Analyze Diet

A biologically active, three-fragment complex of horse heart cytochrome c.

Abstract: No abstract available
Publication Date: 1980-02-10 PubMed ID: 6243298
The Equine Research Bank provides access to a large database of publicly available scientific literature. Inclusion in the Research Bank does not imply endorsement of study methods or findings by Mad Barn.
  • Journal Article

Cite This Article

APA
Juillerat M, Parr GR, Taniuchi H. (1980). A biologically active, three-fragment complex of horse heart cytochrome c. J Biol Chem, 255(3), 845-853.

Publication

ISSN: 0021-9258
NlmUniqueID: 2985121R
Country: United States
Language: English
Volume: 255
Issue: 3
Pages: 845-853

Researcher Affiliations

Juillerat, M
    Parr, G R
      Taniuchi, H

        MeSH Terms

        • Amino Acids / analysis
        • Animals
        • Cytochrome c Group / metabolism
        • Heme
        • Horses
        • Kinetics
        • Myocardium / metabolism
        • Peptide Fragments / analysis
        • Protein Conformation
        • Trypsin

        Citations

        This article has been cited 9 times.
        1. Lindman S, Hernandez-Garcia A, Szczepankiewicz O, Frohm B, Linse S. In vivo protein stabilization based on fragment complementation and a split GFP system.. Proc Natl Acad Sci U S A 2010 Nov 16;107(46):19826-31.
          doi: 10.1073/pnas.1005689107pubmed: 21041669google scholar: lookup
        2. Taniuchi H, Shi Y, San Miguel GI, Ferretti JA, Mack JW, Fisher A, Shah M, Schechter AN, Shiloach J. A study of the influence of the hydrophobic core residues of yeast iso-2-cytochrome c on phosphate binding: a probe of the hydrophobic core-surface charge interactions.. J Protein Chem 2001 Apr;20(3):203-15.
          doi: 10.1023/a:1010906929793pubmed: 11565900google scholar: lookup
        3. Berggård T, Thulin E, Akerfeldt KS, Linse S. Fragment complementation of calbindin D28k.. Protein Sci 2000 Nov;9(11):2094-108.
          doi: 10.1110/ps.9.11.2094pubmed: 11152121google scholar: lookup
        4. Bell S, Matthews JR, Jaffray E, Hay RT. I(kappa)B(gamma) inhibits DNA binding of NF-kappaB p50 homodimers by interacting with residues that contact DNA.. Mol Cell Biol 1996 Nov;16(11):6477-85.
          doi: 10.1128/MCB.16.11.6477pubmed: 8887676google scholar: lookup
        5. Hanai R, Wang JC. Protein footprinting by the combined use of reversible and irreversible lysine modifications.. Proc Natl Acad Sci U S A 1994 Dec 6;91(25):11904-8.
          doi: 10.1073/pnas.91.25.11904pubmed: 7991555google scholar: lookup
        6. Juillerat M, Taniuchi H. Conformational dynamics of a biologically active three-fragment complex of horse cytochrome c.. Proc Natl Acad Sci U S A 1982 Mar;79(6):1825-9.
          doi: 10.1073/pnas.79.6.1825pubmed: 6281788google scholar: lookup
        7. Takano T, Dickerson RE. Redox conformation changes in refined tuna cytochrome c.. Proc Natl Acad Sci U S A 1980 Nov;77(11):6371-5.
          doi: 10.1073/pnas.77.11.6371pubmed: 6256733google scholar: lookup
        8. Rackovsky S, Goldstein DA. On the redox conformational change in cytochrome c.. Proc Natl Acad Sci U S A 1984 Sep;81(18):5901-5.
          doi: 10.1073/pnas.81.18.5901pubmed: 6091118google scholar: lookup
        9. Proudfoot AE, Offord RE, Rose K, Schmidt M, Wallace CJ. A case of spurious product formation during attempted resynthesis of proteins by reverse proteolysis. Some batches of 'pure' glycerol contain cross-linking agents.. Biochem J 1984 Jul 15;221(2):325-31.
          doi: 10.1042/bj2210325pubmed: 6089735google scholar: lookup