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Literature DB >> 5062485

Participation of the protein ligands in the folding of cytochrome c.

J Babul, E Stellwagen.

Abstract

Entities: Gene

Mesh：

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Year: 1972 PMID： 5062485 DOI： 10.1021/bi00757a013

Source DB: PubMed Journal: Biochemistry ISSN： 0006-2960 Impact factor: 3.162

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24 in total

1. Compactness of the denatured state of a fast-folding protein measured by submillisecond small-angle x-ray scattering.

Authors: L Pollack; M W Tate; N C Darnton; J B Knight; S M Gruner; W A Eaton; R H Austin
Journal: Proc Natl Acad Sci U S A Date: 1999-08-31 Impact factor: 11.205

2. An electrospray-ionization mass spectrometry analysis of the pH-dependent dissociation and denaturation processes of a heterodimeric protein.

Authors: T Kashiwagi; N Yamada; K Hirayama; C Suzuki; Y Kashiwagi; F Tsuchiya; Y Arata; N Kunishima; K Morikawa
Journal: J Am Soc Mass Spectrom Date: 2000-01 Impact factor: 3.109

3. Unfolding and refolding of cytochrome c driven by the interaction with lipid micelles.

Authors: N Sanghera; T J Pinheiro
Journal: Protein Sci Date: 2000-06 Impact factor: 6.725

4. RNA oxidation catalyzed by cytochrome c leads to its depurination and cross-linking, which may facilitate cytochrome c release from mitochondria.

Authors: Mikiei Tanaka; Pawel Jaruga; Pascal A Küpfer; Christian J Leumann; Miral Dizdaroglu; William E Sonntag; P Boon Chock
Journal: Free Radic Biol Med Date: 2012-06-07 Impact factor: 7.376

5. Investigations on the Q and CT Bands of Cytochrome c Submonolayer Adsorbed on an Alumina Surface Using Broadband Spectroscopy with Single-Mode Integrated Optical Waveguides.

Authors: Rodrigo S Wiederkehr; Geoffrey C Hoops; Mustafa M Aslan; Courtney L Byard; Sergio B Mendes
Journal: J Phys Chem C Nanomater Interfaces Date: 2009-05-14 Impact factor: 4.126

10. His26 protonation in cytochrome c triggers microsecond β-sheet formation and heme exposure: implications for apoptosis.

Authors: Gurusamy Balakrishnan; Ying Hu; Thomas G Spiro
Journal: J Am Chem Soc Date: 2012-11-06 Impact factor: 15.419

Participation of the protein ligands in the folding of cytochrome c.

1. Compactness of the denatured state of a fast-folding protein measured by submillisecond small-angle x-ray scattering.

2. An electrospray-ionization mass spectrometry analysis of the pH-dependent dissociation and denaturation processes of a heterodimeric protein.

3. Unfolding and refolding of cytochrome c driven by the interaction with lipid micelles.

4. RNA oxidation catalyzed by cytochrome c leads to its depurination and cross-linking, which may facilitate cytochrome c release from mitochondria.

5. Investigations on the Q and CT Bands of Cytochrome c Submonolayer Adsorbed on an Alumina Surface Using Broadband Spectroscopy with Single-Mode Integrated Optical Waveguides.

6. Volume changes of the molten globule transitions of horse heart ferricytochrome c: a thermodynamic cycle.

7. Acid-induced folding of proteins.

8. Submillisecond protein folding kinetics studied by ultrarapid mixing.

9. Heterogeneous folding and stretched kinetics.

10. His26 protonation in cytochrome c triggers microsecond β-sheet formation and heme exposure: implications for apoptosis.