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001-es BibID:	BIBFORM040653
035-os BibID:	PMID:2190554
Első szerző:	Copeland, Terry D.
Cím:	Substitution of proline with pipecolic acid at the scissile bond converts a peptide substrate of HIV proteinase into a selective inhibitor / Terry D. Copeland, Ewald M. Wondrak, Jozsef Tozser, Michael M. Roberts, Stephen Oroszlan
Dátum:	1990
ISSN:	0006-291X
Megjegyzések:	The nonapeptide H-Val-Ser-Gln-Asn-Tyr-Pro-Ile-Val-Gln-NH2 containing the retroviral Tyr-Pro cleavage site is a good substrate for the proteinase of human immunodeficiency viruses but it is not readily hydrolyzed by other nonviral proteinases including the structurally related pepsin-like aspartic proteinases. Replacing the Pro by L-pipecolic acid (2-piperidinecarboxylic acid) converted the substrate into an effective inhibitor of HIV-1 and HIV-2 proteinases with IC50 of approximately 1 microM. This compound showed a high degree of selectivity in that it did not inhibit cathepsin D and renin.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban külföldön készült közlemény
Megjelenés:	Biochemical and Biophysical Research Communications 169 : 1 (1990), p. 310-314. -
További szerzők:	Wondrak, Ewald M. Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész) Roberts, Michael M. Oroszlan, Stephen
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM040661
Első szerző:	Kapust, Rachel B.
Cím:	The P1' specificity of tobacco etch virus protease / Kapust Rachel B., Tözsér József, Copeland Terry D., Waugh David S.
Dátum:	2002
ISSN:	0006-291X
Megjegyzések:	Affinity tags have become indispensable tools for protein expression and purification. Yet, because they have the potential to interfere with structural and functional studies, it is usually desirable to remove them from the target protein. The stringent sequence specificity of the tobacco etch virus (TEV) protease has made it a useful reagent for this purpose. However, a potential limitation of TEV protease is that it is believed to require a Gly or Ser residue in the P1' position of its substrates to process them with reasonable efficiency. Consequently, after an N-terminal affinity tag is removed by TEV protease, the target protein will usually retain a non-native Ser or Gly residue on its N-terminus, and in some cases this may affect its biological activity. To investigate the stringency of the requirement for Gly or Ser in the P1' position of a TEV protease recognition site, we constructed 20 variants of a fusion protein substrate with an otherwise optimal recognition site, each containing a different amino acid in the P1' position. The efficiency with which these fusion proteins were processed by TEV protease was compared both in vivo and in vitro. Additionally, the kinetic parameters K(M) and k(cat) were determined for a representative set of peptide substrates with amino acid substitutions in the P1' position. The results indicate that many side-chains can be accommodated in the P1' position of a TEV protease recognition site with little impact on the efficiency of processing.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Biochemical And Biophysical Research Communications. - 294 : 5 (2002), p. 949-955. -
További szerzők:	Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész) Copeland, Terry D. Waugh, David S.
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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