ArticleProceedings of the National Academy of Sciences of the United States of America1999
Kinetic evidence for an on-pathway intermediate in the folding of cytochrome c.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 62 citations in OpenAlex.
- Differentiating between the sequence of structural events on alternative pathways of folding of a heterodimeric protein.Protein science : a publication of the Protein Society · 2022Article
- Protein folding in vitro and in the cell: From a solitary journey to a team effort.Biophysical chemistry · 2022Review
- The role of key residues in structure, function, and stability of cytochrome-c.Cellular and molecular life sciences : CMLS · 2014Review
- Kinetically trapped metastable intermediate of a disulfide-deficient mutant of the starch-binding domain of glucoamylase.Protein science : a publication of the Protein Society · 2009Article
- NMR analysis of partially folded states and persistent structure in the alpha subunit of tryptophan synthase: implications for the equilibrium folding mechanism of a 29-kDa TIM barrel protein.Journal of molecular biology · 2008Article
- A unified mechanism for protein folding: predetermined pathways with optional errors.Protein science : a publication of the Protein Society · 2007Article
- The folding pathway of T4 lysozyme: an on-pathway hidden folding intermediate.Journal of molecular biology · 2007Article
- A PDZ domain recapitulates a unifying mechanism for protein folding.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- A protein folding pathway with multiple folding intermediates at atomic resolution.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- The 40s Omega-loop plays a critical role in the stability and the alkaline conformational transition of cytochrome c.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2004Article
- Demonstration of a low-energy on-pathway intermediate in a fast-folding protein by kinetics, protein engineering, and simulation.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Cytochrome c folding pathway: kinetic native-state hydrogen exchange.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Folding and signaling share the same pathway in a photoreceptor.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- An amino acid code for protein folding.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Integrity of thermus thermophilus cytochrome c552 synthesized by Escherichia coli cells expressing the host-specific cytochrome c maturation genes, ccmABCDEFGH: biochemical, spectral, and structural characterization of the recombinant protein.Protein science : a publication of the Protein Society · 2000Article
- An essential intermediate in the folding of dihydrofolate reductase.Proceedings of the National Academy of Sciences of the United States of America · 2000Article
- Kinetic evidence of an on-pathway intermediate in the folding of lysozyme.Protein science : a publication of the Protein Society · 2000Article
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
An early folding event of cytochrome c populates a helix-containing intermediate (INC) because of a pH-dependent misligation between the heme iron and nonnative ligands in the unfolded state (U). For folding to proceed, the nonnative ligation error must first be corrected. It is not known whether I is on-pathway, with folding to the native state (N) as in U <-->INC <--> N, or whether the I must first move back through the U and then fold to the N through some alternative path (INC <--> U <--> N). By means of a kinetic test, it is shown here that the cytochrome c I does not first unfold to U. The method used provides an experimental criterion for rejecting the off-pathway I <--> U <--> N option.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.