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Complex of NS3 protease and NS4A peptide of BK strain hepatitis C virus: a 2.2 A resolution structure in a hexagonal crystal form

Autor: Y, Yan, Y, Li, S, Munshi, V, Sardana, J L, Cole, M, Sardana, C, Steinkuehler, L, Tomei, R, De Francesco, L C, Kuo, Z, Chen

Publikováno v: Protein science : a publication of the Protein Society. 7(4)

The crystal structure of the NS3 protease of the hepatitis C virus (BK strain) has been determined in the space group P6(3)22 to a resolution of 2.2 A. This protease is bound with a 14-mer peptide representing the central region of the NS4A protein.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::c0e24971d836a64b96364c8a66af2dce
https://pubmed.ncbi.nlm.nih.gov/9568891

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Activation of RNase L by 2',5'-oligoadenylates. Kinetic characterization

Autor: S S, Carroll, J L, Cole, T, Viscount, J, Geib, J, Gehman, L C, Kuo

Publikováno v: The Journal of biological chemistry. 272(31)

Ribonuclease L (RNase L), the 2',5'-oligoadenylate-dependent ribonuclease, is one of the cellular antiviral systems with enhanced activity in the presence of interferon. A reaction scheme has been developed to model the sequence of steps necessary fo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::20f9acd5a7a497526977e52e81f20166
https://pubmed.ncbi.nlm.nih.gov/9235910

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Activation of RNase L by 2',5'-oligoadenylates. Biophysical characterization

Autor: J L, Cole, S S, Carroll, E S, Blue, T, Viscount, L C, Kuo

Publikováno v: The Journal of biological chemistry. 272(31)

Ribonuclease L (RNase L) is an endoribonuclease that is activated upon binding of adenosine oligomers linked 2' to 5' to cleave viral and cellular RNAs. We recently proposed a model for activation in which activator A binds to monomer, E, to form EA,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e36388207d630a981e92d529ca6d4cc4
https://pubmed.ncbi.nlm.nih.gov/9235909

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Stoichiometry of 2',5'-oligoadenylate-induced dimerization of ribonuclease L. A sedimentation equilibrium study

Autor: J L, Cole, S S, Carroll, L C, Kuo

Publikováno v: The Journal of biological chemistry. 271(8)

Ribonuclease L is an endoribonuclease that is activated by binding of 2',5'-linked oligoadenylates. Activation of ribonuclease L also induces dimerization. Here, we demonstrate using equilibrium sedimentation that dimerization requires the binding of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::7102572290b21797ed208f6d9e294a85
https://pubmed.ncbi.nlm.nih.gov/8626728

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Memory CD4+ T Cells that Recognise Additional Mismatched Alloantigen Provide CD40-independent Help for Effector Anti-MHC Class I Alloantibody Responses

Autor: Eleanor M. Bolton, Gavin J. Pettigrew, J. L. Cole, Thomas M. Conlon, Kourosh Saeb-Parsy, M. Negus, Andrew Bradley

Publikováno v: Transplantation Journal. 94:438

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::c7418e8f21ed83611350e74867611eea
https://doi.org/10.1097/00007890-201211271-00827

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Bone age, social deprivation, and single parent families

Autor: Tim J Cole, A. J. L. Cole

Publikováno v: Archives of disease in childhood. 67(10)

It is well known that deprivation affects bone growth. The study was set up to investigate what aspects of deprivation are of greatest importance. Bone ages of 1593 child trauma patients aged 0-19 years from Middlesbrough General Hospital, Cleveland,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0766c9174983fb99b982a27a6889c976
https://pubmed.ncbi.nlm.nih.gov/1444529

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