Evidence map›Paper›PMID 9261433›Full record

ArticleJournal of virology1997

The protease and the assembly protein of Kaposi's sarcoma-associated herpesvirus (human herpesvirus 8).

A Unal, T R Pray, M Lagunoff, M W Pennington, D Ganem, C S Craik

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

22 citing papers in PubMed, 47 citations in OpenAlex.

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  17. Communication between the active sites and dimer interface of a herpesvirus protease revealed by a transition-state inhibitor.Proceedings of the National Academy of Sciences of the United States of America · 2004
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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

6 authors at 1 institution in 1 country.

A UnalDepartment of Pharmaceutical Chemistry, University of California, San Francisco 94143, USA.
T R Pray
M Lagunoff
M W Pennington
D Ganem
C S Craik
University of California, San Francisco · US

Funding

STRUCTURAL BIOLOGY TRAINING PROGRAMT32GM008284 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI KORTEMME, TANJA · 1988 to 2022
$10.1M
SYNTHESIS, ENZYMOLOGY, AND DRUG DESIGNP01GM039552 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI CRAIK, CHARLES SCOTT · 1987 to 1996
–
NIGMS NIH HHS GM39552NIGMS NIH HHS T32 GM08284
6 · The paper itself

Abstract

A genomic clone encoding the protease (Pr) and the assembly protein (AP) of Kaposi's sarcoma-associated herpesvirus (KSHV) (also called human herpesvirus 8) has been isolated and sequenced. As with other herpesviruses, the Pr and AP coding regions are present within a single long open reading frame. The mature KSHV Pr and AP polypeptides are predicted to contain 230 and 283 residues, respectively. The amino acid sequence of KSHV Pr has 56% identity with that of herpesvirus salmiri, the most similar virus by phylogenetic comparison. Pr is expressed in infected human cells as a late viral gene product, as suggested by RNA analysis of KSHV-infected BCBL-1 cells. Expression of the Pr domain in Escherichia coli yields an enzymatically active species, as determined by cleavage of synthetic peptide substrates, while an active-site mutant of this same domain yields minimal proteolytic activity. Sequence comparisons with human cytomegalovirus (HCMV) Pr permitted the identification of the catalytic residues, Ser114, His46, and His134, based on the known structure of the HCMV enzyme. The amino acid sequences of the release site of KSHV Pr (Tyr-Leu-Lys-Ala*Ser-Leu-Ile-Pro) and the maturation site (Arg-Leu-Glu-Ala*Ser-Ser-Arg-Ser) show that the extended substrate binding pocket differs from that of other members of the family. The conservation of amino acids known to be involved in the dimer interface region of HCMV Pr suggests that KSHV Pr assembles in a similar fashion. These features of the viral protease provide opportunities to develop specific inhibitors of its enzymatic activity.

Indexed as

Amino Acid SequenceAnimalsBase SequenceCell LineDNA, ViralHerpesvirus 8, HumanHumansMolecular Sequence DataProtein PrecursorsProteinsRNA, MessengerRNA, ViralSequence Homology, Amino AcidSerine EndopeptidasesTranscription, GeneticViral Proteinsassembly protein, Human herpesvirus 8DNA, Viralhuman herpesvirus 8 proteaseProtein PrecursorsProteinsRNA, MessengerRNA, ViralSerine EndopeptidasesViral Proteins

Identifiers

PMID9261433
PMCPMC191989
OpenAlexW2105917501

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.