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The HIV-1 Protease as Enzyme and Substrate: Mutagenesis of Autolysis Sites and Generation of a Stable Mutant with Retained Kinetic Properties

Autor: D J Rothrock, Carol A. Bannow, C S Tomich, J M Lull, A. M. Mildner, I M Reardon, J L Sarcich, Clark W. Smith, W J Howe, Joseph W. Leone

Publikováno v: Biochemistry. 33:9405-9413

Site-directed mutagenesis of autolysis sites in the human immunodeficiency virus type 1 (HIV-1) protease was applied in an analysis of enzyme specificity; the protease served, therefore, as both enzyme and substrate in this study. Inspection of natur

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d1c53661bef00e283b8c61084e47454c
https://doi.org/10.1021/bi00198a005

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Stable production of an analog of human tissue plasminogen activator from culturedDrosophila cells

Autor: S K Rockenbach, Mary K. Olsen, J G Hoogerheide, H D Fischer, C S Tomich

Publikováno v: Cytotechnology. 10:157-167

We have studied the expression of an analog of human tissue plasminogen activator, FK2P, in Drosophila Schneider 2 cells. A number of promoters were tested, including the Drosophila metallothionein promoter (MTd), baculovirus immediate early promoter

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9ccf7780f01e86b43a8c968e072d2e6a
https://doi.org/10.1007/bf00570892

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The crystallographic structure of the protease from human immunodeficiency virus type 2 with two synthetic peptidic transition state analog inhibitors

Autor: A M, Mulichak, J O, Hui, A G, Tomasselli, R L, Heinrikson, K A, Curry, C S, Tomich, S, Thaisrivongs, T K, Sawyer, K D, Watenpaugh

Publikováno v: The Journal of biological chemistry. 268(18)

The crystal structure of human immunodeficiency virus (HIV) type 2 protease has been determined in complexes with peptidic inhibitors Noa-His-Cha psi [CH(OH)CH(OH)]Val-Ile-Amp (U75875) and Qnc-Asn-Cha psi [CH(OH)CH2]Val-Npt(U92163) (where Noa is naph

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::c14c3e22a5f86e681b1cc7dd09fb8a7d
https://pubmed.ncbi.nlm.nih.gov/8514751

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Folding and activation of recombinant human prorenin

Autor: S K, Sharma, D B, Evans, C S, Tomich, J C, Cornette, R G, Ulrich

Publikováno v: Biotechnology and applied biochemistry. 9(2)

In vitro folding of mature renin, prorenin, and fused prorenin, all produced in denatured form in inclusion bodies in recombinant Escherichia coli, has been studied in order to evaluate the importance of prosequence in the folding of human renin. The

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::551397dbe96649bceb5eeceeaa9d4a61
https://pubmed.ncbi.nlm.nih.gov/3297099

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The nusA recognition site. Alteration in its sequence or position relative to upstream translation interferes with the action of the N antitermination function of phage lambda

Autor: E R, Olson, C S, Tomich, D I, Friedman

Publikováno v: Journal of molecular biology. 180(4)

The phage lambda transcription antitermination protein, pN, acts with host factors, Nus, at sites on the phage genome, nut, to render RNA polymerase resistant to subsequent downstream termination signals. The NusA protein appears to recognize a seven

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a27ded6e1eb3aabbbd0c782411c2eb4f
https://pubmed.ncbi.nlm.nih.gov/6098688

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