Zobrazeno 1 - 10
of 83
pro vyhledávání: '"Freddie R Salsbury"'
Autor:
Dizhou Wu, Freddie R. Salsbury
Publikováno v:
ACS Omega, Vol 9, Iss 21, Pp 23086-23100 (2024)
Externí odkaz:
https://doaj.org/article/632a7a96f6b142fcb1f231bf1d5fa539
Autor:
Natalie R Gassman, Jill E Clodfelter, Anita K McCauley, Keith Bonin, Freddie R Salsbury, Karin D Scarpinato
Publikováno v:
PLoS ONE, Vol 6, Iss 3, p e17907 (2011)
Human mismatch repair proteins MSH2-MSH6 play an essential role in maintaining genetic stability and preventing disease. While protein functions have been extensively studied, the substantial amino-terminal region (NTR*) of MSH6 that is unique to euk
Externí odkaz:
https://doaj.org/article/e611ffec021a49cd852cb1bcd002ac7f
Autor:
Wayne O. Hemphill, Sean R. Simpson, Mingyong Liu, Freddie R. Salsbury, Thomas Hollis, Jason M. Grayson, Fred W. Perrino
Publikováno v:
Frontiers in Immunology, Vol 12 (2021)
Mutations in the TREX1 3’ → 5’ exonuclease are associated with a spectrum of autoimmune disease phenotypes in humans and mice. Failure to degrade DNA activates the cGAS-STING DNA-sensing pathway signaling a type-I interferon (IFN) response that
Externí odkaz:
https://doaj.org/article/6b112cac40a84ca48d20a8c220831359
The 3’ → 5’ exonuclease TREX1 functions in vivo to degrade DNA and prevent chronic immune activation through the cGAS-STING pathway. TREX1 has been described as a nonprocessive enzyme with little preference for ss-versus dsDNA, raising question
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e48127256ac396cb64af2fbe70679aa4
https://doi.org/10.1101/2022.02.25.481063
https://doi.org/10.1101/2022.02.25.481063
Publikováno v:
Biophysical Journal. 122:216a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d06f00caa8678e201f9ad2ca8bf733b9
https://doi.org/10.1016/j.bpj.2022.11.1288
https://doi.org/10.1016/j.bpj.2022.11.1288
Autor:
Dizhou Wu, Freddie R. Salsbury
Publikováno v:
J Mol Model
Thrombin is a Na[Formula: see text]-activated serine protease existing in two forms targeted to procoagulant and anticoagulant activities, respectively. There is one Na[Formula: see text]-binding site that has been the focus of the study of the throm
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a4618ac3245d58221078a18ec14d1936
https://pubmed.ncbi.nlm.nih.gov/35419655
https://pubmed.ncbi.nlm.nih.gov/35419655
Publikováno v:
The Journal of Chemical Physics. 157:085102
The proteolytic cleavage of C99 by γ-secretase is the last step in the production of amyloid- β (A β) peptides. Previous studies have shown that membrane lipid composition, cholesterol concentration, and mutation in the transmembrane helix modifie
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::124b993c97b8065e2108eb1e9ed33b9d
https://doi.org/10.1063/5.0101622
https://doi.org/10.1063/5.0101622
Autor:
Freddie R. Salsbury, Thomas Hollis, Wayne O. Hemphill, Sean R Simpson, Fred W. Perrino, Jason M. Grayson, Mingyong Liu
Publikováno v:
Frontiers in Immunology, Vol 12 (2021)
Frontiers in Immunology
Frontiers in Immunology
Mutations in the TREX1 3’ → 5’ exonuclease are associated with a spectrum of autoimmune disease phenotypes in humans and mice. Failure to degrade DNA activates the cGAS-STING DNA-sensing pathway signaling a type-I interferon (IFN) response that
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6c0c52a93679712b4f51ad10eda07917
https://doi.org/10.3389/fimmu.2021.660184
https://doi.org/10.3389/fimmu.2021.660184
Publikováno v:
J Chem Inf Model
Thrombin plays an important role in the process of hemostasis and blood coagulation. Studies in thrombin can help us find ways to treat cancer because thrombin is able to reduce the characteristic hypercoagulability of cancer. Thrombin is composed of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::18e62d493326b2c6f20ba0bb148b4846
https://pubmed.ncbi.nlm.nih.gov/33450154
https://pubmed.ncbi.nlm.nih.gov/33450154
Publikováno v:
ACS Omega, Vol 3, Iss 9, Pp 10668-10678 (2018)
Open in a separate window The fidelity of protein synthesis is largely dominated by the accurate recognition of transfer RNAs (tRNAs) by their cognate aminoacyl-tRNA synthetases. Aminoacylation of each tRNA with its cognate amino acid is necessary to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f99b8a86d369ef8ba6540001138cd9dc
https://doi.org/10.1021/acsomega.8b00280
https://doi.org/10.1021/acsomega.8b00280