Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Patrick J. Salveson"'
Autor:
Meerit Y. Said, Christine S. Kang, Shunzhi Wang, William Sheffler, Patrick J. Salveson, Asim K. Bera, Alex Kang, Hannah Nguyen, Ryanne Ballard, Xinting Li, Hua Bai, Lance Stewart, Paul Levine, David Baker
Publikováno v:
Chemistry of Materials. 34:9736-9744
Despite remarkable advances in the assembly of highly structured coordination polymers and metal-organic frameworks, the rational design of such materials using more conformationally flexible organic ligands such as peptides remains challenging. In a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d9e776c6a2a84adcde63a4476e2a3974
https://doi.org/10.1021/acs.chemmater.2c02597
https://doi.org/10.1021/acs.chemmater.2c02597
Autor:
Paul M. Levine, Timothy W. Craven, Xinting Li, Aaron T. Balana, Gregory H. Bird, Marina Godes, Patrick J. Salveson, Patrick W. Erickson, Mila Lamb, Maggie Ahlrichs, Michael Murphy, Cassandra Ogohara, Meerit Y. Said, Loren D. Walensky, Matthew R. Pratt, David Baker
Publikováno v:
ACS Chem Biol
Peptide and protein bioconjugation technologies have revolutionized our ability to site-specifically or chemoselectively install a variety of functional groups for applications in chemical biology and medicine, including the enhancement of bioavailab
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b694595cf409370fd01594d28a8eb682
https://pubmed.ncbi.nlm.nih.gov/35319882
https://pubmed.ncbi.nlm.nih.gov/35319882
Publikováno v:
Angew Chem Int Ed Engl
Although β-hairpins are widespread in proteins, there is still no universal tool to coax any small peptide to adopt a β-hairpin conformation, regardless of sequence. Here, we report that δ-linked γ(R)-methyl-ornithine ((δ)MeOrn) provides an impr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::099645a472d828764e99b51b38a4e661
https://doi.org/10.1002/anie.202105559
https://doi.org/10.1002/anie.202105559
Autor:
Adam G. Kreutzer, Tuan D. Samdin, Sepehr Haerianardakani, James S. Nowick, Patrick J. Salveson, Gretchen Guaglianone
Publikováno v:
J Am Chem Soc
Oligomers of the β-amyloid peptide, Aβ, play a central role in the pathogenesis and progression of Alzheimer’s disease. Trimers and higher-order oligomers composed of trimers are thought to be the most neurotoxic Aβ oligomers. To gain insights i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::77b27863ebe8c599c164692b9824c474
https://doi.org/10.1021/jacs.0c09281
https://doi.org/10.1021/jacs.0c09281
Autor:
Stan Yoo, Adam G. Kreutzer, Patrick J. Salveson, Alexander Thuy-Boun, Borries Demeler, Sepehr Haerianardakani, James S. Nowick
Publikováno v:
J Am Chem Soc
Soluble oligomers of the β-amyloid peptide, Aβ, are associated with the progression of Alzheimer’s disease. Although many small molecules bind to these assemblies, the details of how these molecules interact with Aβ oligomers remain unknown. Thi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::64127c46ae1eb3d3df3c98744fda0094
https://doi.org/10.1021/jacs.8b06568
https://doi.org/10.1021/jacs.8b06568
Autor:
Imane L. Hamza, Ryan K. Spencer, Kate J. McKnelly, James S. Nowick, Adam G. Kreutzer, Stan Yoo, Patrick J. Salveson
Publikováno v:
Biochemistry
The absence of high-resolution structures of amyloid oligomers constitutes a major gap in our understanding of amyloid diseases. A growing body of evidence indicates that oligomers of the β-amyloid peptide Aβ are especially important in the progres
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bb08e84626dc223a6c06e22f1a6e111d
http://europepmc.org/articles/PMC5689071
http://europepmc.org/articles/PMC5689071
Publikováno v:
Organic Letters. 19:3462-3465
The assembly of the β-amyloid peptide, Aβ, into soluble oligomers is associated with neurodegeneration in Alzheimer’s disease. The Aβ oligomers are thought to be composed of β-hairpins. Here, the effect of shifting the residue pairing of the β
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a6c5d721526d3e3eaf7d03fec3a1ff37
https://doi.org/10.1021/acs.orglett.7b01445
https://doi.org/10.1021/acs.orglett.7b01445
Autor:
Adam G. Kreutzer, James S. Nowick, Alexander Thuy-Boun, Patrick J. Salveson, Sepehr Haerianardakani
Publikováno v:
Journal of the American Chemical Society. 140(17)
A key challenge in studying the biological and biophysical properties of amyloid-forming peptides is that they assemble to form heterogeneous mixtures of soluble oligomers and insoluble fibrils. Photolabile protecting groups have emerged as tools to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8f56e327b8af5b0cc2f8de4bba8deed7
https://pubmed.ncbi.nlm.nih.gov/29627987
https://pubmed.ncbi.nlm.nih.gov/29627987
Publikováno v:
Organic letters. 19(13)
The assembly of the β-amyloid peptide, Aβ, into soluble oligomers is associated with neurodegeneration in Alzheimer's disease. The Aβ oligomers are thought to be composed of β-hairpins. Here, the effect of shifting the residue pairing of the β-h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::db623b0a8420f9e74ca785f94460ed05
https://pubmed.ncbi.nlm.nih.gov/28683555
https://pubmed.ncbi.nlm.nih.gov/28683555
Publikováno v:
Journal of the American Chemical Society
Oligomeric assemblies of the protein α-synuclein are thought to cause neurodegeneration in Parkinson’s disease and related synucleinopathies. Characterization of α-synuclein oligomers at high resolution is an outstanding challenge in the field of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8e3b7e9e91530a0c5ca1c83c446351ec
https://pubmed.ncbi.nlm.nih.gov/26926877
https://pubmed.ncbi.nlm.nih.gov/26926877