Evidence map›Paper›PMID 24699145›Full record

ArticleMolecules (Basel, Switzerland)2014

PBDE: structure-activity studies for the inhibition of hepatitis C virus NS3 helicase.

Kazi Abdus Salam, Atsushi Furuta, Naohiro Noda, Satoshi Tsuneda, Yuji Sekiguchi, Atsuya Yamashita, Kohji Moriishi, Masamichi Nakakoshi, Hidenori Tani, Sona Rani Roy and 3 more

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.6field-weighted citation impact, top 32% 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

6 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
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

13 authors at 7 institutions in 1 country.

Kazi Abdus SalamRadioisotope Center, The University of Tokyo, 2-11-16 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan. salam_bio26@yahoo.com.
Atsushi FurutaDepartment of Life Science and Medical Bioscience, Waseda University, 2-2 Wakamatsu-cho, Shinjuku-ku, Tokyo 162-8480, Japan. atsushi.5961@ruri.waseda.jp.
Naohiro NodaDepartment of Life Science and Medical Bioscience, Waseda University, 2-2 Wakamatsu-cho, Shinjuku-ku, Tokyo 162-8480, Japan. noda-naohiro@aist.go.jp.
Satoshi TsunedaDepartment of Life Science and Medical Bioscience, Waseda University, 2-2 Wakamatsu-cho, Shinjuku-ku, Tokyo 162-8480, Japan. stsuneda@waseda.jp.
Yuji SekiguchiBiomedical Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), 1-1-1 Higashi, Tsukuba, Ibaraki 305-8566, Japan. y.sekiguchi@aist.go.jp.
Atsuya YamashitaDepartment of Microbiology, Graduate School of Medicine and Engineering, University of Yamanashi, 1110 Shimokato, Chuo-shi, Yamanashi 409-3898, Japan. atsuyay@yamanashi.ac.jp.
Kohji MoriishiDepartment of Microbiology, Graduate School of Medicine and Engineering, University of Yamanashi, 1110 Shimokato, Chuo-shi, Yamanashi 409-3898, Japan. kmoriishi@yamanashi.ac.jp.
Masamichi NakakoshiFaculty of Pharmaceutical Sciences, Toho University, 2-2-1 Miyama, Funabashi, Chiba 274-8510, Japan. nakakoshi@phar.toho-u.ac.jp.
Hidenori TaniResearch Institute for Environmental Management Technology, National Institute of Advanced Industrial Science and Technology (AIST), 16-1, Onogawa, Tsukuba, Ibaraki 305-8569, Japan. h.tani@aist.go.jp.
Sona Rani RoyDepartment of Chemistry, Biology and Marine Science, University of the Ryukyus, Nishihara, Okinawa 903-0213, Japan. sonarroy@gmail.com.
Junichi TanakaDepartment of Chemistry, Biology and Marine Science, University of the Ryukyus, Nishihara, Okinawa 903-0213, Japan. jtanaka@sci.u-ryukyu.ac.jp.
Masayoshi TsubukiInstitute of Medical Chemistry, Hoshi University, Ebara 2-4-41, Shinagawa-ku, Tokyo 142-8501, Japan. tsubuki@hoshi.ac.jp.
Nobuyoshi AkimitsuRadioisotope Center, The University of Tokyo, 2-11-16 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan. akimitsu@ric.u-tokyo.ac.jp.
Waseda University · JPNational Institute of Advanced Industrial Science and Technology · JPThe University of Tokyo · JPUniversity of the Ryukyus · JPUniversity of Yamanashi Hospital · JPHoshi University · JPToho University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The helicase portion of the hepatitis C virus nonstructural protein 3 (NS3) is considered one of the most validated targets for developing direct acting antiviral agents. We isolated polybrominated diphenyl ether (PBDE) 1 from a marine sponge as an NS3 helicase inhibitor. In this study, we evaluated the inhibitory effects of PBDE (1) on the essential activities of NS3 protein such as RNA helicase, ATPase, and RNA binding activities. The structure-activity relationship analysis of PBDE (1) against the HCV ATPase revealed that the biphenyl ring, bromine, and phenolic hydroxyl group on the benzene backbone might be a basic scaffold for the inhibitory potency.

Indexed as

Adenosine TriphosphatasesAnimalsAntiviral AgentsDEAD-box RNA HelicasesEnzyme InhibitorsHalogenated Diphenyl EthersHepacivirusHumansNucleoside-TriphosphatasePoriferaRNA HelicasesSerine EndopeptidasesStructure-Activity RelationshipViral Nonstructural ProteinsViral ProteasesAdenosine TriphosphatasesAntiviral AgentsDEAD-box RNA HelicasesEnzyme InhibitorsHalogenated Diphenyl EthersNS3 protein, hepatitis C virusNucleoside-TriphosphataseRNA HelicasesSerine EndopeptidasesViral Nonstructural ProteinsViral Proteases

Identifiers

PMID24699145
PMCPMC6271602
OpenAlexW1989121125

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.