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Pro-sequence of subtilisin can guide the refolding of denatured subtilisin in an intermolecular process.
Abstract
Subtilisin E, an alkaline serine protease consisting of a single polypeptide chain of 275 amino acids is produced from a pre-pro-protein. The pre-sequence functions as the signal peptide for protein secretion across the membrane. Deletion of the pro-sequence yields mature but inactive subtilisin: the 77-amino acid pro-sequence must precede the mature subtilisin to guide the latter into an active conformation. Pro-subtilisin denatured in 6 M guanidine-HCl can be self-processed to the active enzyme intramolecularly, with concomitant cleavage of the pro-sequence, when dialysed against renaturing buffer. We have constructed an active-centre mutant of pro-subtilisin (Asp 32----Asn) which is not processed to active enzyme, unlike the wild-type pro-subtilisin, because intramolecular processing is prevented. Here we report an intermolecular pathway for the refolding of the inactive mature protein to an active enzyme in vitro with the aid of exogenously added pro-sequence. We establish conditions under which the mature inactive form, as well as acid-denatured subtilisins Carlsberg and BPN', can be renatured by the mutant pro-subtilisin.
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“The pro-peptide of subtilisin is a catalyst for correct folding of the active enzyme (Zhu et al., 1989).”
From Modeled Structure of the Cell Envelope Proteinase of Lactococcus lactis (2020) · cites this paper as Zhu et al., 1989
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Cites
Kim, P. S., & Baldwin, R. L. (1982) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.51.070182.002331 · Cited by 1,036
Cloning, sequencing, and secretion of Bacillusamyloliquefacienssubtillisin inBacillus subtilis
Wells, J. A., Ferrari, E., Henner, D. J., Estell, D. A., & Chen, E. Y. (1983) · Nucleic Acids Research · doi:10.1093/nar/11.22.7911 · Cited by 350
Requirement of pro-sequence for the production of active subtilisin E in Escherichia coli.
Ikemura, H., Takagi, H., & Inouye, M. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47646-6 · Cited by 333
Self-citationStahl, M., & Ferrari, E. (1984) · Journal of Bacteriology · doi:10.1128/jb.158.2.411-418.1984 · Cited by 304
Cloning, sequencing and expression of subtilisin Carlsberg fromBacillus licheniformis
Jacobs, M. F., Eliasson, M., Uhlén, M., & Flock, J. (1985) · Nucleic Acids Research · doi:10.1093/nar/13.24.8913 · Cited by 203
In vitro processing of pro-subtilisin produced in Escherichia coli.
Ikemura, H., & Inouye, M. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)37656-7 · Cited by 141
Self-citationGenetic Studies Of Protein Stability And Mechanisms Of Folding
Goldenberg, D. P. (1988) · Annual Review of Biophysics and Biophysical Chemistry · doi:10.1146/annurev.bb.17.060188.002405 · Cited by 99
Determination of the signal peptidase cleavage site in the preprosubtilisin of Bacillus subtilis.
Wong, S. L., & Doi, R. H. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)67507-6 · Cited by 81
Zabin, I., & Villarejo, M. R. (1975) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.44.070175.001455 · Cited by 68
Production of two proteolytic enzymes by a transformable strain of Bacillus subtilis
Boyer, H. W., & Carlton, B. C. (1968) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(68)90050-7 · Cited by 59
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Regulation of bacterial protease activity
Władyka, B., & Pustelny, K. (2007) · Cellular & Molecular Biology Letters · doi:10.2478/s11658-007-0048-4 · Cited by 27
Powner, D., & Davey, J. F. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.1.400 · Cited by 27
Protein engineering on subtilisin
Takagi, H. (1993) · International Journal of Biochemistry · doi:10.1016/0020-711x(93)90617-n · Cited by 27
Taguchi, S., Odaka, A., Watanabe, Y., & Momose, H. (1995) · Applied and Environmental Microbiology · doi:10.1128/aem.61.1.180-186.1995 · Cited by 26
Soerensen, P., Winther, J. R., Kaarsholm, N. C., & Poulsen, F. M. (1993) · Biochemistry · doi:10.1021/bi00096a028 · Cited by 26
Kaulmann, G., Palm, G. J., Schilling, K., Hilgenfeld, R., & Wiederanders, B. (2006) · Protein Science · doi:10.1110/ps.062401806 · Cited by 25
Functional analysis of the propeptides of subtilisin E and aqualysin I as intramolecular chaperones
Takagi, H., Koga, M., Katsurada, S., Yabuta, Y., Shinde, U. P., Inouye, M., & Nakamori, S. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)03053-8 · Cited by 25
Self-citationThe protease genes of Bacillus subtilis
He, X.-S., Brückner, R., & Doi, R. H. (1991) · Research in Microbiology · doi:10.1016/0923-2508(91)90058-i · Cited by 25
2 Protein Folding and its Implications for the Production of Recombinant Proteins
Hlodan, R., Craig, S., & Pain, R. H. (1991) · Biotechnology and Genetic Engineering Reviews · doi:10.1080/02648725.1991.10647877 · Cited by 25
Identification of the Interactions Critical for Propeptide-Catalyzed Folding of Tk-Subtilisin
Tanaka, S., Matsumura, H., Koga, Y., Takano, K., & Kanaya, S. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.09.028 · Cited by 24
Kim, D., Lee, Y.-C., & Matsuzawa, H. (1997) · FEMS Microbiology Letters · doi:10.1016/s0378-1097(97)00451-5 · Cited by 24
Extracellular autoprocessing of a metalloprotease from Streptomyces cacaoi.
Chang, P. C., & Lee, Y. W. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50618-4 · Cited by 24
In Vitro Refolding of Porcine Pepsin Immobilized on Agarose Beads
Kurimoto, E., Harada, T., Akiyama, A., Sakai, T., & Kato, K. (2001) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a002985 · Cited by 24
Lee, Y., Koike, H., Taguchi, H., Ohta, T., & Matsuzawa, H. (1994) · FEMS Microbiology Letters · doi:10.1016/0378-1097(94)00177-4 · Cited by 24
A rapid solubility-optimized screening procedure for recombinant subtilisins in E. coli
Bjerga, G. E. K., Arsın, H., Larsen, Ø., Puntervoll, P., & Kleivdal, H. (2016) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2016.02.009 · Cited by 23
Lesage, G., Prat, A., Lacombe, J., Thomas, D. Y., Seidah, N. G., & Boileau, G. (2000) · Molecular Biology of the Cell · doi:10.1091/mbc.11.6.1947 · Cited by 23
Okamoto, K., Nomura, T., Hamada, M., Fukuda, T., Noguchi, Y., & Fujii, Y. (2000) · Microbiology and Immunology · doi:10.1111/j.1348-0421.2000.tb02565.x · Cited by 22
Niu, W. L., Li, Z.-P., & Tan, T. (2005) · Molecular Biotechnology · doi:10.1385/mb:32:1:073 · Cited by 22
Substrate-induced activation of a trapped IMC-mediated protein folding intermediate.
Inouye, M., Fu, X., & Shinde, U. P. (2001) · Nature Structural Biology · doi:10.1038/86194 · Cited by 22
Self-citationProtein Transport Pathways inBacillus subtilis: a Genome-Based Road Map
van Dijl, J. M., Bolhuis, A., Tjalsma, H., Jongbloed, J. D. H., de Jong, A., & Bron, S. (2014) · ASM Press eBooks · doi:10.1128/9781555817992.ch24 · Cited by 22
Strausberg, S. L., Alexander, P., Wang, L., Gallagher, T., Gilliland, G. L., & Bryan, P. N. (1993) · Biochemistry · doi:10.1021/bi00090a012 · Cited by 22
Song, J., Xu, P., Xiang, H., Su, Z., Storer, A. C., & Ni, F. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01644-6 · Cited by 22
Nagle, G. T., Garcia, A. T., Knock, S. L., GORHAM, E. L., van Heumen, W. R. A., & Kurosky, A. (1995) · DNA and Cell Biology · doi:10.1089/dna.1995.14.145 · Cited by 22
Matsubara, M., Kurimoto, E., Kojima, S., Miura, K.-I., & Sakai, T. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)80499-0 · Cited by 22
The zymogen of plasmepsin V from Plasmodium falciparum is enzymatically active
Xiao, H., Bryksa, B. C., Bhaumik, P., Gustchina, A., Kiso, Y., Yao, S. Q., Wlodawer, A., & Yada, R. Y. (2014) · Molecular and Biochemical Parasitology · doi:10.1016/j.molbiopara.2014.10.004 · Cited by 21
Contran, N., Cerana, R., Crosti, P., & Malerba, M. (2007) · PROTOPLASMA · doi:10.1007/s00709-007-0250-2 · Cited by 21
Nagarajan, V. (2014) · ASM Press eBooks · doi:10.1128/9781555818388.ch49 · Cited by 21
Chaperone function: cracking the second half of the genetic code
Ellis, R. J. (1991) · The Plant Journal · doi:10.1111/j.1365-313x.1991.00009.x · Cited by 20
Rekik, H., Frikha, F., Jaouadi, N. Z., Gargouri, F., Jmal, N., Béjar, S., & Jaouadi, B. (2018) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2018.12.103 · Cited by 19
Egnell, P., & Flock, J. (1992) · Molecular Microbiology · doi:10.1111/j.1365-2958.1992.tb01549.x · Cited by 19
Ueda, K., Lipkind, G. M., Zhou, A., Zhu, X., Kuznetsov, A., Philipson, L. H., Gardner, P., Zhang, C., & Steiner, D. F. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0631617100 · Cited by 19
Self-citationStructure, Processing and Catalytic Action of Penicillin Acylase
Virden, R. (1990) · Biotechnology and Genetic Engineering Reviews · doi:10.1080/02648725.1990.10647869 · Cited by 19
Chang, A. K., Park, J. W., Lee, E. H., & Lee, J. S. (2007) · Journal of Bacteriology · doi:10.1128/jb.00396-07 · Cited by 18
Fukada, K., Inoue, T., & Shiraishi, H. (2006) · The Plant Cell · doi:10.1105/tpc.106.041343 · Cited by 18
Yu, C., Chen, Y., Su, S., Forouhar, F., Lee, S.-H., & Chow, L. (2002) · Biochemical Journal · doi:10.1042/bj3630707 · Cited by 18
Mansfeld, J., Petermann, E., Dürrschmidt, P., & Ulbrich‐Hofmann, R. (2004) · Protein Expression and Purification · doi:10.1016/j.pep.2004.10.008 · Cited by 18
Baier, K., Nicklisch, S., & Lockau, W. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.00750.x · Cited by 18
Short peptides assist the folding of free class I heavy chains in solution
Elliott, T. J., Cerundolo, V., & Townsend, A. (1992) · European Journal of Immunology · doi:10.1002/eji.1830221214 · Cited by 18
Brown, E. D., & Yada, R. Y. (1991) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(91)90484-h · Cited by 18
Eun, H. (1996) · Elsevier eBooks · doi:10.1016/b978-012243740-3/50004-1 · Cited by 19
Raval, V. H., Rawal, C. M., Pandey, S., Bhatt, H. B., Dahima, B. R., & Singh, S. P. (2014) · Annals of Microbiology · doi:10.1007/s13213-014-0869-0 · Cited by 17
Functional Properties of Pro Region of Escherichia coli Heat‐Stable Enterotoxin
Yamanaka, H., Fuke, Y., Hitotsubashi, S., Fujii, Y., & Okamoto, K. (1993) · Microbiology and Immunology · doi:10.1111/j.1348-0421.1993.tb03200.x · Cited by 17
Schu, P. V., & Wolf, D. H. (1991) · FEBS Letters · doi:10.1016/0014-5793(91)80558-k · Cited by 17
Gunne, H., & Steiner, H. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb17923.x · Cited by 17
Nagle, G. T., Garcia, A. T., GORHAM, E. L., Knock, S. L., van Heumen, W. R. A., Spijker, S., Smit, A. B., Geraerts, W. P. M., & Kurosky, A. (1995) · DNA and Cell Biology · doi:10.1089/dna.1995.14.431 · Cited by 17
Modeled Structure of the Cell Envelope Proteinase of Lactococcus lactis
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Pande, M., Kumari, N. K. P., Dubey, V. K., Tripathi, P., & Jagannadham, M. V. (2009) · Process Biochemistry · doi:10.1016/j.procbio.2009.04.016 · Cited by 16
Mechanism of Folding and Activation of Subtilisin Kexin Isozyme-1 (SKI-1)/Site-1 Protease (S1P)
da Palma, J. R., Cendron, L., Seidah, N. G., Pasquato, A., & Kunz, S. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.677757 · Cited by 14
Mains, R. E., Milgram, S. L., Keutmann, H. T., & Eipper, B. A. (1995) · Molecular Endocrinology · doi:10.1210/me.9.1.3 · Cited by 16
Wetmore, D. R., Wong, S., & Roche, R. S. (1994) · Molecular Microbiology · doi:10.1111/j.1365-2958.1994.tb01062.x · Cited by 16
Lange, C. M., & Rudolph, R. (2005) · Wiley eBooks · doi:10.1002/9783527619498.ch71 · Cited by 16
Renaturation of the mature subtilisin BPN' immobilized on agarose beads
Hayashi, T., Matsubara, M., Nohara, D., Kojima, S., Miura, K., & Sakai, T. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00744-6 · Cited by 16
Recombinant prosegment peptide acts as a folding catalyst and inhibitor of native pepsin
Dee, D. R., Filonowicz, S., Horimoto, Y., & Yada, R. Y. (2009) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.08.017 · Cited by 15
Structural basis of cucumisin protease activity regulation by its propeptide
Sotokawauchi, A., Kato-Murayama, M., Murayama, K., Hosaka, T., Maeda, I., Onjo, M., Ohsawa, N., Kato, D., Arima, K., & Shirouzu, M. (2016) · The Journal of Biochemistry · doi:10.1093/jb/mvw053 · Cited by 15
Pero, J. G., & Sloma, A. (2014) · ASM Press eBooks · doi:10.1128/9781555818388.ch63 · Cited by 15
O'Neil, H. S., Forster, B. M., Roberts, K. L., Chambers, A. J., Bitar, A. P., & Marquis, H. (2009) · Journal of Bacteriology · doi:10.1128/jb.01168-08 · Cited by 14
Jacob, R., Pürschel, B., & Naim, H. Y. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204116200 · Cited by 14
Collinson, L., Rangarajan, M., & Curtis, M. A. (1998) · Microbiology · doi:10.1099/00221287-144-9-2487 · Cited by 14
Chang, S.-C., Mei-Han, S. U., & Lee, Y. W. (1997) · Biochemical Journal · doi:10.1042/bj3210029 · Cited by 14
Tanksale, A. M., Ghatge, M. S., & DESHPANDE, V. V. (2002) · Protein Science · doi:10.1110/ps.0201802 · Cited by 14
Sun, D., Liu, Q., He, Y., Wang, C., Wu, F., Tian, C., & Zang, J. (2013) · Protein & Cell · doi:10.1007/s13238-013-3089-7 · Cited by 14
Kakeshita, H., Kageyama, Y., Ara, K., Ozaki, K., & Nakamura, K. (2010) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-010-2954-z · Cited by 13
Linden, H. M., & Kaushansky, K. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201297200 · Cited by 13
Sroga, G. E., & Dordick, J. S. (2001) · Protein Engineering Design and Selection · doi:10.1093/protein/14.11.929 · Cited by 13
Kim, D.-Y., Lee, J., Saraswat, V., & Park, Y. (2000) · Biotechnology and Bioengineering · doi:10.1002/1097-0290(20000820)69:4 · Cited by 13
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Kunugi, S., Yanagi, Y., Kitayaki, M., Tanaka, N., & Kunugi, Y. (1997) · Bulletin of the Chemical Society of Japan · doi:10.1246/bcsj.70.1459 · Cited by 13
Orlichenko, L. S., Stolz, D. B., Noel, P., Behari, J., Liu, S., & Singh, V. P. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.328815 · Cited by 12
Kim, D.-W., Lin, S.-J., Morita, S., Terada, I., & Matsuzawa, H. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1996.5899 · Cited by 12
Valenzuela, B., Solís-Cornejo, F., Araya, R., & Zamorano, P. L. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241914512 · Cited by 11
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Larsen, Ø., & Bjerga, G. E. K. (2018) · Microorganisms · doi:10.3390/microorganisms6020051 · Cited by 11
Chaudhuri, B., Latham, S. E., Helliwell, S. B., & Seeboth, P. G. (1992) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(92)91630-9 · Cited by 11
Prions and molecular chaperones
Liautard, J. (1993) · Archives of virology. Supplementum · doi:10.1007/978-3-7091-9300-6_18 · Cited by 11
Rosenthal, P. J. (1993) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/0167-4781(93)90250-h · Cited by 11
Martínez, M., Bouillon, A., Brûlé, S., Raynal, B. D. E., Haouz, A., Alzari, P. M., & Barale, J.-C. (2024) · mBio · doi:10.1128/mbio.00198-24 · Cited by 10
Falkenberg, F., Bott, M. H., Bongaerts, J., & Siegert, P. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.1017978 · Cited by 10
Some new aspects of molecular mechanisms of cyclosporin A effect on immune response
Zav'yalov, V. P., Denesyuk, A. I., Lundell, J., & Korpela, T. (1995) · Apmis · doi:10.1111/j.1699-0463.1995.tb01125.x · Cited by 10
Yonezawa, M., Suzuki, J., Nishiyama, M., Horinouchi, S., & Beppu, T. (1993) · Journal of Biotechnology · doi:10.1016/0168-1656(93)90127-9 · Cited by 10
Sakamoto, S., Terada, I., Lee, Y.-C., Uehara, K., Matsuzawa, H., & Iijima, M. (1996) · Applied Microbiology and Biotechnology · doi:10.1007/s002530050654 · Cited by 10
Nandana, V., Singh, S. K., Singh, A. N., & Dubey, V. K. (2014) · Protein Expression and Purification · doi:10.1016/j.pep.2014.08.003 · Cited by 9
Darnis, S., Juge, N., Marino‐Buslje, C., Avilés, F. X., PUIGSERVER, A. J., Chaix, J., & Guo, X. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00091.x · Cited by 9
Equilibrium and kinetic studies on reversible and irreversible denaturation of micrococcal nuclease
Nohara, D., Yamada, T., Watanabe, A., & Sakai, T. (1994) · Biotechnology and Bioengineering · doi:10.1002/bit.260440304 · Cited by 9
Structures and Functions of Precursors of Bacterial Proteases
Serkina, A. V., Shevelev, A. B., & Chestukhina, G. G. (2001) · Russian Journal of Bioorganic Chemistry · doi:10.1023/a:1012322813107 · Cited by 9
Nohara, D., Sakakibara, H., Kurimoto, E., Hayashi, T., & Sakai, T. (1996) · Journal of Fermentation and Bioengineering · doi:10.1016/0922-338x(96)88827-1 · Cited by 9
Kobayashi, H., Yoshida, T., Miyakawa, T., Tashiro, M., Okamoto, K., Yamanaka, H., Tanokura, M., & Tsuge, H. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.622852 · Cited by 8
Egnell, P., & Flock, J. (1991) · Gene · doi:10.1016/0378-1119(91)90008-y · Cited by 8
The role of tryptophan residues in the autoprocessing of prosubtilisin E
Sone, M., Falzon, L., & Inouye, M. (2005) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2005.01.011 · Cited by 8
Self-citationKitagawa, M., Ito, N., Matsumoto, Y., Saito, M., Tamura, T., Kusakabe, H., Inagaki, K., & Imada, K. (2021) · Journal of Structural Biology X · doi:10.1016/j.yjsbx.2021.100044 · Cited by 8
Gedi, V., Duarte, F., Patel, P., Bhattacharjee, P., Teçza, M., McGourty, K., & Hudson, S. P. (2023) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.3c00207 · Cited by 7
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Xiao, H., Dee, D. R., & Yada, R. Y. (2011) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2011.06.017 · Cited by 7
Determinants of Ascaris Hemoglobin Octamer Formation
Minning, D. M., & Goldberg, D. E. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.49.32644 · Cited by 7
Schaller, A. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-382219-2.00717-1 · Cited by 7
Araújo, R., Cavaco-Paulo, A. M., & Casal, M. (2008) · Engineering in Life Sciences · doi:10.1002/elsc.200700056 · Cited by 7
Self-Processing of Subunits of the Proteasome
Seemüller, E., Zwickl, P., & Baumeister, W. P. (2002) · The Enzymes · doi:10.1016/s1874-6047(02)80013-0 · Cited by 7
Quantitative in vitro Renaturation of Subtilisin BPN’ without the Aid of Pro-sequence
Matsubara, M., Kurimoto, E., Kojima, S., Miura, K., & Sakai, T. (1993) · Chemistry Letters · doi:10.1246/cl.1993.1783 · Cited by 7
Imamura, T., Murakami, Y., & Nitta, H. (2017) · Biological Chemistry · doi:10.1515/hsz-2016-0344 · Cited by 6
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Mutated Intramolecular Chaperones Generate High-Activity Isomers of Mature Enzymes
Nagayama, M., Maeda, H., Kuroda, K., & Ueda, M. (2012) · Biochemistry · doi:10.1021/bi3001159 · Cited by 6
Sinsereekul, N., Foophow, T., Yamanouchi, M., Koga, Y., Takano, K., & Kanaya, S. (2011) · FEBS Journal · doi:10.1111/j.1742-4658.2011.08107.x · Cited by 6
Improvement of Heterologous Protein Secretion by Bacillus subtilis
Kakeshita, H., Kageyama, Y., Ozaki, K., Nakamura, K., & Ar, K. (2012) · InTech eBooks · doi:10.5772/29256 · Cited by 6
Harmsen, M. M., Smits, C., & de Geus, B. (2002) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-002-1136-z · Cited by 6
Metadata
- Authors
- Zhu, X., Ohta, Y., Jordan, F., & Inouye, M.
- Affiliations
- Rutgers, The State University of New Jersey (US)
- Venue
- Nature
- Published
- 1989-06
- Volume
- 339
- Issue
- 6224
- Pages
- 483-484
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2045786862
- Cited by
- 344
- References
- 10
- Citations by year
- 2025: 2 · 2024: 2 · 2023: 4 · 2022: 3 · 2021: 2 · 2020: 4 · 2019: 2 · 2018: 3 · 2017: 3 · 2016: 3 · 2015: 5 · 2014: 8 · 2013: 4 · 2012: 10
- FWCI
- 8.12
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- subtilisin, protein refolding, protein denaturation, guanidine hydrochloride denaturation, serine protease activation, active site mutants, subtilisin Carlsberg, subtilisin BPN', renaturation
- MeSH terms
- Enzyme Activation, Enzyme Precursors, Escherichia coli, Genetic Vectors, Kinetics, Peptide Fragments, Plasmids, Protein Conformation, Protein Denaturation, Recombinant Proteins, Subtilisins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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