813 resultados para Founding


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Owing to their pathogenical role and unique ability to exist both as soluble proteins and transmembrane complexes, pore-forming toxins (PFTs) have been a focus of microbiologists and structural biologists for decades. PFTs are generally secreted as water-soluble monomers and subsequently bind the membrane of target cells. Then, they assemble into circular oligomers, which undergo conformational changes that allow membrane insertion leading to pore formation and potentially cell death. Aerolysin, produced by the human pathogen Aeromonas hydrophila, is the founding member of a major PFT family found throughout all kingdoms of life. We report cryo-electron microscopy structures of three conformational intermediates and of the final aerolysin pore, jointly providing insight into the conformational changes that allow pore formation. Moreover, the structures reveal a protein fold consisting of two concentric β-barrels, tightly kept together by hydrophobic interactions. This fold suggests a basis for the prion-like ultrastability of aerolysin pore and its stoichiometry.

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Mode of access: Internet.

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[Vols. 4-6] are called "Series IV-VI."

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"Published in commemoration of its founding at Cornell University, July 1908."

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Mode of access: Internet.

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Title on cover: Specimens of book types, J.S. Cushing & Co., Boston.

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List of members in vols. for 1857-64; the list in the vol. for 1857 covers period from founding of the academy.

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Mode of access: Internet.

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Includes index.

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"Books for the type man": p. 150-153.

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"The text has been written by John Findlay McRae, mainly from authentic documents supplied by H. W. Caslon & co. ltd., A.D.1920."

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Published in London, <1921->; by DMG World Media,

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Cover title.