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Structure (78)
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Fowler, S. B., & Clarke, J. (2001). Mapping the Folding Pathway of an Immunoglobulin Domain. Structure, 9(5), 355–366.

Authors 2
  1. Susan B. Fowler (first)
  2. Jane Clarke (additional)
References 69 Referenced 176
  1. 10.1038/379096a0 / Nature / Conserved residues and the mechanism of protein folding by Shakhnovich (1996)
  2. 10.1006/jmbi.1997.1620 / J. Mol. Biol. / Protein folding and protein evolution by Ptitsyn (1998)
  3. 10.1006/jmbi.1999.2911 / J. Mol. Biol. / Universally conserved positions in protein folds by Mirny (1999)
  4. 10.1016/S0006-3495(00)76430-7 / Biophys. J. / Sequence evolution and the mechanism of protein folding by Oritz (2000)
  5. 10.1006/jmbi.1999.3663 / J. Mol. Biol. / Evolutionary conservation in protein folding kinetics by Plaxco (2000)
  6. 10.1038/14890 / Nat. Struct. Biol. / Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding by Chiti (1999)
  7. 10.1038/14896 / Nat. Struct. Biol. / The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved by Martinez (1999)
  8. 10.1038/nsb1096-874 / Nat. Struct. Biol. / Different folding transition states may result in the same native structure by Viguera (1996)
  9. 10.1002/(SICI)1097-0134(19981001)33:1<107::AID-PROT10>3.0.CO;2-P / Proteins / Folding mechanism of three structurally similar beta-sheet proteins by Burns (1998)
  10. 10.1006/jmbi.1998.2548 / J. Mol. Biol. / Rapid folding with and without populated intermediates in the homologous four-helix proteins Im7 and Im9 by Ferguson (1999)
  11. 10.1021/bi991937j / Biochemistry / Beta-sheet proteins with nearly identical structures have different folding intermediates by Dalessio (2000)
  12. 10.1038/77985 / Nat. Struct. Biol. / Conservation of folding pathways in evolutionarily distant globin sequences by Nishimura (2000)
  13. 10.1038/35011000 / Nature / A surprising simplicity to protein folding by Baker (2000)
  14. 10.1073/pnas.97.4.1525 / Proc. Natl. Acad. Sci. USA / Transition-state structure as a unifying basis in protein-folding mechanisms by Fersht (2000)
  15. 10.1021/bi000200n / Biochemistry / Topology, stability, sequence and length by Plaxco (2000)
  16. {'key': '10.1016/S0969-2126(01)00596-2_BIB16', 'first-page': '309', 'article-title': 'The immunoglobulin fold. Structural classification, sequence patterns and common core', 'volume': '242', 'author': 'Bork', 'year': '1994', 'journal-title': 'J. Mol. Biol.'} / J. Mol. Biol. / The immunoglobulin fold. Structural classification, sequence patterns and common core by Bork (1994)
  17. 10.1016/S0969-2126(99)80181-6 / Structure / Folding studies of Ig-like beta-sandwich proteins suggest a common folding pathway by Clarke (1999)
  18. 10.1016/S0959-440X(97)80054-1 / Curr. Opin. Struct. Biol. / Population statistics of protein structures by Brenner (1997)
  19. 10.1093/nar/28.1.263 / Nucleic Acids Res. / The Pfam protein families database by Bateman (2000)
  20. 10.1006/jmbi.1996.0665 / J. Mol. Biol. / Structure and stability of an immunoglobulin superfamily domain from twitchin, a muscle protein of the nematode Caenorhabditis elegans by Fong (1996)
  21. 10.1021/bi9801659 / Biochemistry / The effect of boundary selection on the stability and folding of the third fibronectin domain from human tenascin by Hamill (1998)
  22. 10.1110/ps.9.1.112 / Protein Sci. / Folding of beta-sandwich proteins by Cota (2000)
  23. 10.1006/jmbi.2000.4053 / J. Mol. Biol. / Two proteins with the same structure respond very differently to mutation- the role of plasticity in protein stability by Cota (2000)
  24. 10.1006/jmbi.1999.3360 / J. Mol. Biol. / Conservation of folding and stability within a protein family by Hamill (2000)
  25. 10.1006/jmbi.2000.3517 / J. Mol. Biol. / The folding of an immunoglobulin-like greek key protein is defined by a common core nucleus and regions constrained by topology by Hamill (2000)
  26. 10.1006/jmbi.2000.4378 / J. Mol. Biol. / The folding nucleus of a fibronectin type III domain is composed of core residues of the conserved immunoglobulin-like fold by Cota (2001)
  27. 10.1021/bi9817820 / Biochemistry / Effects of core mutations on the folding of a beta-sheet protein by Lorch (1999)
  28. 10.1006/jmbi.1998.2028 / J. Mol. Biol. / The assembly of immunoglobulin-like modules in titin by Improta (1998)
  29. 10.1073/pnas.96.7.3694 / Proc. Natl. Acad. Sci. USA. / Mechanical and chemical unfolding of a single protein by Carrion-Vasquez (1999)
  30. 10.1073/pnas.120048697 / Proc. Natl. Acad. Sci. USA / Atomic force microscopy reveals the mechanical design of a modular protein by Li (2000)
  31. 10.1021/bi00181a604 / Biochemistry / Immunoglobulin-type domains of titin by Politou (1994)
  32. 10.1016/S0006-3495(95)80131-1 / Biophys. J. / The folding and stability of titin immunoglobulin-like modules with implications for the mechanism of elasticity by Politou (1995)
  33. 10.1016/S0969-2126(96)00036-6 / Structure / Immunoglobulin-like modules from titin I-band by Improta (1996)
  34. 10.1006/jmbi.1996.0050 / J. Mol. Biol. / The elastic I-band region of titin is assembled in a “modular” fashion by weakly interacting Ig-like domains by Politou (1996)
  35. 10.1021/bi971294c / Biochemistry / Acquisition of native beta-strand topology during the rapid collapse phase of protein folding by Parker (1997)
  36. 10.1006/jmbi.1996.0736 / J. Mol. Biol. / Module-module interactions in the cell binding region of fibronectin by Spitzfaden (1997)
  37. 10.1006/jmbi.1997.1553 / J. Mol. Biol. / Folding kinetics of the SH3 domain of PI3 kinase by real-time NMR combined with optical spectroscopy by Guijarro (1998)
  38. 10.1021/bi972075u / Biochemistry / The folding kinetics and thermodynamics of the Fyn-SH3 domain by Plaxco (1998)
  39. 10.1038/14901 / Nat. Struct. Biol. / Experiment and theory highlight role of native state topology in SH3 folding by Riddle (1999)
  40. {'key': '10.1016/S0969-2126(01)00596-2_BIB40', 'series-title': 'Structure and Mechanism in Protein Science', 'author': 'Fersht', 'year': '1998'} / Structure and Mechanism in Protein Science by Fersht (1998)
  41. 10.1038/342296a0 / Nature / Capping and alpha-helix stability by Serrano (1989)
  42. 10.1021/bi00040a016 / Biochemistry / Structural factors contributing to the hydrophobic effect by Otzen (1995)
  43. 10.1021/bi973111s / Biochemistry / Context dependent nature of destabilising mutants on the stability of FKBP12 by Main (1998)
  44. 10.1016/0022-2836(92)90561-W / J. Mol. Biol. / The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding by Fersht (1992)
  45. 10.1016/0959-440X(95)80012-P / Curr. Opin. Struct. Biol. / Characterizing transition states in protein folding by Fersht (1995)
  46. 10.1021/bi00041a047 / Biochemistry / Movement of the position of the transition state in protein folding by Matouschek (1995)
  47. 10.1006/jmbi.1997.1612 / J. Mol. Biol. / The changing nature of the protein folding transition state by Oliveberg (1998)
  48. 10.1021/bi982819j / Biochemistry / Structural changes in the transition state of protein folding by Otzen (1999)
  49. 10.1038/nsb0497-305 / Nat. Struct. Biol. / The energy landscape of a fast-folding protein mapped by Ala→Gly substitutions by Burton (1997)
  50. 10.1021/ja01607a027 / J. Am. Chem. Soc. / A correlation of reaction rates by Hammond (1955)
  51. 10.1073/pnas.90.16.7814 / Proc. Natl. Acad. Sci. USA / Application of physical-organic chemistry to engineered mutants of proteins by Matouschek (1993)
  52. 10.1006/jmbi.1995.0616 / J. Mol. Biol. / The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods-evidence for a nucleation-condensation mechanism for protein folding by Itzhaki (1995)
  53. 10.1021/bi00020a027 / Biochemistry / Exploring the energy surface of protein folding by structure-reactivity relationships and engineered proteins by Matthews (1995)
  54. 10.1073/pnas.96.26.14854 / Proc. Natl. Acad. Sci. USA / From snapshot to movie by Ternstrom (1999)
  55. 10.1021/bi972798d / Biochemistry / Movement of the intermediate and rate determining transition state of barnase on the energy landscape with changing temperature by Dalby (1998)
  56. 10.1021/ja981558y / J. Am. Chem. Soc. / Combined molecular dynamics and phi value analysis of structure-reactivity relationships in the transition state and unfolding pathway of barnase by Daggett (1998)
  57. 10.1073/pnas.95.9.4976 / Proc. Natl. Acad. Sci. U.S.A. / How evolution makes proteins fold quickly by Mirny (1998)
  58. 10.1021/bi982427c / Biochemistry / Conserved residues and their role in the structure, function, and stability of acyl-coenzyme A binding protein by Kragelund (1999)
  59. 10.1021/bi00174a022 / Biochemistry / Thermodynamic and kinetic analysis of the SH3 domain of spectrin shows a two-state folding transition by Viguera (1994)
  60. 10.1021/bi971786p / Biochemistry / Folding dynamics of the src SH3 domain by Grantcharova (1997)
  61. 10.1038/nsb1097-805 / Nat. Struct. Biol. / Functional rapidly folding proteins from simplified amino acid sequences by Riddle (1997)
  62. 10.1006/jmbi.2000.3701 / J. Mol. Biol. / A breakdown of symmetry in the folding transition state of protein L by Kim (2000)
  63. 10.1038/77971 / Nat. Struct. Biol. / Critical role of beta-hairpin formation in protein G by McCallister (2000)
  64. Hubbard, S.J., and Thornton, J.M. (1993). NACCESS: Computer program. Department of Biochemistry and Molecular Biology, University College London, UK.
  65. 10.1016/0076-6879(86)31045-0 / Methods Enzymol. / Determination and analysis of urea and guanidinium hydrochloride denaturation curves by Pace (1986)
  66. 10.1021/bi00067a022 / Biochemistry / Engineered dilsulfide bonds as probes of the folding pathway of barnase by Clarke (1993)
  67. 10.1021/bi00107a010 / Biochemistry / Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition by Jackson (1991)
  68. 10.1006/jmbi.1994.1312 / J. Mol. Biol. / Many of the immunoglobulin superfamily domains in cell adhesion molecules and surface receptors belong to a new structural set which is close to that containing variable domains by Harpaz (1994)
  69. 10.1107/S0021889891004399 / J. Appl. Crystallogr. / MolScript, a program to produce both detailed and schematic plots of protein structures by Kraulis (1991)
Dates
Type When
Created 23 years, 1 month ago (July 25, 2002, 6:07 p.m.)
Deposited 6 years, 4 months ago (April 19, 2019, 10:26 a.m.)
Indexed 2 months, 3 weeks ago (June 5, 2025, 9:41 a.m.)
Issued 24 years, 4 months ago (May 1, 2001)
Published 24 years, 4 months ago (May 1, 2001)
Published Print 24 years, 4 months ago (May 1, 2001)
Funders 0

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@article{Fowler_2001, title={Mapping the Folding Pathway of an Immunoglobulin Domain}, volume={9}, ISSN={0969-2126}, url={http://dx.doi.org/10.1016/s0969-2126(01)00596-2}, DOI={10.1016/s0969-2126(01)00596-2}, number={5}, journal={Structure}, publisher={Elsevier BV}, author={Fowler, Susan B. and Clarke, Jane}, year={2001}, month=may, pages={355–366} }