Purification of active herpes simplex virus-1 protease expressed in Escherichia coli

Autor: P L, Darke, E, Chen, D L, Hall, M K, Sardana, C A, Veloski, R L, LaFemina, J A, Shafer, L C, Kuo

Publikováno v: The Journal of biological chemistry. 269(29)

Assembly of viral capsids for replication of herpes simplex virus requires the proteolytic processing of the assembly protein ICP35. The protease responsible for this process is encoded within the 635-amino acid open reading frame of the UL26 gene of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::61e24208cbc86d414e5edc5efa49aec5
https://pubmed.ncbi.nlm.nih.gov/8034621

Human immunodeficiency virus type 1 protease inhibitors: evaluation of resistance engendered by amino acid substitutions in the enzyme's substrate binding site

Autor: Culberson Jc, R L LaFemina, Kohl Ne, Donald J. Graham, Graham P, V V Sardana, Gotlib L, Jon H. Condra, A J Schlabach, Bush Bl

Publikováno v: Biochemistry. 33(8)

The human immunodeficiency virus type 1 (HIV-1) protease is a homodimeric aspartyl endopeptidase that is required for virus replication. A number of specific, active-site inhibitors for this enzyme have been described. Many of the inhibitors exhibit

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::72f78109bec56c4dc7f7c9031d85a599
https://pubmed.ncbi.nlm.nih.gov/8117657

Requirement of active human immunodeficiency virus type 1 integrase enzyme for productive infection of human T-lymphoid cells

Autor: P L Callahan, K LeGrow, R L LaFemina, William A. Schleif, Emilio A. Emini, C L Schneider, Elizabeth Roth, H L Robbins

The human immunodeficiency virus type 1 (HIV-1) integrase enzyme exhibits significant amino acid sequence conservation with integrase proteins of other retroviruses. We introduced specific amino acid substitutions at a number of the conserved residue

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a610463f1a14a8ef4011fbc83d620f4e
https://europepmc.org/articles/PMC240448/

Substrate specificity of recombinant human immunodeficiency virus integrase protein

Autor: R L LaFemina, P L Callahan, M G Cordingley

Publikováno v: Journal of virology. 65(10)

Recombinant human immunodeficiency virus type 1 (HIV-1) integrase (IN) produced in Escherichia coli efficiently cleaves two nucleotides from the 3' end of synthetic oligonucleotide substrates which mimic the termini of HIV-1 proviral DNA. Efficient c

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::30f71754f180dbfccf744fa49d9d3241
https://pubmed.ncbi.nlm.nih.gov/1895409

Synthesis and Cytotoxic and Antiviral Activity Profiling of All‐Four Isomeric Series of Pyrido‐Fused 7‐Deazapurine Ribonucleosides.

Autor: Veselovská, Lucia¹ (AUTHOR), Kudlová, Natálie^2,3 (AUTHOR), Gurská, Soňa^2,3 (AUTHOR), Lišková, Barbora² (AUTHOR), Medvedíková, Martina² (AUTHOR), Hodek, Ondřej¹ (AUTHOR), Tloušťová, Eva¹ (AUTHOR), Milisavljevic, Nemanja^1,4 (AUTHOR), Tichý, Michal¹ (AUTHOR), Perlíková, Pavla¹ (AUTHOR), Mertlíková‐Kaiserová, Helena¹ (AUTHOR), Trylčová, Jana¹ (AUTHOR), Pohl, Radek¹ (AUTHOR), Klepetářová, Blanka¹ (AUTHOR), Džubák, Petr^2,3 (AUTHOR), Hajdúch, Marián^2,3 (AUTHOR), Hocek, Michal^1,4 (AUTHOR) hocek@uochb.cas.cz

Publikováno v: Chemistry - A European Journal. 10/9/2020, Vol. 26 Issue 57, p13002-13015. 14p.