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.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Editor

Share

Personal info

View

Links

  • Homologues
  • NCBI Gene
  • NCBI SNP
  • iHOP resource
  • SNPedia

Table of contents

About

Terms

 

Gene Review: 

SDHA  -  succinate dehydrogenase complex, subunit A...

Bos taurus

 
 
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 SDHA

  • Iron-sulfur clusters S-1, S-2, and S-3 were assembled also when the covalently bound flavin in the Fp subunit was absent [1].
  • Iron-sulfur cluster S-1 was found to be assembled in soluble succinate dehydrogenase subunits in the cytoplasm, but only if full-length Fp polypeptides and relatively large fragments of Ip polypeptides were present [1].
  • Furthermore, the Ascaris Fp subunit was shown to contain two regions exhibiting striking sequence similarity to the segments that have been predicted to interact noncovalently with the AMP moiety of FAD in bacterial Fp subunits [2].
  • Mapping of the SDHA locus to bovine chromosome 20 [3].
 

Associations of SDHA with chemical compounds

  • Succinate dehydrogenase is a conserved membrane-bound enzyme consisting of two nonidentical subunits: a flavo iron-sulfur protein (Fp) subunit, containing a covalently bound flavin, and an iron-sulfur protein (Ip) subunit [1].
  • The flavoprotein (Fp) subunit of mitochondrial complex II contains covalently bound FAD as a prosthetic group [2].

References

  1. Characterization by electron paramagnetic resonance and studies on subunit location and assembly of the iron-sulfur clusters of Bacillus subtilis succinate dehydrogenase. Hederstedt, L., Maguire, J.J., Waring, A.J., Ohnishi, T. J. Biol. Chem. (1985) [Pubmed]
  2. Structural studies on three flavin-interacting regions of the flavoprotein subunit of complex II in Ascaris suum mitochondria. Furushima, R., Kita, K., Takamiya, S., Konishi, K., Aoki, T., Oya, H. FEBS Lett. (1990) [Pubmed]
  3. Mapping of the SDHA locus to bovine chromosome 20. Sonstegard, T.S., Kappes, S.M. Anim. Genet. (1999) [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 WikiGenesOpen Access LicencePrivacy PolicyTerms of Useapsburg
 
WikiGenes - Universities