Zobrazeno 1 - 10
of 749
pro vyhledávání: '"Degrado WF"'
Publikováno v:
Elkins, MR; Wang, T; Nick, M; Jo, H; Lemmin, T; Prusiner, SB; et al.(2016). Structural Polymorphism of Alzheimer's beta-Amyloid Fibrils as Controlled by an E22 Switch: A Solid-State NMR Study. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 138(31), 9840-9852. doi: 10.1021/jacs.6b03715. UCSF: Retrieved from: http://www.escholarship.org/uc/item/3sh5h1d1
The amyloid-β (Aβ) peptide of Alzheimer's disease (AD) forms polymorphic fibrils on the micrometer and molecular scales. Various fibril growth conditions have been identified to cause polymorphism, but the intrinsic amino acid sequence basis for th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______325::62b086046297da1e411fe03387f6b650
http://www.escholarship.org/uc/item/3sh5h1d1
http://www.escholarship.org/uc/item/3sh5h1d1
Autor:
Thomaston, JL, Alfonso-Prieto, M, Woldeyes, RA, Fraser, JS, Klein, ML, Fiorin, G, DeGrado, WF
Publikováno v:
Thomaston, JL; Alfonso-Prieto, M; Woldeyes, RA; Fraser, JS; Klein, ML; Fiorin, G; et al.(2016). High-resolution structures of the M2 channel from influenza A virus reveal dynamic pathways for proton stabilization and transduction (vol 112, pg 14260, 2015). PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 113(18), E2548-E2548. doi: 10.1073/pnas.1605322113. UCSF: Retrieved from: http://www.escholarship.org/uc/item/56m8j2h3
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______325::145c671d467948dc1ac3c7a540ce4d73
http://www.escholarship.org/uc/item/56m8j2h3
http://www.escholarship.org/uc/item/56m8j2h3
Publikováno v:
Reed, NI; Jo, H; Chen, C; Tsujino, K; Arnold, TD; DeGrado, WF; et al.(2015). The αvβ1integrin plays a critical in vivo role in tissue fibrosis. Science Translational Medicine, 7(288). doi: 10.1126/scitranslmed.aaa5094. UCSF: Retrieved from: http://www.escholarship.org/uc/item/5vh192c4
Integrins are transmembrane heterodimeric receptors that contribute to diverse biological functions and play critical roles in many human diseases. Studies using integrin subunit knockout mice and inhibitory antibodies have identified important roles
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______325::04afa4f068b5415d1e5026457cb12b8e
http://www.escholarship.org/uc/item/5vh192c4
http://www.escholarship.org/uc/item/5vh192c4
Publikováno v:
Degrado, WF; Reed, NI; Jo, H; Chen, C; Tsujino, K; Arnold, TD; et al.(2015). The avß1 integrin plays a critical in vivo role in tissue fibrosis.. Science translational medicine, 7(288). UC San Francisco: Retrieved from: http://www.escholarship.org/uc/item/3qn6x6qq
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______325::1d65d4a611a06d1b43513ddb29b61ff1
http://www.escholarship.org/uc/item/3qn6x6qq
http://www.escholarship.org/uc/item/3qn6x6qq
Publikováno v:
Degrado, William; Dong, H; Fiorin, G; Degrado, WF; & Klein, ML. (2014). Proton release from the histidine-tetrad in the M2 channel of the influenza A virus. UC San Francisco: Retrieved from: http://www.escholarship.org/uc/item/71z9g7t4
© 2014 American Chemical Society.The activity of the M2 proton channel of the influenza A virus is controlled by pH. The tautomeric state and conformation of His37, a key residue in the M2 transmembrane four-helix bundle, controls the gating of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______325::c4738f3c1a1149adde121131fd6c3022
http://www.escholarship.org/uc/item/71z9g7t4
http://www.escholarship.org/uc/item/71z9g7t4
Publikováno v:
Degrado, William; Gonzalez, G; Hannigan, B; & DeGrado, WF. (2014). A Real-Time All-Atom Structural Search Engine for Proteins. UC San Francisco: Retrieved from: http://www.escholarship.org/uc/item/1rs2z3tv
Protein designers use a wide variety of software tools for de novo design, yet their repertoire still lacks a fast and interactive all-atom search engine. To solve this, we have built the Suns program: a real-time, atomic search engine integrated int
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______325::814b5270542251a29a7f2324c043c6c0
http://www.escholarship.org/uc/item/1rs2z3tv
http://www.escholarship.org/uc/item/1rs2z3tv
Autor:
Degrado, William, Rufo, CM, Moroz, YS, Moroz, OV, Stöhr, J, Smith, TA, Hu, X, Degrado, WF, Korendovych, IV
Publikováno v:
Degrado, William; Rufo, CM; Moroz, YS; Moroz, OV; Stöhr, J; Smith, TA; et al.(2014). Short peptides self-assemble to produce catalytic amyloids. UC San Francisco: Retrieved from: http://www.escholarship.org/uc/item/5sd9h04q
Enzymes fold into unique three-dimensional structures, which underlie their remarkable catalytic properties. The requirement to adopt a stable, folded conformation is likely to contribute to their relatively large size (>10,000 Da). However, much sho
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______325::b5f84f6da69d34f235e73847eacb78d7
http://www.escholarship.org/uc/item/5sd9h04q
http://www.escholarship.org/uc/item/5sd9h04q
Publikováno v:
Degrado, William; Pavone, V; Zhang, SQ; Merlino, A; Lombardi, A; Wu, Y; et al.(2014). Crystal structure of an amphiphilic foldamer reveals a 48-mer assembly comprising a hollow truncated octahedron. UC San Francisco: Retrieved from: http://www.escholarship.org/uc/item/0rb0d6h5
Foldamers provide an attractive medium to test the mechanisms by which biological macromolecules fold into complex three-dimensional structures, and ultimately to design novel protein-like architectures with properties unprecedented in nature. Here,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______325::a84135b1f081dbbd908c865a9112d4d3
http://www.escholarship.org/uc/item/0rb0d6h5
http://www.escholarship.org/uc/item/0rb0d6h5