

Javascript disabled

Please enable Javascript support in your browser to use this application.

Instructions on how to enable JavaScript on different browsers can be found here: http://www.google.com/support/bin/answer.py?answer=23852.

[edit this page]

Gene Review:

CYTH4 - cytohesin 4

Homo sapiens

Synonyms: CYT4, Cytohesin-4, DJ63G5.1, PH, SEC7 and coiled-coil domain-containing protein 4, PSCD4, ...

Ogasawara, M. et al., Suzuki, I. et al.

Ogasawara, Kim, Adamik, Togawa, Ferrans, Takeda, Kirby, Moss, Vaughan,

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

High impact information on PSCD4

Two mRNAs with and without the 3-base pair sequence were found in brain in different ratios for cytohesin-1, -2, and -3 but not cytohesin-4 [1].
Thus, in gene structure and brefeldin A-insensitive GEP activity, cytohesin-4 resembles other cytohesins, but its tissue distribution differs considerably, consistent with a different specific function [1].
A novel ARF GEP, designated cytohesin-4, was cloned from a human brain cDNA library [1].
A cytohesin-4 mRNA of approximately 3.7 kilobases, abundant in leukocytes, was not detected in most tissues [1].
Among separated populations of blood cells, approximately 90% of CD33(+) (monocytes), 80% of CD2(+) (NK/T), and 10-20% of CD19(+) (B) cells contained cytohesin-4 mRNA by in situ hybridization [1].

Biological context of PSCD4

No obvious gene expression for cytohesin-4 and ARF-GEP100 was detected in the brain at any stages of development [2].

Associations of PSCD4 with chemical compounds

Similarities in function and gene structure of cytohesin-4 and cytohesin-1, guanine nucleotide-exchange proteins for ADP-ribosylation factors [1].

References

Similarities in function and gene structure of cytohesin-4 and cytohesin-1, guanine nucleotide-exchange proteins for ADP-ribosylation factors. Ogasawara, M., Kim, S.C., Adamik, R., Togawa, A., Ferrans, V.J., Takeda, K., Kirby, M., Moss, J., Vaughan, M. J. Biol. Chem. (2000) [Pubmed]
Localization of mRNAs for subfamily of guanine nucleotide-exchange proteins (GEP) for ARFs (ADP-ribosylation factors) in the brain of developing and mature rats under normal and postaxotomy conditions. Suzuki, I., Owada, Y., Suzuki, R., Yoshimoto, T., Kondo, H. Brain Res. Mol. Brain Res. (2002) [Pubmed]

Contributions to this collaborative article are from individual authors of WikiGenes or mined by the WikiGenes Data Mining Engine from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenes Open Access Licence Privacy Policy Terms of Use apsburg

CYTH4	Bos taurus
CYTH4	Canis lupus familiaris
cyth4a	Danio rerio
cyth4b	Danio rerio
CYTH4	Gallus gallus
CYTH4	Macaca mulatta
Cyth4	Mus musculus
CYTH4	Pan troglodytes
Cyth4	Rattus norvegicus

The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.