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Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli.
Zapun A, Missiakas D, Raina S, Creighton TE. Zapun A, et al. Biochemistry. 1995 Apr 18;34(15):5075-89. doi: 10.1021/bi00015a019. Biochemistry. 1995. PMID: 7536035
DsbC is a soluble protein of the bacterial periplasm that was identified genetically as being involved in protein disulfide formation. ...Gel filtration and subunit hybridization indicate that DsbC is a stable dimer of identical subunits. Each subunit has a - …
DsbC is a soluble protein of the bacterial periplasm that was identified genetically as being involved in protein disulfide formation …
The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo.
Zapun A, Bardwell JC, Creighton TE. Zapun A, et al. Biochemistry. 1993 May 18;32(19):5083-92. doi: 10.1021/bi00070a016. Biochemistry. 1993. PMID: 8494885
It has only two cysteine residues that are separated in the sequence by two other residues and are shown to form a disulfide bond reversibly. ...These properties indicate that disulfide-bonded DsbA is a potent oxidant and ideally suited for generating protein disulf …
It has only two cysteine residues that are separated in the sequence by two other residues and are shown to form a disulfide bond rev …
Replacement of the active-site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo.
Zapun A, Cooper L, Creighton TE. Zapun A, et al. Biochemistry. 1994 Feb 22;33(7):1907-14. doi: 10.1021/bi00173a038. Biochemistry. 1994. PMID: 8110795
DsbA is a periplasmic protein of Escherichia coli that was identified genetically as being involved in the formation of disulfide bonds in secreted proteins. ...Even though the thiol group of Cys30 is exposed and reactive, it formed a very unstable mixed disulfide w …
DsbA is a periplasmic protein of Escherichia coli that was identified genetically as being involved in the formation of disulfide bon …
Mechanisms and catalysts of disulfide bond formation in proteins.
Creighton TE, Zapun A, Darby NJ. Creighton TE, et al. Among authors: zapun a. Trends Biotechnol. 1995 Jan;13(1):18-23. doi: 10.1016/s0167-7799(00)88896-4. Trends Biotechnol. 1995. PMID: 7765801 Review.
Folding in vitro of bovine pancreatic trypsin inhibitor in the presence of proteins of the endoplasmic reticulum.
Zapun A, Creighton TE, Rowling PJ, Freedman RB. Zapun A, et al. Proteins. 1992 Sep;14(1):10-5. doi: 10.1002/prot.340140104. Proteins. 1992. PMID: 1384031
Effects of DsbA on the disulfide folding of bovine pancreatic trypsin inhibitor and alpha-lactalbumin.
Zapun A, Creighton TE. Zapun A, et al. Biochemistry. 1994 May 3;33(17):5202-11. doi: 10.1021/bi00183a025. Biochemistry. 1994. PMID: 7513556
DsbA is a protein found in the periplasm of Escherichia coli that is required for the formation of disulfide bonds in secreted proteins. ...Disulfide-bonded DsbA in stoichiometric amounts proved to be a very potent donor of disulfide bonds to reduced BPTI but showed …
DsbA is a protein found in the periplasm of Escherichia coli that is required for the formation of disulfide bonds in secreted protei …
Crystallization of DsbC, the disulfide bond isomerase of Escherichia coli.
Rybin V, Zapun A, Törrönen A, Raina S, Missiakas D, Creighton TE, Metcalf P. Rybin V, et al. Among authors: zapun a. Acta Crystallogr D Biol Crystallogr. 1996 Nov 1;52(Pt 6):1219-21. doi: 10.1107/S0907444996008967. Acta Crystallogr D Biol Crystallogr. 1996. PMID: 15299592
DsbC is a 2 x 23 kDa soluble dimeric protein molecule involved in protein disulfide bond formation in the E. coli periplasm, primarily catalyzing disulfide bond rearrangements. ...Cell dimensions obtained for frozen crystals were in the range a = 58.8 (0.3), b = 78. …
DsbC is a 2 x 23 kDa soluble dimeric protein molecule involved in protein disulfide bond formation in the E. coli periplasm, primaril …
Protein folding in a specialized compartment: the endoplasmic reticulum.
Zapun A, Jakob CA, Thomas DY, Bergeron JJ. Zapun A, et al. Structure. 1999 Aug 15;7(8):R173-82. doi: 10.1016/s0969-2126(99)80112-9. Structure. 1999. PMID: 10467145 Review.
Automated high-throughput process for site-directed mutagenesis, production, purification, and kinetic characterization of enzymes.
Carapito R, Gallet B, Zapun A, Vernet T. Carapito R, et al. Among authors: zapun a. Anal Biochem. 2006 Aug 1;355(1):110-6. doi: 10.1016/j.ab.2006.04.047. Epub 2006 May 19. Anal Biochem. 2006. PMID: 16797473
To address the need for convenient parallel production of numerous point mutants of a protein, we developed an automated method to perform classical site-directed mutagenesis, protein purification, and characterization in a high-throughput manner. ...Moreover, seven …
To address the need for convenient parallel production of numerous point mutants of a protein, we developed an automated method to pe …
Identification and crystallization of a protease-resistant core of calnexin that retains biological activity.
Hahn M, Borisova S, Schrag JD, Tessier DC, Zapun A, Tom R, Kamen AA, Bergeron JJ, Thomas DY, Cygler M. Hahn M, et al. Among authors: zapun a. J Struct Biol. 1998 Nov;123(3):260-4. doi: 10.1006/jsbi.1998.4032. J Struct Biol. 1998. PMID: 9878580
A truncated gene was cloned accordingly. Its product, cnxDeltaN25C15, was purified to apparent homogeneity and crystallized. ...A heavy atom derivative was identified....
A truncated gene was cloned accordingly. Its product, cnxDeltaN25C15, was purified to apparent homogeneity and crystallized. ...A
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