Evidence map›Paper›PMID 18701588›Full record

ArticleJournal of virology2008

Amino acid preferences of retroviral proteases for amino-terminal positions in a type 1 cleavage site.

Helga Eizert, Pálma Bander, Péter Bagossi, Tamás Sperka, Gabriella Miklóssy, Péter Boross, Irene T Weber, József Tözsér

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.6field-weighted citation impact, top 37% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 25 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Functional Study of the Retrotransposon-Derived Human PEG10 Protease.International journal of molecular sciences · 2020
    Article
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  8. Article
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  11. Article
  12. Critical differences in HIV-1 and HIV-2 protease specificity for clinical inhibitors.Protein science : a publication of the Protein Society · 2012
    Article
  13. Article
  14. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 2 countries.

Helga EizertUniversity of Debrecen, Department of Biochemistry and Molecular Biology, Nagyerdei krt. 98, Debrecen H-4012, Hungary.
Pálma Bander
Péter Bagossi
Tamás Sperka
Gabriella Miklóssy
Péter Boross
Irene T Weber
József Tözsér
University of Debrecen · HUGeorgia State University · US

Funding

ACTIVITY OF RESISTANT VARIANTS OF HIV PROTEASER01GM062920 · NIGMS · GEORGIA STATE UNIVERSITY · PI WEBER, IRENE T · 2000 to 2012
$3.3M
Inhibition of Resistant Variants of HIV ProteaseU01GM062920 · NIGMS · GEORGIA STATE UNIVERSITY · PI HARRISON, ROBERT WILSON, WEBER, IRENE T · 2013 to 2018
$2.1M
SPECIFICITY STUDIES OF HIV AND HTLV PROTEASESR03TW001001 · FIC · THOMAS JEFFERSON UNIVERSITY · PI WEBER, IRENE T · 1999 to 2004
$199k
FIC NIH HHS R03 TW001001FIC NIH HHS TW01001NIGMS NIH HHS GM062920NIGMS NIH HHS R01 GM062920NIGMS NIH HHS U01 GM062920
6 · The paper itself

Abstract

The specificities of the proteases of 11 retroviruses were studied using a series of oligopeptides with amino acid substitutions in the P1, P3, and P4 positions of a naturally occurring type 1 cleavage site (Val-Ser-Gln-Asn-Tyr downward arrowPro-Ile-Val-Gln) in human immunodeficiency virus type 1 (HIV-1). Previously, the substrate specificity of the P2 site was studied for the same representative set of retroviral proteases, which included at least one member from each of the seven genera of the family Retroviridae (P. Bagossi, T. Sperka, A. Fehér, J. Kádas, G. Zahuczky, G. Miklóssy, P. Boross, and J. Tözsér, J. Virol. 79:4213-4218, 2005). Our enzyme set comprised the proteases of HIV-1, HIV-2, equine infectious anemia virus, avian myeloblastosis virus (AMV), Mason-Pfizer monkey virus, mouse mammary tumor virus (MMTV), Moloney murine leukemia virus, human T-lymphotropic virus type 1, bovine leukemia virus, walleye dermal sarcoma virus, and human foamy virus. Molecular models were used to interpret the similarities and differences in specificity between these retroviral proteases. The results showed that the retroviral proteases had similar preferences (Phe and Tyr) for the P1 position in this sequence context, but differences were found for the P3 and P4 positions. Importantly, the sizes of the P3 and P4 residues appear to be a major contributor for specificity. The substrate specificities correlated well with the phylogenetic tree of the retroviruses. Furthermore, while the specificities of some enzymes belonging to different genera appeared to be very similar (e.g., those of AMV and MMTV), the specificities of the primate lentiviral proteases substantially differed from that observed for a nonprimate lentiviral protease.

Indexed as

Amino Acid SequenceAmino AcidsAmino Acid SubstitutionAnimalsHIV-1HumansMolecular StructureOligopeptidesPeptide HydrolasesPhylogenyProtein ConformationRetroviridaeSubstrate SpecificityViral ProteinsAmino AcidsOligopeptidesPeptide HydrolasesViral Proteins

Identifiers

PMID18701588
PMCPMC2566267
OpenAlexW2119536226

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.