Literature DB >> 16742616

The chemical nature of the site of action of dicyclohexylcarbodi-imide in mitochondria.

I G Knight1, C T Holloway, A M Roberton, R B Beechey.   

Abstract

Entities:  

Year:  1968        PMID： 16742616      PMCID： PMC1186858          DOI： 10.1042/bj1090027p

Source DB:  PubMed          Journal:  Biochem J        ISSN： 0264-6021            Impact factor:   3.857


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  4 in total

1.  The isolation of dicyclohexylcarbodi-imide-binding proteins from mitochondrial membranes.

Authors:  K J Cattell; I G Knight; C R Lindop; R B Beechey
Journal:  Biochem J       Date:  1970-05       Impact factor: 3.857

Review 2.  Structure and function of the membrane-integral components of the mitochondrial H+-ATPase.

Authors:  J Houstĕk; J Kopecký; P Svoboda; Z Drahota
Journal:  J Bioenerg Biomembr       Date:  1982-02       Impact factor: 2.945

3.  The effects of carbodiimides on functions associated with the energy-conservation mechanism in beef heart sub-mitochondrial particles.

Authors:  R B Beechey; I G Knight
Journal:  J Bioenerg Biomembr       Date:  1978-08       Impact factor: 2.945

Review 4.  The 3D structures of VDAC represent a native conformation.

Authors:  Sebastian Hiller; Jeff Abramson; Carmen Mannella; Gerhard Wagner; Kornelius Zeth
Journal:  Trends Biochem Sci       Date:  2010-08-12       Impact factor: 13.807
  4 in total

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