Cargando…
The Thermal Stability of the Collagen Triple Helix Is Tuned According to the Environmental Temperature
Triple helix formation of procollagen occurs in the endoplasmic reticulum (ER) where the single-stranded α-chains of procollagen undergo extensive post-translational modifications. The modifications include prolyl 4- and 3-hydroxylations, lysyl hydroxylation, and following glycosylations. The modifi...
Autores principales: | Fujii, Kazunori K., Taga, Yuki, Takagi, Yusuke K., Masuda, Ryo, Hattori, Shunji, Koide, Takaki |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8877210/ https://www.ncbi.nlm.nih.gov/pubmed/35216155 http://dx.doi.org/10.3390/ijms23042040 |
Ejemplares similares
-
In-depth correlation analysis demonstrates that 4-hydroxyproline at the Yaa position of Gly-Xaa-Yaa repeats dominantly stabilizes collagen triple helix
por: Taga, Yuki, et al.
Publicado: (2021) -
Lowering the culture temperature corrects collagen abnormalities caused by HSP47 gene knockout
por: Fujii, Kazunori K., et al.
Publicado: (2019) -
Hydroxyproline Ring Pucker Causes Frustration of Helix Parameters in the Collagen Triple Helix
por: Ying Chow, W., et al.
Publicado: (2015) -
Non-linearity of the collagen triple helix in solution and implications for collagen function
por: Walker, Kenneth T., et al.
Publicado: (2017) -
Cis-trans isomerization of peptoid residues in the collagen triple-helix
por: Qiu, Rongmao, et al.
Publicado: (2023)