Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Thomas E. Speltz"'
Autor:
Thomas E. Speltz, Zeyu Qiao, Colin S. Swenson, Xianghang Shangguan, John S. Coukos, Christopher W. Lee, Deborah M. Thomas, Jesse Santana, Sean W. Fanning, Geoffrey L. Greene, Raymond E. Moellering
Publikováno v:
Nature Biotechnology. 41:541-551
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::817090da9ae4b01a5bbe054312722da7
https://doi.org/10.1038/s41587-022-01504-x
https://doi.org/10.1038/s41587-022-01504-x
Autor:
Thomas E, Speltz, Zeyu, Qiao, Colin S, Swenson, Xianghang, Shangguan, John S, Coukos, Christopher W, Lee, Deborah M, Thomas, Jesse, Santana, Sean W, Fanning, Geoffrey L, Greene, Raymond E, Moellering
Publikováno v:
Nature biotechnology.
Despite unequivocal roles in disease, transcription factors (TFs) remain largely untapped as pharmacologic targets due to the challenges in targeting protein-protein and protein-DNA interactions. Here we report a chemical strategy to generate modular
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::ff907d855d7dee6430a301b1e57278a4
https://pubmed.ncbi.nlm.nih.gov/36302987
https://pubmed.ncbi.nlm.nih.gov/36302987
Publikováno v:
Nature Chemistry. 12:885-887
Electrophilic groups that undergo sulfur-exchange chemistry with protein nucleophiles can serve as the functional basis of chemical proteomic probes. A new addition to this class, sulfuramidimidoyl fluoride (SAF), which can be included in an array of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::61a775a58ac7f201e570079eac311d22
https://doi.org/10.1038/s41557-020-00553-6
https://doi.org/10.1038/s41557-020-00553-6
Publikováno v:
Nature chemistry
Drug candidates that form covalent linkages with their target proteins have been under-explored compared to conventional counterparts that modulate biological function by reversible binding to proteins, in part due to concerns about off-target reacti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::7a8f6f19ac31c153efe6440532b6d358
https://pubmed.ncbi.nlm.nih.gov/32868886
https://pubmed.ncbi.nlm.nih.gov/32868886
Publikováno v:
Med Res Rev
Given the ubiquity of the ⍺-helix in the proteome, there has been much research in developing mimics of ⍺-helices, and most of this study has been toward developing protein-protein interaction inhibitors. A common strategy for mimicking ⍺-helic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9b2361770e47a836910bcb83cf8ee9d8
https://doi.org/10.1002/med.21540
https://doi.org/10.1002/med.21540
Autor:
Jonna Frasor, Jeremy J. Wolff, Brian P. David, Thomas E. Speltz, Laura M. Sanchez, Terry W. Moore, Oleksii Dubrovskyi
Publikováno v:
ACS medicinal chemistry letters, vol 9, iss 7
[Image: see text] Matrix assisted laser desorption ionization time-of-flight (MALDI-TOF) imaging mass spectrometry has emerged as a powerful, label-free technique to visualize penetration of small molecules in vivo and in vitro, including in 3D cell
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5a3ed6893e94491d8c42fa0ec785a1c0
https://doi.org/10.1021/acsmedchemlett.8b00091
https://doi.org/10.1021/acsmedchemlett.8b00091
Publikováno v:
ACS Chemical Biology. 13:676-684
We and others have proposed that coactivator binding inhibitors, which block the interaction of estrogen receptor and steroid receptor coactivators, may represent a potential class of new breast cancer therapeutics. The development of coactivator bin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4146bb2745e09635e24f5fecb028aa2c
https://doi.org/10.1021/acschembio.7b01016
https://doi.org/10.1021/acschembio.7b01016
Autor:
Sean W. Fanning, Zamia Siddiqui, Terry W. Moore, Emad Tajkhorshid, Geoffrey L. Greene, Christopher G. Mayne, Thomas E. Speltz
Publikováno v:
Organic & Biomolecular Chemistry. 16:3702-3706
A new computational approach to obtain quantitative energy profiles for helix folding was used in the design of orthogonal hydrocarbon and lactam bicyclic peptides. The proteolytically stable, "cross-stitched" peptide SRC2-BCP1 shows nanomolar affini
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a40f145e38726c53ba7e1af964c73eee
https://doi.org/10.1039/c8ob00790j
https://doi.org/10.1039/c8ob00790j
Autor:
Justin A. Donnelly, Jeffrey E. Montgomery, John S. Coukos, Sean W. Fanning, Thomas E. Speltz, Raymond E. Moellering, Xianghang Shangguan, Geoffrey L. Greene
Publikováno v:
J Am Chem Soc
Macrocyclization can improve bioactive peptide ligands through preorganization of molecular topology, leading to improvement of pharmacologic properties like binding affinity, cell permeability and metabolic stability. Here we demonstrate that Diels-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::79c77ef8345d49b120a6a29381f371ed
https://pubmed.ncbi.nlm.nih.gov/31523967
https://pubmed.ncbi.nlm.nih.gov/31523967
Autor:
Emad Tajkhorshid, Thomas E. Speltz, Terry W. Moore, Christopher G. Mayne, C.E. Fowler, Sean W. Fanning, Geoffrey L. Greene
Publikováno v:
Angewandte Chemie International Edition. 55:4252-4255
"Stapled" peptides are typically designed to replace two non-interacting residues with a constraining, olefinic staple. To mimic interacting leucine and isoleucine residues, we have created new amino acids that incorporate a methyl group in the γ-po
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5078a2465e72c0b71474aafa60637fa1
https://doi.org/10.1002/anie.201510557
https://doi.org/10.1002/anie.201510557