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Year Number of Results
1923 1
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1929 2
1932 1
1935 1
1936 3
1937 1
1938 1
1941 1
1942 2
1943 1
1944 1
1945 10
1946 32
1947 47
1948 49
1949 51
1950 114
1951 142
1952 140
1953 111
1954 130
1955 106
1956 113
1957 94
1958 63
1959 80
1960 89
1961 82
1962 116
1963 179
1964 254
1965 229
1966 277
1967 277
1968 322
1969 349
1970 379
1971 462
1972 568
1973 649
1974 661
1975 633
1976 661
1977 609
1978 566
1979 569
1980 614
1981 638
1982 707
1983 784
1984 853
1985 947
1986 942
1987 1010
1988 1048
1989 1132
1990 1117
1991 1181
1992 1336
1993 1250
1994 1407
1995 1431
1996 1538
1997 1461
1998 1480
1999 1504
2000 1625
2001 1702
2002 1712
2003 1793
2004 2010
2005 1968
2006 2184
2007 2153
2008 2200
2009 2186
2010 2339
2011 2468
2012 2590
2013 2773
2014 2677
2015 2887
2016 2966
2017 3023
2018 3185
2019 3351
2020 3447
2021 3287
2022 3302
2023 3232
2024 1203

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87,022 results

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The following term was not found in PubMed: sec-dibutyl
Page 1
Poly(disulfide)s: From Synthesis to Drug Delivery.
Zhang R, Nie T, Fang Y, Huang H, Wu J. Zhang R, et al. Biomacromolecules. 2022 Jan 10;23(1):1-19. doi: 10.1021/acs.biomac.1c01210. Epub 2021 Dec 7. Biomacromolecules. 2022. PMID: 34874705 Review.
Bioresponsive polymers have been widely used in drug delivery because of their degradability. For example, poly(disulfide)s with repeating disulfide bonds in the main chain have attracted considerable research attention. ...This review introduces the synthesis metho …
Bioresponsive polymers have been widely used in drug delivery because of their degradability. For example, poly(disulfide)s with repe …
Thiol-disulfide exchange in signaling: disulfide bonds as a switch.
Messens J, Collet JF. Messens J, et al. Antioxid Redox Signal. 2013 May 1;18(13):1594-6. doi: 10.1089/ars.2012.5156. Epub 2013 Feb 25. Antioxid Redox Signal. 2013. PMID: 23330837
The major function of disulfide bonds is not only the stabilization of protein structures. ...It is now clear that disulfide bonds play a pivotal role in cellular reduction and oxidation processes. ...
The major function of disulfide bonds is not only the stabilization of protein structures. ...It is now clear that disulfide b …
How proteins form disulfide bonds.
Depuydt M, Messens J, Collet JF. Depuydt M, et al. Antioxid Redox Signal. 2011 Jul 1;15(1):49-66. doi: 10.1089/ars.2010.3575. Epub 2011 Mar 31. Antioxid Redox Signal. 2011. PMID: 20849374 Review.
The identification of protein disulfide isomerase, almost 50 years ago, opened the way to the study of oxidative protein folding. Oxidative protein folding refers to the composite process by which a protein recovers both its native structure and its native disulfide …
The identification of protein disulfide isomerase, almost 50 years ago, opened the way to the study of oxidative protein folding. Oxi …
Cellular disulfide bond formation in bioactive peptides and proteins.
Patil NA, Tailhades J, Hughes RA, Separovic F, Wade JD, Hossain MA. Patil NA, et al. Int J Mol Sci. 2015 Jan 14;16(1):1791-805. doi: 10.3390/ijms16011791. Int J Mol Sci. 2015. PMID: 25594871 Free PMC article. Review.
A systematic network of enzymes--a disulfide bond generating enzyme, a disulfide bond donor enzyme and a redox cofactor--that function inside the cell dictates the formation and maintenance of disulfide bonds. ...This review summarizes the formation of dis …
A systematic network of enzymes--a disulfide bond generating enzyme, a disulfide bond donor enzyme and a redox cofactor--that …
Disulfide bonding in protein biophysics.
Fass D. Fass D. Annu Rev Biophys. 2012;41:63-79. doi: 10.1146/annurev-biophys-050511-102321. Epub 2011 Dec 20. Annu Rev Biophys. 2012. PMID: 22224600 Review.
In addition to the classic mechanisms by which disulfide bonds enhance protein thermodynamic stability, disulfides in certain configurations contribute particular mechanical properties to proteins that sense and respond to tensile forces. ...Disulfides can al …
In addition to the classic mechanisms by which disulfide bonds enhance protein thermodynamic stability, disulfides in certain …
Quantification of thiols and disulfides.
Winther JR, Thorpe C. Winther JR, et al. Biochim Biophys Acta. 2014 Feb;1840(2):838-46. doi: 10.1016/j.bbagen.2013.03.031. Epub 2013 Apr 6. Biochim Biophys Acta. 2014. PMID: 23567800 Free PMC article. Review.
Dissecting the extent of oxidation and reduction of disulfides is an ongoing challenge due, in part, to the facility of thiol/disulfide exchange reactions. ...GENERAL SIGNIFICANCE: Many unresolved questions in the metabolic interconversion of thiols and disulfide …
Dissecting the extent of oxidation and reduction of disulfides is an ongoing challenge due, in part, to the facility of thiol/disu …
Disulfide Bonds: A Key Modification in Bacterial Extracytoplasmic Proteins.
Lee SF, Davey L. Lee SF, et al. J Dent Res. 2017 Dec;96(13):1465-1473. doi: 10.1177/0022034517725059. Epub 2017 Aug 10. J Dent Res. 2017. PMID: 28797211 Review.
In Actinomyces oris, disulfide bond formation is needed for pilus assembly, coaggregation, and biofilm formation. ...In conclusion, disulfide bond formation in oral bacteria is an emerging field, and the ability to form disulfide bonds plays an important role …
In Actinomyces oris, disulfide bond formation is needed for pilus assembly, coaggregation, and biofilm formation. ...In conclusion, …
The Formation of Native Disulfide Bonds: Treading a Fine Line in Protein Folding.
Narayan M. Narayan M. Protein J. 2021 Apr;40(2):134-139. doi: 10.1007/s10930-021-09976-7. Epub 2021 Mar 25. Protein J. 2021. PMID: 33765253 Review.
While the presence of disulfide bonds significantly increases the complexity of the folding landscape, it is generally recognized that native disulfide bonds help funnel the trajectory towards the final folded form. Here, we review the role of disulfide bonds …
While the presence of disulfide bonds significantly increases the complexity of the folding landscape, it is generally recognized tha …
Allosteric disulfide bonds.
Schmidt B, Ho L, Hogg PJ. Schmidt B, et al. Biochemistry. 2006 Jun 20;45(24):7429-33. doi: 10.1021/bi0603064. Biochemistry. 2006. PMID: 16768438
These bonds can be thought of as allosteric disulfides. To better define the properties of allosteric disulfides, we have analyzed the geometry and dihedral strain of 6874 unique disulfide bonds in 2776 X-ray structures. ...We suggest that the -RHStaple confi …
These bonds can be thought of as allosteric disulfides. To better define the properties of allosteric disulfides, we have anal …
DIsulfide Mapping PLanner Software Tool.
Kist AM, Lampert A, O'Reilly AO. Kist AM, et al. J Comput Biol. 2018 Apr;25(4):430-434. doi: 10.1089/cmb.2017.0129. Epub 2017 Aug 17. J Comput Biol. 2018. PMID: 28817312
Disulfide bridges are side-chain-mediated covalent bonds between cysteines that stabilize many protein structures. Disulfide mapping experiments to resolve these linkages typically involve proteolytic cleavage of the protein of interest followed by mass spectroscopy …
Disulfide bridges are side-chain-mediated covalent bonds between cysteines that stabilize many protein structures. Disulfide m …
87,022 results
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