Matsusaki M, Okada R, Tanikawa Y, Kanemura S, Ito D, Lin Y
Biology (Basel). 2021; 10(11).
PMID: 34827105
PMC: 8615271.
DOI: 10.3390/biology10111112.
Butera D, Hogg P
Nat Commun. 2020; 11(1):5468.
PMID: 33122656
PMC: 7596563.
DOI: 10.1038/s41467-020-19295-7.
Matsusaki M, Okuda A, Matsuo K, Gekko K, Masuda T, Naruo Y
J Biol Chem. 2019; 294(49):18820-18835.
PMID: 31685660
PMC: 6901294.
DOI: 10.1074/jbc.RA119.010917.
Chiu J, Hogg P
J Biol Chem. 2019; 294(8):2949-2960.
PMID: 30635401
PMC: 6393624.
DOI: 10.1074/jbc.REV118.005604.
Matsusaki M, Okuda A, Masuda T, Koishihara K, Mita R, Iwasaki K
Plant Physiol. 2015; 170(2):774-89.
PMID: 26645455
PMC: 4734590.
DOI: 10.1104/pp.15.01781.
Expression and characterization of protein disulfide isomerase family proteins in bread wheat.
Kimura S, Higashino Y, Kitao Y, Masuda T, Urade R
BMC Plant Biol. 2015; 15:73.
PMID: 25849633
PMC: 4355359.
DOI: 10.1186/s12870-015-0460-2.
Cysteine sulfenic acid as an intermediate in disulfide bond formation and nonenzymatic protein folding.
Rehder D, Borges C
Biochemistry. 2010; 49(35):7748-55.
PMID: 20712299
PMC: 2945302.
DOI: 10.1021/bi1008694.
Block of sodium channels by divalent mercury: role of specific cysteinyl residues in the P-loop region.
Hisatome I, Kurata Y, Sasaki N, Morisaki T, Morisaki H, Tanaka Y
Biophys J. 2000; 79(3):1336-45.
PMID: 10968996
PMC: 1301028.
DOI: 10.1016/S0006-3495(00)76386-7.
Probing protein folding and stability using disulfide bonds.
Darby N, Creighton T
Mol Biotechnol. 1997; 7(1):57-77.
PMID: 9163722
DOI: 10.1007/BF02821544.
Expression of wild-type and mutant bovine pancreatic ribonuclease A in Escherichia coli.
Laity J, Shimotakahara S, Scheraga H
Proc Natl Acad Sci U S A. 1993; 90(2):615-9.
PMID: 8421696
PMC: 45714.
DOI: 10.1073/pnas.90.2.615.
Separation of intermediates in the refolding of reduced erabutoxin b by analytical isoelectric focusing in layers of polyacrylamide gel.
Bouet F, Menez A, Hider R, FROMAGEOT P
Biochem J. 1982; 201(3):495-9.
PMID: 7092808
PMC: 1163674.
DOI: 10.1042/bj2010495.
Implication of the structure and stability of disulfide intermediates of lysozyme on the mechanism of renaturation.
Acharya A, Taniuchi H
Mol Cell Biochem. 1982; 44(3):129-48.
PMID: 7050652
DOI: 10.1007/BF00238502.
The problem of the stability globular proteins.
Pfeil W
Mol Cell Biochem. 1981; 40(1):3-28.
PMID: 7031463
DOI: 10.1007/BF00230185.
Toward an understanding of the folding of ribonuclease A.
Scheraga H, Konishi Y, Rothwarf D, Mui P
Proc Natl Acad Sci U S A. 1987; 84(16):5740-4.
PMID: 3475701
PMC: 298938.
DOI: 10.1073/pnas.84.16.5740.
Thioredoxin-catalyzed refolding of disulfide-containing proteins.
Pigiet V, Schuster B
Proc Natl Acad Sci U S A. 1986; 83(20):7643-7.
PMID: 3463991
PMC: 386777.
DOI: 10.1073/pnas.83.20.7643.
Local interactions favor the native 8-residue disulfide loop in the oxidation of a fragment corresponding to the sequence Ser-50-Met-79 derived from bovine pancreatic ribonuclease A.
Milburn P, Scheraga H
J Protein Chem. 1988; 7(4):377-98.
PMID: 3255371
DOI: 10.1007/BF01024887.
Toward a better understanding of protein folding pathways.
Creighton T
Proc Natl Acad Sci U S A. 1988; 85(14):5082-6.
PMID: 2455892
PMC: 281692.
DOI: 10.1073/pnas.85.14.5082.
Redox properties and cross-linking of the dithiol/disulphide active sites of mammalian protein disulphide-isomerase.
HAWKINS H, De Nardi M, Freedman R
Biochem J. 1991; 275 ( Pt 2):341-8.
PMID: 2025221
PMC: 1150058.
DOI: 10.1042/bj2750341.
