Literature DB >> 8256281

Is the slow exchange core the protein folding core?

C Woodward1.   

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Year:  1993        PMID: 8256281     DOI: 10.1016/0968-0004(93)90086-3

Source DB:  PubMed          Journal:  Trends Biochem Sci        ISSN: 0968-0004            Impact factor:   13.807


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  24 in total

1.  Cooperative folding units of escherichia coli tryptophan repressor.

Authors:  A Wallqvist; T A Lavoie; J A Chanatry; D G Covell; J Carey
Journal:  Biophys J       Date:  1999-09       Impact factor: 4.033

2.  The propagation of binding interactions to remote sites in proteins: analysis of the binding of the monoclonal antibody D1.3 to lysozyme.

Authors:  E Freire
Journal:  Proc Natl Acad Sci U S A       Date:  1999-08-31       Impact factor: 11.205

Review 3.  The hydrogen exchange core and protein folding.

Authors:  R Li; C Woodward
Journal:  Protein Sci       Date:  1999-08       Impact factor: 6.725

4.  Antibody-detected folding: kinetics of surface epitope formation are distinct from other folding phases.

Authors:  C S Raman; R Jemmerson; B T Nall
Journal:  Protein Sci       Date:  2000-01       Impact factor: 6.725

5.  Can allosteric regulation be predicted from structure?

Authors:  E Freire
Journal:  Proc Natl Acad Sci U S A       Date:  2000-10-24       Impact factor: 11.205

6.  Early formation of a beta hairpin during folding of staphylococcal nuclease H124L as detected by pulsed hydrogen exchange.

Authors:  William F Walkenhorst; Jason A Edwards; John L Markley; Heinrich Roder
Journal:  Protein Sci       Date:  2002-01       Impact factor: 6.725

Review 7.  Seven transmembrane receptors as shapeshifting proteins: the impact of allosteric modulation and functional selectivity on new drug discovery.

Authors:  Terry Kenakin; Laurence J Miller
Journal:  Pharmacol Rev       Date:  2010-04-14       Impact factor: 25.468

8.  Tracing primordial protein evolution through structurally guided stepwise segment elongation.

Authors:  Hideki Watanabe; Kazuhiko Yamasaki; Shinya Honda
Journal:  J Biol Chem       Date:  2013-12-19       Impact factor: 5.157

9.  The pH dependence of hydrogen-deuterium exchange in trp repressor: the exchange rate of amide protons in proteins reflects tertiary interactions, not only secondary structure.

Authors:  M D Finucane; O Jardetzky
Journal:  Protein Sci       Date:  1996-04       Impact factor: 6.725

10.  The equilibrium unfolding of Azotobacter vinelandii apoflavodoxin II occurs via a relatively stable folding intermediate.

Authors:  C P van Mierlo; W M van Dongen; F Vergeldt; W J van Berkel; E Steensma
Journal:  Protein Sci       Date:  1998-11       Impact factor: 6.725

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