Zobrazeno 1 - 10
of 400
pro vyhledávání: '"D. Distefano"'
Publikováno v:
Results in Chemistry, Vol 6, Iss , Pp 101044- (2023)
Pyridoxal 5′-phosphate (PLP) is a ubiquitous and versatile cofactor utilized by numerous enzymes involved in amino acid biosynthetic pathways. Immobilized PLP is a valuable tool to isolate unknown PLP-dependent enzymes in nature or to perform in vi
Externí odkaz:
https://doaj.org/article/1353e24e4cfa46f7952e90f1f6a6ff70
Autor:
Anastasiia Petenkova, Shelby A. Auger, Jeffrey Lamb, Daisy Quellier, Cody Carter, On Tak To, Jelena Milosevic, Rana Barghout, Abirami Kugadas, Xiaoxiao Lu, Jennifer Geddes-McAlister, Raina Fichorova, David B. Sykes, Mark D. Distefano, Mihaela Gadjeva
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-16 (2023)
Abstract The bactericidal function of neutrophils is dependent on a myriad of intrinsic and extrinsic stimuli. Using systems immunology approaches we identify microbiome- and infection-induced changes in neutrophils. We focus on investigating the Pre
Externí odkaz:
https://doaj.org/article/2b4852753ce447db8b49d73723254ac4
Autor:
Garrett L. Schey, Emily R. Hildebrandt, You Wang, Safwan Diwan, Holly A. Passetti, Gavin W. Potts, Andrea M. Sprague-Getsy, Ethan R. Leoni, Taylor S. Kuebler, Yuk Y. Sham, James L. Hougland, Lorena S. Beese, Walter K. Schmidt, Mark D. Distefano
Publikováno v:
International Journal of Molecular Sciences, Vol 25, Iss 10, p 5324 (2024)
Protein farnesylation is a post-translational modification where a 15-carbon farnesyl isoprenoid is appended to the C-terminal end of a protein by farnesyltransferase (FTase). This process often causes proteins to associate with the membrane and part
Externí odkaz:
https://doaj.org/article/ea08ad4e851649e0a556fa2f9888c3aa
Autor:
Kiall F. Suazo, Angela Jeong, Mina Ahmadi, Caroline Brown, Wenhui Qu, Ling Li, Mark D. Distefano
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-17 (2021)
Abstract Protein prenylation involves the attachment of one or two isoprenoid group(s) onto cysteine residues positioned near the C-terminus. This modification is essential for many signal transduction processes. In this work, the use of the probe C1
Externí odkaz:
https://doaj.org/article/f4786b4aa4244e60b820bd8d07c24a07
Autor:
Yi Zhang, Yiao Wang, Safak Uslu, Sneha Venkatachalapathy, Mohammad Rashidian, Jonas V. Schaefer, Andreas Plückthun, Mark D. Distefano
Publikováno v:
International Journal of Molecular Sciences, Vol 23, Iss 19, p 11537 (2022)
Protein-based conjugates have been extensively utilized in various biotechnological and therapeutic applications. In order to prepare homogeneous conjugates, site-specific modification methods and efficient purification strategies are both critical f
Externí odkaz:
https://doaj.org/article/8ff71f23a0da4ed888b54d3f35ee1bf2
Autor:
Yiao Wang, Lakmal Rozumalski, Ozgun Kilic, Caitlin Lichtenfels, Jacob Petersberg, Mark D. Distefano, Carston R. Wagner
Publikováno v:
Biomacromolecules
Inspired by the natural intercellular material transfer process of trans-endocytosis or trogocytosis, we proposed that targeted farnesylated chemically self-assembled nanorings (f-CSANs) could serve as a biomimetic trogocytosis vehicle for engineerin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8b9b8cb22c8bf4147cef5153897b8b1f
https://doi.org/10.1021/acs.biomac.2c00837
https://doi.org/10.1021/acs.biomac.2c00837
Autor:
Johannes Morstein, Taysir Bader, Ariana L. Cardillo, Julian Schackmann, Sudhat Ashok, James L. Hougland, Christine A. Hrycyna, Dirk H. Trauner, Mark D. Distefano
Publikováno v:
ACS Chemical Biology. 17:2945-2953
Photoswitchable lipids have emerged as attractive tools for the optical control of lipid bioactivity, metabolism, and biophysical properties. Their design is typically based on the incorporation of an azobenzene photoswitch into the hydrophobic lipid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eeb19c92a26a6054aa394d5ecad65ed4
https://doi.org/10.1021/acschembio.2c00645
https://doi.org/10.1021/acschembio.2c00645
Autor:
Angela Jeong, Shelby A. Auger, Sanjay Maity, Kristina Fredriksen, Rui Zhong, Ling Li, Mark D. Distefano
Publikováno v:
ACS Chemical Biology. 17:2863-2876
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::755232e302c6b5e894ee02abe12767a5
https://doi.org/10.1021/acschembio.2c00486
https://doi.org/10.1021/acschembio.2c00486
Autor:
Garrett L. Schey, Peter H. Buttery, Emily R. Hildebrandt, Sadie X. Novak, Walter K. Schmidt, James L. Hougland, Mark D. Distefano
Publikováno v:
International Journal of Molecular Sciences, Vol 22, Iss 21, p 12042 (2021)
Protein farnesylation is a post-translational modification where a 15-carbon farnesyl isoprenoid is appended to the C-terminal end of a protein by farnesyltransferase (FTase). This modification typically causes proteins to associate with the membrane
Externí odkaz:
https://doaj.org/article/273def10be134692b1140cbbd0a3aa91
Publikováno v:
Analytical chemistry. 94(33)
Protein prenylation is an essential post-translational modification that plays a key role in facilitating protein localization. Aberrations in protein prenylation have been indicated in multiple disease pathologies including progeria, some forms of c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e701ba7e3a979256e022370d6e0768ac
https://pubmed.ncbi.nlm.nih.gov/35952372
https://pubmed.ncbi.nlm.nih.gov/35952372