Zobrazeno 1 - 7
of 7
pro vyhledávání: '"H M, Petrassi"'
Autor:
Kaley M Wilburn, Christine R Montague, Peter G. Schultz, H. M. Petrassi, Brian C. VanderVen, B. Qin, Ashley K. Woods, Teresa L. Southard, Case W. McNamara, Melissa S. Love, Ling-Ting Huang
There is a growing appreciation for the idea that bacterial utilization of host-derived lipids, including cholesterol, supports Mycobacterium tuberculosis (Mtb) pathogenesis. This has generated interest in identifying novel antibiotics that can disru
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7c6c1572a2d6a2ac9e0b0768bc80e9ac
https://doi.org/10.1101/2021.08.03.454881
https://doi.org/10.1101/2021.08.03.454881
Autor:
Jeffery W. Kelly, C S Smith, H M Petrassi, Joleen T. White, James C. Sacchettini, Xin Jiang, Per Hammarström
Publikováno v:
Biochemistry. 40:11442-11452
Transthyretin (TTR) is a soluble human plasma protein that can be converted into amyloid by acid-mediated dissociation of the homotetramer into monomers. The pH required for disassembly also results in tertiary structural changes within the monomeric
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::182d7e7a23546f51d1d93655c6011fd3
https://doi.org/10.1021/bi011194d
https://doi.org/10.1021/bi011194d
Autor:
Thomas Klabunde, Prakash Raman, V.B. Oza, James C. Sacchettini, Jeffery W. Kelly, H M Petrassi
Publikováno v:
Nature Structural Biology. 7:312-321
The human amyloid disorders, familial amyloid polyneuropathy, familial amyloid cardiomyopathy and senile systemic amyloidosis, are caused by insoluble transthyretin (TTR) fibrils, which deposit in the peripheral nerves and heart tissue. Several nonst
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b54a73078f0648d2eb987e2eb5c4d4f1
https://doi.org/10.1038/74082
https://doi.org/10.1038/74082
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 9:1-6
Eight small molecules were synthesized to evaluate the structure activity relationships (SAR) of N-substituted anthranilic acids. The molecules were synthesized by benzylation or arylation of methyl anthranilate. A light scattering-based amyloid fibr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3ce99bec01714b8b61d67c1e380a7d2f
https://doi.org/10.1016/s0960-894x(98)00696-9
https://doi.org/10.1016/s0960-894x(98)00696-9
Publikováno v:
Nature structural biology. 7(4)
The human amyloid disorders, familial amyloid polyneuropathy, familial amyloid cardiomyopathy and senile systemic amyloidosis, are caused by insoluble transthyretin (TTR) fibrils, which deposit in the peripheral nerves and heart tissue. Several nonst
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::ecb776e7447c4ee9fcd8f8fdd20d0bc3
https://pubmed.ncbi.nlm.nih.gov/10742161
https://pubmed.ncbi.nlm.nih.gov/10742161
Publikováno v:
SPIE Proceedings.
Microwave energy has been shown to be able to induce drastic rate increase for certain reactions. These rate enhancements have been proposed to originate from non-thermal dynamics. However, these model system have often been studied under high pressu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8a5f0058ad22ab594d0c28d1c29e661b
https://doi.org/10.1117/12.372893
https://doi.org/10.1117/12.372893
Publikováno v:
Protein science : a publication of the Protein Society. 8(4)
The objective of this study was to evaluate the suitability of the WW domain as a desirable model system to understand the folding and stability of an isolated three-stranded antiparallel beta-sheet structure. The WW domain was subjected to thermal a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::07057a8a352015f78668e3d7f6e26774
https://pubmed.ncbi.nlm.nih.gov/10211830
https://pubmed.ncbi.nlm.nih.gov/10211830