Evidence map›Paper›PMID 30309962›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Discovery of a small-molecule inhibitor of specific serine residue BAD phosphorylation.

Vijay Pandey, Baocheng Wang, Chakrabhavi Dhananjaya Mohan, Ainiah Rushdiana Raquib, Shobith Rangappa, Venkatachalaiah Srinivasa, Julian E Fuchs, Kesturu S Girish, Tao Zhu, Andreas Bender and 5 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
2.6field-weighted citation impact, top 9% 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

38 citing papers in PubMed, 57 citations in OpenAlex.

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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

15 authors at 9 institutions in 4 countries.

Vijay PandeyTsinghua-Berkeley Shenzhen Institute, Tsinghua University, 518055 Shenzhen, Peoples' Republic of China.
Baocheng WangTsinghua-Berkeley Shenzhen Institute, Tsinghua University, 518055 Shenzhen, Peoples' Republic of China.
Chakrabhavi Dhananjaya MohanDepartment of Studies in Molecular Biology, University of Mysore, Manasagangotri, 570006 Mysore, India.
Ainiah Rushdiana RaquibCancer Science Institute of Singapore, National University of Singapore, 117599 Singapore.
Shobith RangappaAdichunchanagiri Institute for Molecular Medicine, BG Nagara, 571448 Karnataka, India.
Venkatachalaiah SrinivasaLaboratory of Chemical Biology, Department of Chemistry, Bangalore University, 560001 Bangalore, India.
Julian E FuchsCentre for Molecular Informatics, Department of Chemistry, University of Cambridge, Cambridge CB2 1TN, United Kingdom.
Kesturu S GirishDepartment of Studies and Research in Biochemistry, Tumkur University, 572103 Tumkur, India.
Tao ZhuHefei National Laboratory for Physical Sciences at Microscale, University of Science and Technology of China, 230026 Anhui, Peoples' Republic of China.
Andreas BenderCentre for Molecular Informatics, Department of Chemistry, University of Cambridge, Cambridge CB2 1TN, United Kingdom.
Lan MaTsinghua-Berkeley Shenzhen Institute, Tsinghua University, 518055 Shenzhen, Peoples' Republic of China.
Zhinan YinThe First Affiliated Hospital, Jinan University, 510632 Guangzhou, Peoples' Republic of China.
BasappaLaboratory of Chemical Biology, Department of Chemistry, Bangalore University, 560001 Bangalore, India; salundibasappa@gmail.com rangappaks@yahoo.com pelobie@sz.tsinghua.edu.cn.
Kanchugarakoppal S RangappaInstitution of Excellence, University of Mysore, Manasagangotri, 570006 Mysore, India salundibasappa@gmail.com rangappaks@yahoo.com pelobie@sz.tsinghua.edu.cn.
Peter E LobieTsinghua-Berkeley Shenzhen Institute, Tsinghua University, 518055 Shenzhen, Peoples' Republic of China; salundibasappa@gmail.com rangappaks@yahoo.com pelobie@sz.tsinghua.edu.cn.
University of Mysore · INTsinghua–Berkeley Shenzhen Institute · CNTsinghua University · CNUniversity of Cambridge · GBBangalore University · INNational University of Singapore · SGTumkur University · INTumor Hospital of Guangxi Medical University · CNUniversity of Science and Technology of China · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human BCL-2-associated death promoter (hBAD) is an apoptosis-regulatory protein mediating survival signals to carcinoma cells upon phosphorylation of Ser99, among other residues. Herein, we screened multiple small-molecule databases queried in a Laplacian-modified naive Bayesian-based cheminformatics platform and identified a Petasis reaction product as a site-specific inhibitor for hBAD phosphorylation. Based on apoptotic efficacy against mammary carcinoma cells,

Indexed as

Antineoplastic AgentsApoptosisbcl-Associated Death ProteinBenzamidesCell ProliferationCell SurvivalDatabases, FactualDrug Delivery SystemsDrug DiscoveryHumansMCF-7 CellsPhosphorylationPiperazinesRNA InterferenceSerineSmall Molecule LibrariesAntineoplastic AgentsBAD protein, humanbcl-Associated Death ProteinBenzamidesN-cyclopentyl-3-((4-(2,3-dichlorophenyl) piperazin-1-yl) (2-hydroxyphenyl) methyl) benzamidePiperazinesSerineSmall Molecule LibrariesAKT-PKBBAD phosphorylationcarcinomaLaplacian-modified naive Bayesian classifierNPB

Identifiers

PMID30309962
PMCPMC6217419
OpenAlexW2896536135

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.