Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Matthew R. Hoag"'
Autor:
Riyao Yang, Su Huang, Cai Huang, Nathan S. Fay, Yanan Wang, Saroja Putrevu, Kimberly Wright, Mohd Saif Zaman, Wenyan Cai, Betty Huang, Bo Wang, Meredith Wright, Matthew R. Hoag, Allison Titong, Yue Liu
Publikováno v:
Scientific Reports, Vol 13, Iss 1, Pp 1-13 (2023)
Abstract The landscape of current cancer immunotherapy is dominated by antibodies targeting PD-1/PD-L1 and CTLA-4 that have transformed cancer therapy, yet their efficacy is limited by primary and acquired resistance. The blockade of additional immun
Externí odkaz:
https://doaj.org/article/079a39b41a854fccb3850dced3f2c63c
Autor:
Bo Wang, Jun Lin, Matthew R Hoag, Meredith Wright, Mingjun Ma, Wenyan Cai, Sachith Gallolu Kankanamalage, Yue Liu
Publikováno v:
Antibody therapeutics. 5(3)
The classical `knob-into-holes' (KIH) strategy (knob(T366Y)/hole (Y407T)) has successfully enhanced the heterodimerization of a bispecific antibody (BsAb) resulting in heterodimer formation up to 92% of protein A (ProA)-purified protein pool. However
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::546dfe9938407ac7846b34dc5538ac02
https://pubmed.ncbi.nlm.nih.gov/36042698
https://pubmed.ncbi.nlm.nih.gov/36042698
Autor:
Nikola, Kenjić, Matthew R, Hoag, Garrett C, Moraski, Carol A, Caperelli, Graham R, Moran, Audrey L, Lamb
Publikováno v:
Archives of biochemistry and biophysics. 664
The hydroxyornithine transformylase from Pseudomonas aeruginosa is known by the gene name pvdF, and has been hypothesized to use N(10)-formyltetrahydrofolate (N(10)-fTHF) as a co-substrate formyl donor to convert N(5)-hydroxyornithine (OHOrn) to N(5)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::eba026dd618d1f658e6a578d49f913cb
https://pubmed.ncbi.nlm.nih.gov/30689984
https://pubmed.ncbi.nlm.nih.gov/30689984
Publikováno v:
Journal of the American Chemical Society. 135:13980-13987
Renalase is a protein hormone secreted into the blood by the kidney that is reported to lower blood pressure and slow heart rate. Since its discovery in 2005, renalase has been the subject of conjecture pertaining to its catalytic function. While it
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::666b0a48e7a806cea90e029406ab88be
https://doi.org/10.1021/ja407384h
https://doi.org/10.1021/ja407384h
Autor:
Audrey L. Lamb, Matthew R. Hoag, Brett A. Beaupre, Graham R. Moran, Joseph V. Roman, Kathleen M. Meneely, Nicholas R. Silvaggi
Publikováno v:
Archives of biochemistry and biophysics. 612
Renalase catalyzes the oxidation of isomers of β-NAD(P)H that carry the hydride in the 2 or 6 positions of the nicotinamide base to form β-NAD(P)+. This activity is thought to alleviate inhibition of multiple β-NAD(P)-dependent enzymes of primary
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::22f38d30667a1bfa4d2f04a5160e0444
https://pubmed.ncbi.nlm.nih.gov/27769837
https://pubmed.ncbi.nlm.nih.gov/27769837
Publikováno v:
Biochemistry. 54(24)
Despite a lack of convincing in vitro evidence and a number of sound refutations, it is widely accepted that renalase is an enzyme unique to animals that catalyzes the oxidative degradation of catecholamines in blood in order to lower vascular tone.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c6dfbc83a3b11e31ff55adaf0a3308e
https://pubmed.ncbi.nlm.nih.gov/26016690
https://pubmed.ncbi.nlm.nih.gov/26016690
Publikováno v:
Archives of biochemistry and biophysics. 579
It is widely accepted that the function of human renalase is to oxidize catecholamines in blood. However, this belief is based on experiments that did not account for slow, facile catecholamine autoxidation reactions. Recent evidence has shown that r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6975f79bfb894c692f16a753ce1a64c8
https://pubmed.ncbi.nlm.nih.gov/26049000
https://pubmed.ncbi.nlm.nih.gov/26049000
Kinetics and equilibria of the reductive and oxidative half-reactions of human renalase with α-NADPH
Publikováno v:
Biochemistry. 52(49)
Renalase is a recently discovered flavoprotein that has been reported to be a hormone produced by the kidney to down-modulate blood pressure and heart rate. The consensus belief has been that renalase oxidizes circulating catecholamine neurotransmitt
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a87fe04dffa64cc54cd1626cc6e4a67a
https://pubmed.ncbi.nlm.nih.gov/24266457
https://pubmed.ncbi.nlm.nih.gov/24266457