26 citations
,
January 2018 in “Skin appendage disorders” Thallium, mercury, selenium, and colchicine strongly cause hair loss.
Protein profiling of forehead skin can help distinguish between frontal fibrosing alopecia and androgenetic alopecia.
January 1995 in “Seoul National University Open Repository (Seoul National University)” SSO helps in skin protection and 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.
15 citations
,
October 1936 in “Archives of Dermatology” Cystine is crucial for forming keratin in hair, wool, and nails.
2 citations
,
July 1968 in “Experimental Biology and Medicine” Cystaselenonine causes temporary hair loss in mice by interfering with hair growth.
39 citations
,
June 2012 in “Journal of Structural Biology” Disulfide bonds are crucial for hair structure during keratinization.
May 2024 in “International Journal of Cosmetic Science” Disulfide bonds are crucial for hair's strength, especially when wet.
March 1990 in “Journal of Dermatological Science”
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.
53 citations
,
March 2006 in “Biopolymers” TTD hair is brittle due to fewer sulfur amino acids and unstable disulfide bonds.
February 2020 in “The Pharmaceutical Society of Japan” 11 citations
,
April 2022 in “Biophysical Journal” Disulfide bonds in keratin fibers break more easily under stress, especially when wet, affecting fiber strength.
January 2008 in “Chinese Journal of Spectroscopy Laboratory” Cysteine formation on hair indicates damage, best detected at pH 4.5.
22 citations
,
November 2014 in “Proteins Structure Function and Bioinformatics” Cysteines in wool fibers are accessible and form important disulfide bonds.
36 citations
,
October 2014 in “Langmuir” Bleaching hair removes its protective top layer and exposes more hydrophilic groups, changing its chemical surface and affecting how it interacts with products.
1 citations
,
January 2009 in “Journal of S C C J” Changing disulfide bonds in human hair affects its melting behavior and thermal stability.
10 citations
,
January 2012 in “International Journal of Cosmetic Science” Thioglycolic acid mainly affects the unordered areas in hair structure.
January 2024 in “International Journal of Cosmetic Science” A new method using 1,4-n-butylene dimaleate effectively repairs and strengthens damaged hair.
June 1996 in “Journal of Dermatological Science” 26 citations
,
January 1983 in “PubMed” Trichothiodystrophy involves brittle hair due to low sulfur amino acids, not a transport defect.
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.
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.
7 citations
,
January 1959 in “Canadian Journal of Chemistry” Human and horse hair have similar end groups to wool and feathers.
3 citations
,
January 2004 in “Sen i Gakkaishi” DTDG in hair treatments reduces damage and preserves hair structure.
11 citations
,
January 1997 in “Journal of Dermatological Science” A new protein linked to hair strength was identified, aiding in understanding brittle hair conditions.
6 citations
,
April 1989 in “Nuclear Instruments and Methods in Physics Research Section B Beam Interactions with Materials and Atoms” Sulphur in hair follicles increases from the bulb and then levels off, while other elements vary in distribution.
20 citations
,
December 2012 in “Journal of molecular structure” The study found that thioglycolic acid breaks down hair bonds more consistently than l-cysteine, which is less damaging to hair.
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.
1 citations
,
February 1991 in “Journal of Biological Chemistry”