D. Baker, J. L. Sohl, and D. A. Agard, A protein-folding reaction under kinetic control, Nature, vol.356, issue.6366, pp.263-265, 1992.
DOI : 10.1038/356263a0

S. Brahms and J. Brahms, Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroism, Journal of Molecular Biology, vol.138, issue.2, pp.149-178, 1980.
DOI : 10.1016/0022-2836(80)90282-X

P. Bryan, Subtilisin engineered for Facile folding: analysis of uncatalyzed and prodomain catalyzed folding, In Intramolecular Chaperones and Protein Folding, pp.85-112, 1995.

P. Bryan, L. Wang, J. Hoskins, S. Ruvinov, S. Strausberg et al., Catalysis of a protein folding reaction: Mechanistic implications of the 2.0 .ANG. structure of the subtilisin-prodomain complex, Biochemistry, vol.34, issue.32, pp.10310-10318, 1995.
DOI : 10.1021/bi00032a026

S. C. Chang, P. C. Chang, and Y. H. Lee, The roles of propeptide in maturation and secretion of Npr protease from Streptomyces, J. Biol. Chem, vol.269, pp.3548-3554, 1994.

G. E. Conner, The role of the cathepsin D propeptide in sorting to the lysosome, J. Biol. Chem, vol.267, pp.21738-21745, 1992.

A. E. Eakin, M. E. Mcgrath, J. H. Mckerrow, R. J. Fletterick, and C. S. Craik, Production of crystallizable cruzain, the major cysteine protease from Trypanosoma cruzi, J. Biol. Chem, vol.268, pp.6115-6118, 1993.

J. Eder, M. Rheinnecker, and A. Fersht, Folding of Subtilisin BPN': Role of the Pro-sequence, Journal of Molecular Biology, vol.233, issue.2, pp.293-304, 1993.
DOI : 10.1006/jmbi.1993.1507

J. Eder and A. R. Fersht, Pro-sequence-assisted protein folding, Molecular Microbiology, vol.88, issue.4, pp.609-614, 1995.
DOI : 10.1038/339483a0

J. Eder, M. Rheinnecker, and A. Fersht, Folding of subtilisin BPN': characterization of a folding intermediate, Biochemistry, vol.32, issue.1, pp.18-26, 1993.
DOI : 10.1021/bi00052a004

X. Fu, M. Inouye, and U. P. Shinde, Folding Pathway Mediated by an Intramolecular Chaperone. THE INHIBITORY AND CHAPERONE FUNCTIONS OF THE SUBTILISIN PROPEPTIDE ARE NOT OBLIGATORILY LINKED, Journal of Biological Chemistry, vol.275, issue.22, pp.16871-1687, 2000.
DOI : 10.1074/jbc.275.22.16871

K. Gast, D. Zirwer, M. Muller-frohne, and G. Damaschun, Compactness of the kinetic molten globule of bovine alpha-lactalbumin: a dynamic light scattering study, Protein Sci, vol.7, 1998.

A. M. Gray and A. J. Mason, Requirement for activin A and transforming growth factor--beta 1 pro-regions in homodimer assembly, Science, vol.247, issue.4948, pp.1328-1330, 1990.
DOI : 10.1126/science.2315700

N. J. Green®eld, Methods to Estimate the Conformation of Proteins and Polypeptides from Circular Dichroism Data, Analytical Biochemistry, vol.235, issue.1, pp.1-10, 1996.
DOI : 10.1006/abio.1996.0084

Z. Hu, K. Hagjhoo, and F. Jordan, Further evidence for the structure of the subtilisin propeptide and for its interactions with mature subtilisin, J. Biol. Chem, vol.271, pp.13375-3384, 1996.

H. Ikemura and M. Inouye, In vitro processing of pro-subtilisin produced in Escherichia coli, J. Biol. Chem, vol.263, pp.12959-12963, 1988.

H. Ikemura, H. Takagi, and M. Inouye, Requirement of pro-sequence for the production of active subtilisin E in Escherichia coli, J. Biol. Chem, vol.262, pp.7859-7864, 1987.

M. Inouye, Intramolecular chaperone; the role of the pro-peptide in protein folding, Enzyme, vol.45, pp.314-321, 1991.

M. V. Jagannadham and D. Balasubramanian, The molten globular intermediate form in the folding pathway of human carbonic anhydrase B, FEBS Letters, vol.21, issue.2, pp.326-330, 1985.
DOI : 10.1016/0014-5793(85)80396-3

S. Jain, U. P. Shinde, Y. Li, M. Inouye, and H. Berman, The crystal structure of an autoprocessed Ser221Cys-subtilisin E-propeptide complex at 2.0 ?? resolution, Journal of Molecular Biology, vol.284, issue.1, pp.137-144, 1998.
DOI : 10.1006/jmbi.1998.2161

D. Kim, Y. Lee, and H. Matsuzawa, Role of the COOH-terminal pro-sequence of aqualysin I (a heat-stable serine protease) in its extracellular secretion by Thermus thermophilus, FEMS Microbiology Letters, vol.157, issue.1, pp.39-45, 1997.
DOI : 10.1111/j.1574-6968.1997.tb12750.x

S. Kojima, T. Minagawa, and K. Miura, Tertiary structure formation in the propeptide of subtilisin BPN??? by successive amino acid replacements and its close relation to function, Journal of Molecular Biology, vol.277, issue.5, pp.1007-1013, 1998.
DOI : 10.1006/jmbi.1998.1671

K. Kuwajima, The molten globule state of a-lactalbumin, FASEB J, vol.10, pp.102-109, 1996.

Y. Lee, Y. Miyata, I. Terada, T. Ohta, and H. Matsuzawa, Involvement of NH2-terminal prosequence in the production of active aqualysin I (a thermophilic serine protease, 1991.

Y. Li, Z. Hu, F. Jordan, and M. Inouye, Functional analysis of the propeptide of subtilisin E as an intramolecular chaperone for protein folding; puri®cation and characterization of mutant propeptides, 1995.

M. C. Manning and R. W. Woody, Theoretical study of the contribution of aromatic side chains to the circular dichroism of basic bovine pancreatic trypsin inhibitor, Biochemistry, vol.28, issue.21, pp.8609-8613, 1989.
DOI : 10.1021/bi00447a051

C. Marie-claire, E. Ruffet, A. Beaumont, and B. P. Roques, The prosequence of thermolysin acts as an intramolecular chaperone when expressed in trans with the mature sequence in Escherichia coli, 1999.
URL : https://hal.archives-ouvertes.fr/inserm-00171255

H. Matsuzawa, D. Kim, and Y. Lee, Amino and carboxy terminal pro-sequences required for folding and extracellular secretion of aqualysin I, respectively, Intramolecular Chaperones and Protein Folding, pp.145-156, 1995.

H. Matsuzawa, K. Tokugawa, M. Hamaoki, M. Mizoguchi, H. Taguchi et al., Purification and characterization of aqualysin I (a thermophilic alkaline serine protease) produced by Thermus aquaticus YT-1, European Journal of Biochemistry, vol.36, issue.3, pp.441-447, 1988.
DOI : 10.1016/0003-9861(59)90090-6

Y. Ohta, H. Hojo, S. Aimoto, T. Kobayashi, X. Zhu et al., Pro-peptide as an intramolecular chaperone: renaturation of denatured subtilisin E with a synthetic pro-peptide, 1991.

J. Olmos, R. De-anda, E. Ferrari, F. Bolivar, and F. Valle, Effects of the sinR and degU32 (Hy) mutations on the regulation of the aprE gene in Bacillus subtilis, Molecular and General Genetics MGG, vol.253, issue.5, pp.562-567, 1997.
DOI : 10.1007/s004380050358

X. L. Qi, C. Holt, D. Mcnulty, D. T. Clarke, S. Brownlow et al., -lactoglobulin at pH??6.7, as determined by CD and IR spectroscopy: a test of the molten globule hypothesis, Biochemical Journal, vol.324, issue.1, pp.341-346, 1997.
DOI : 10.1042/bj3240341

URL : https://hal.archives-ouvertes.fr/in2p3-00025581

C. Red®eld, B. A. Schulman, M. A. Milhollen, P. S. Kim, and C. M. Dobson, Alpha-lactalbumin forms a compact molten globule in the absence of disul®de bonds, Nature Structural Biology, vol.6, issue.10, pp.948-952, 1999.
DOI : 10.1038/13318

S. W. Rogers and M. C. Rechsteiner, Microinjection studies on selective protein degradation: relationships between stability, structure, and location, Biomedica Biochimica Acta, vol.45, pp.1611-1618, 1986.

G. Semisotnov, N. Rodionova, J. Blank, and O. B. Ptitsyn, Sequential mechanism of refolding of carbonic anhydrase B, FEBS Letters, vol.37, issue.1, pp.9-13, 1987.
DOI : 10.1016/0014-5793(87)80412-X

U. P. Shinde and M. Inouye, Intramolecular chaperones and protein folding, Trends in Biochemical Sciences, vol.18, issue.11, pp.442-446, 1993.
DOI : 10.1016/0968-0004(93)90146-E

U. P. Shinde and M. Inouye, The Structural and Functional Organization of Intramolecular Chaperones: The N-Terminal Propeptides Which Mediate Protein Folding1, The Journal of Biochemistry, vol.115, issue.4, pp.629-636, 1994.
DOI : 10.1093/oxfordjournals.jbchem.a124386

U. P. Shinde and M. Inouye, Folding pathway mediated by an intramolecular chaperone., Proceedings of the National Academy of Sciences, vol.90, issue.15, pp.25-30, 1995.
DOI : 10.1073/pnas.90.15.6924

URL : https://hal.archives-ouvertes.fr/inserm-00171014

U. P. Shinde and M. Inouye, Folding Mediated by an Intramolecular Chaperone: Autoprocessing Pathway of the Precursor Resolvedviaa Substrate Assisted Catalysis Mechanism, Journal of Molecular Biology, vol.247, issue.3, pp.390-395, 1995.
DOI : 10.1006/jmbi.1994.0147

U. P. Shinde and M. Inouye, Intramolecular chaperones: polypeptide extensions that modulate protein folding, Seminars in Cell & Developmental Biology, vol.11, issue.1, pp.35-44, 2000.
DOI : 10.1006/scdb.1999.0349

U. P. Shinde, X. Fu, and M. Inouye, A Pathway for Conformational Diversity in Proteins Mediated by Intramolecular Chaperones, Journal of Biological Chemistry, vol.274, issue.22, pp.15615-15621, 1999.
DOI : 10.1074/jbc.274.22.15615

U. P. Shinde, Y. Li, S. Chatterjee, and M. Inouye, Folding pathway mediated by an intramolecular chaperone., Proc. Natl Acad. Sci. USA, pp.6924-6928, 1993.
DOI : 10.1073/pnas.90.15.6924

URL : https://hal.archives-ouvertes.fr/inserm-00171014

U. P. Shinde, J. J. Liu, and M. Inouye, Erratum: Protein memory through altered folding mediated by intramolecular chaperones, Nature, vol.389, issue.6672, pp.520-522, 1997.
DOI : 10.1038/32469

U. P. Shinde, J. Liu, and M. Inouye, Protein folding mediated by intramolecular chaperones, Molecular Chaperones in the Life Cycle of Proteins, pp.467-490, 1998.

M. Shopova and N. Genov, Protonated form of histidine 238 quenches the fluorescence of tryptophan 241 in subtilisin Novo, International Journal of Peptide and Protein Research, vol.73, issue.5, pp.475-478, 1983.
DOI : 10.1111/j.1399-3011.1983.tb02674.x

R. J. Siezen, J. A. Leunissen, and U. P. Shinde, Homology analysis of the propeptides of subtilisinlike serine proteases (Subtilases), Intramolecular Chaperones and Protein Folding, pp.233-256, 1995.

J. L. Silen and D. A. Agard, The alpha-lytic protease pro-region does not require a physical linkage to activate the protease domain in vivo, Nature, vol.341, pp.362-264, 1989.

S. M. Smith and M. M. Gottesman, Activity and deletion analysis of recombinant human cathepsin L expressed in Escherichia coli, J. Biol. Chem, vol.264, pp.20487-20495, 1989.

. Tyrosine, phenylalanine, and disul®de contributions to the circular dichroism of proteins: circular dichroism spectra of wild-type and mutant bovine pancreatic trypsin inhibitor, Biochemistry, vol.38, pp.10814-10822

S. Strausberg, P. Alexander, L. Wang, F. Schwarz, and P. Bryan, Catalysis of a protein folding reaction: Thermodynamic and kinetic analysis of subtilisin BPN' interactions with its propeptide fragment, Biochemistry, vol.32, issue.32, pp.8112-8119, 1993.
DOI : 10.1021/bi00083a009

U. Suter, C. Angst, C. L. Tien, C. C. Drinkwater, R. M. Lindsay et al., NGF/ BDNF chimeric proteins: analysis of neurotrophin speci®city by homolog-scanning mutagenesis, 1992.

I. Terada, S. Kwon, Y. Miyata, H. Matsuzawa, and T. Ohta, Unique precursor structure of an extracellular protease, aqualysin I, with NH 2 and COOH-terminal pro-sequences and its processing in Escherichia coli, J. Biol. Chem, vol.265, pp.6576-6581, 1990.

V. M. Uversky, G. V. Semisotnov, R. H. Pain, and O. B. Ptitsyn, ???All-or-none??? mechanism of the molten globule unfolding, FEBS Letters, vol.155, issue.1, pp.89-92, 1992.
DOI : 10.1016/0014-5793(92)81468-2

L. Wang, S. Ruvinov, S. Strausberg, D. T. Gallagher, G. Gilliland et al., Prodomain Mutations at the Subtilisin Interface: Correlation of Binding Energy and the Rate of Catalyzed Folding, Biochemistry, vol.34, issue.47, pp.15415-15420, 1995.
DOI : 10.1021/bi00047a004

J. S. Weissman and P. S. Kim, The pro region of BPTI facilitates folding, Cell, vol.71, issue.5, pp.841-851, 1992.
DOI : 10.1016/0092-8674(92)90559-U

S. L. Wong and R. H. Doi, Determination of the signal peptidase cleavage site in the preprosubtilisin of Bacillus subtilis, J. Biol. Chem, vol.261, pp.10176-10181, 1986.

X. Zhu, Y. Ohta, F. Jordan, and M. Inouye, Pro-sequence of subtilisin can guide the refolding of denatured subtilisin in an intermolecular process, Nature, vol.339, issue.6224, pp.483-484, 1989.
DOI : 10.1038/339483a0