22 citations
,
November 2014 in “Proteins Structure Function and Bioinformatics” Cysteines in wool fibers are accessible and form important disulfide bonds.
39 citations
,
June 2012 in “Journal of Structural Biology” Disulfide bonds are crucial for hair structure during keratinization.
75 citations
,
March 2007 in “Journal of Biological Chemistry” QSOX enzymes help form protein bonds in cells, especially in tissues with high secretory activity.
53 citations
,
March 2006 in “Biopolymers” TTD hair is brittle due to fewer sulfur amino acids and unstable disulfide bonds.
March 2010 in “International Journal of Cosmetic Science” Disulfide bonds affect the melting behavior of hair's crystalline structure, but hair retains some stability even after these bonds are broken.
1 citations
,
January 2009 in “Journal of S C C J” Changing disulfide bonds in human hair affects its melting behavior and thermal stability.
May 2024 in “International Journal of Cosmetic Science” Disulfide bonds are crucial for hair's strength, especially when wet.
11 citations
,
April 2022 in “Biophysical Journal” Disulfide bonds in keratin fibers break more easily under stress, especially when wet, affecting fiber strength.
2 citations
,
September 1996 in “Journal of Applied Polymer Science” Potassium cyanide changes hair's disulfide bonds to monosulfide, affecting high-sulfur proteins more.
3 citations
,
September 2018 in “Journal of Structural Biology” Oxidized trichocyte keratin has a helical dislocation in its structure.
January 2024 in “International Journal of Cosmetic Science” A new method using 1,4-n-butylene dimaleate effectively repairs and strengthens damaged hair.
11 citations
,
September 1996 in “Journal of applied polymer science” Potassium cyanide treatment changes hair's disulfide bonds, making it more elastic.
4 citations
,
January 2015 in “Sen'i Gakkaishi” Hair and wool strength is affected by the number and type of bonds in their protein structures, with hair having more protein aggregates than wool.
15 citations
,
October 1936 in “Archives of Dermatology” Cystine is crucial for forming keratin in hair, wool, and nails.
84 citations
,
June 1970 in “Journal of Investigative Dermatology”
18 citations
,
January 2008 in “Sen'i Gakkaishi” Thioglycolic acid and L-cysteine change hair structure differently during perms, affecting hair strength and curling efficiency.
51 citations
,
September 2012 in “Biomacromolecules” Disulfide bonds make keratin in hair stronger and tougher.
144 citations
,
May 1990 in “Journal of the American Academy of Dermatology” February 2020 in “The Pharmaceutical Society of Japan” 23 citations
,
April 2003 in “Journal of Structural Biology” Keratin structure changes during keratinization, but the exact model remains uncertain.
75 citations
,
August 2018 in “Plant physiology” Hydrogen sulfide disrupts protein function and root hair growth in plants by modifying proteins.
8 citations
,
January 1991 in “Soviet physics. Doklady”
2 citations
,
January 2015 in “Sen'i Gakkaishi” Washing permed hair after using thioglycolic acid helps reform strong bonds, making hair stronger.
31 citations
,
February 2007 in “Journal of Structural Biology” Oxidation changes the structure of hair protein filaments, causing them to compact and rearrange.
January 2018 in “ScholarWorks @UVM (University of Vermont)” Selenium in proteins helps prevent over-oxidation and supports chemical reversibility.
175 citations
,
December 1980 in “Archives of Dermatology” Trichothiodystrophy is a condition with brittle hair and various physical and mental issues due to low sulfur in proteins.
44 citations
,
January 1984 in “Molecular and Cellular Biochemistry” 26 citations
,
January 1983 in “PubMed” Trichothiodystrophy involves brittle hair due to low sulfur amino acids, not a transport defect.
1 citations
,
January 2013 in “PubMed” Permanent wave treatment with thioglycolic acid changes hair structure by altering disulfide bonds.
83 citations
,
July 2008 in “Current Opinion in Chemical Biology” The document concludes that understanding sulfation biology is crucial for creating treatments due to its importance in biological functions and disease.