Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Jonathan K, Dozier"'
Autor:
Idrees Mohammed, Mark D. Distefano, Brandon J. Floyd, Shahienaz E. Hampton, Jonathan K. Dozier, Timothy M. Dore, Haley E. Smith, Emily R. Hildebrandt, Robert A. Kutlik, Surya P. Manandhar, Louise Ashall, Walter K. Schmidt
Publikováno v:
Bioorganic & Medicinal Chemistry. 24:160-178
Ras converting enzyme 1 (Rce1) is an endoprotease that catalyzes processing of the C-terminus of Ras protein by removing -aaX from the CaaX motif. The activity of Rce1 is crucial for proper localization of Ras to the plasma membrane where it function
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8af84349be9af85fef2d22680639b88f
https://doi.org/10.1016/j.bmc.2015.11.043
https://doi.org/10.1016/j.bmc.2015.11.043
Autor:
Mark D. Distefano, Jonathan K. Dozier
Publikováno v:
International Journal of Molecular Sciences, Vol 16, Iss 10, Pp 25831-25864 (2015)
International Journal of Molecular Sciences
International Journal of Molecular Sciences
The use of proteins as therapeutics has a long history and is becoming ever more common in modern medicine. While the number of protein-based drugs is growing every year, significant problems still remain with their use. Among these problems are rapi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::76908927f960a7e99f74a83c14e5bdcd
http://www.mdpi.com/1422-0067/16/10/25831
http://www.mdpi.com/1422-0067/16/10/25831
Publikováno v:
ACS Chemical Biology
Protein farnesytransferase (PFTase) catalyzes the farnesylation of proteins with a carboxy-terminal tetrapeptide sequence denoted as a Ca1a2X box. To explore the specificity of this enzyme, an important therapeutic target, solid-phase peptide synthes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::45dfe1d4115160b78d13be72e16beb2d
https://doi.org/10.1021/cb5002312
https://doi.org/10.1021/cb5002312
Publikováno v:
Current Protocols in Chemical Biology
In a facile and potentially general method for protein modification at the C-terminus, aldehyde-modified proteins, obtained from enzymatic protein prenylation, react rapidly with hydrazide and aminooxy surfaces and fluorophores at neutral pH and in m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::17bb2df6a100553db7bb3d6139ac99ea
https://doi.org/10.1002/9780470559277.ch120247
https://doi.org/10.1002/9780470559277.ch120247
Autor:
Stepan Lenevich, Charuta C. Palsuledesai, Mark D. Distefano, Amanda J. DeGraw, Jonathan K. Dozier, Mohammad Rashidian, Joshua D. Ochocki
Publikováno v:
Chemical Biology & Drug Design. 76:460-471
Protein prenyltransferases catalyze the attachment of C15 (farnesyl) and C20 (geranylgeranyl) groups to proteins at specific sequences localized at or near the C-termini of specific proteins. Determination of the specific protein prenyltransferase su
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::814e8f9ddd88f4b70f04761592e0e9d3
https://doi.org/10.1111/j.1747-0285.2010.01037.x
https://doi.org/10.1111/j.1747-0285.2010.01037.x
Autor:
Yen Chih Wang, Jonathan K. Dozier, Santoshkumar L. Khatwani, James W. Wollack, Mark D. Distefano, Claudia Schmidt-Dannert
Publikováno v:
Bioconjugate Chemistry
Creating covalent protein conjugates is an active area of research due to the wide range of uses for protein conjugates spanning everything from biological studies to protein therapeutics. Protein Farnesyltransferase (PFTase) has been used for the cr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::906848cbff370d982e58fde0a19c1d46
https://pubmed.ncbi.nlm.nih.gov/24946229
https://pubmed.ncbi.nlm.nih.gov/24946229
Autor:
Jonathan K. Dozier, Benjamin J. Monson, Joseph J. Dalluge, Mark D. Distefano, James W. Wollack, Kristina Poss, Scott A. Hilderbrand
There is a growing library of functionalized non-natural substrates for the enzyme protein farnesyltransferase (PFTase). PFTase covalently attaches these functionalized non-natural substrates to proteins ending in the sequence CAAX, where C is a cyst
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cf9d0e14d5ef2a05f58ec0d943f1ab3d
https://europepmc.org/articles/PMC4107141/
https://europepmc.org/articles/PMC4107141/
Site-specific modification of proteins is a major challenge in modern chemical biology due to the large number of reactive functional groups typically present in polypeptides. Because of its importance in biology and medicine, the development of meth
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::448a442eeadfc3ddca656af07fdfde09
https://europepmc.org/articles/PMC3864113/
https://europepmc.org/articles/PMC3864113/
Autor:
Dayanara P. Parra, Erhan Bat, Jonathan K. Dozier, Mark D. Distefano, Zachary P. Tolstyka, Bruce Dunn, Wade Richardson, Caitlin J. Stevens, Heather D. Maynard
Publikováno v:
Chembiochem : a European journal of chemical biology. 14(18)
Herein, a combination of microcontact printing of functionalized alkanethiols and site-specific modification of proteins is utilized to chemoselectively immobilize proteins onto gold surfaces either by oxime or copper catalyzed alkyne-azide click che
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::80e9f275685ef46639abd51481fdf3b8
https://pubmed.ncbi.nlm.nih.gov/24166802
https://pubmed.ncbi.nlm.nih.gov/24166802
Autor:
Rachit Shah, Mohammad Rashidian, M. Mohsen Mahmoodi, Jonathan K. Dozier, Mark D. Distefano, Carston R. Wagner
Publikováno v:
Bioconjugate chemistry. 24(3)
Imine-based reactions are useful for a wide range of bioconjugation applications. Although aniline is known to catalyze the oxime ligation reaction under physiological conditions, it suffers from slow reaction kinetics, specifically when a ketone is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a10f69d8e43bdfaa8dd6f06fbd05cae1
https://pubmed.ncbi.nlm.nih.gov/23425124
https://pubmed.ncbi.nlm.nih.gov/23425124