Výsledky vyhledávání - "I C, Deckman"

The 80's loop (residues 78 to 85) is important for the differential activity of retroviral proteases

Autor: J, Stebbins, E M, Towler, M G, Tennant, I C, Deckman, C, Debouck

Publikováno v: Journal of molecular biology. 267(3)

The abundance of structural data available for retroviral proteases affords a unique opportunity to investigate structure activity relationships. Our approach attempts to genetically engineer an HIV (human immunodeficiency virus)-1 protease that is f

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::18c0c615a8cb52dfc7acfe9e00640b13
https://pubmed.ncbi.nlm.nih.gov/9126830

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Identification of the herpes simplex virus-1 protease cleavage sites by direct sequence analysis of autoproteolytic cleavage products

Autor: C L, DiIanni, D A, Drier, I C, Deckman, P J, McCann, F, Liu, B, Roizman, R J, Colonno, M G, Cordingley

Publikováno v: The Journal of biological chemistry. 268(3)

Herpes simplex virus type-1 (HSV-1) encodes a protease responsible for proteolytic processing of the virus assembly protein, ICP35 (infected cell protein 35). The coding region of ICP35 is contained within the gene that encodes the protease, and ICP3

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ac177b0f2d67367da983d3a41f912d5d
https://pubmed.ncbi.nlm.nih.gov/8380586

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Herpes simplex virus type 1 protease expressed in Escherichia coli exhibits autoprocessing and specific cleavage of the ICP35 assembly protein

Autor: I C Deckman, M Hagen, P J McCann

Publikováno v: Journal of virology. 66(12)

The UL26 gene of herpes simplex virus type 1 (HSV-1) encodes a protease which is responsible for the C-terminal cleavage of the nucleocapsid-associated proteins, ICP35 c and d, to their posttranslationally modified counterparts, ICP35 e and f. To fur

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::135701814b0a4c0aacc15be354a47aed
https://pubmed.ncbi.nlm.nih.gov/1331526

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S4-alpha mRNA translation regulation complex. II. Secondary structures of the RNA regulatory site in the presence and absence of S4

Autor: I C, Deckman, D E, Draper

Publikováno v: Journal of molecular biology. 196(2)

The secondary structure of the Escherichia coli alpha mRNA leader sequence has been determined using nucleases specific for single- or double-stranded RNA. Three different length alpha RNA fragments were studied at 0 degrees C and 37 degrees C. A ver

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::b82bbd43becade5d486aaa6ebd1c6175
https://pubmed.ncbi.nlm.nih.gov/2443720

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Physical studies of ribosomal protein-RNA interactions

Autor: D E, Draper, I C, Deckman, J V, Vartikar

Publikováno v: Methods in enzymology. 164

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::01c487793aea26a0d59c48c7be3f15b9
https://pubmed.ncbi.nlm.nih.gov/3071663

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S4-alpha mRNA translation repression complex. I. Thermodynamics of formation

Autor: I C, Deckman, D E, Draper, M S, Thomas

Publikováno v: Journal of molecular biology. 196(2)

Expression of the four ribosomal proteins from the Escherichia coli alpha operon (S4, S11, S13, and L17) is regulated at the level of translation by the binding of S4 to the alpha mRNA. Using a filter binding assay and alpha mRNA sequences prepared b

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::5c8859467086c0f986f39988ccd97142
https://pubmed.ncbi.nlm.nih.gov/2443719

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