Evidence map›Paper›PMID 33450915›Full record

ArticleMolecules (Basel, Switzerland)2021

Specificity of Molecular Fragments Binding to S100B versus S100A1 as Identified by NMR and Site Identification by Ligand Competitive Saturation (SILCS).

Brianna D Young, Wenbo Yu, Darex J Vera Rodríguez, Kristen M Varney, Alexander D MacKerell, David J Weber

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

5 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Article
  3. The S100B Protein: A Multifaceted Pathogenic Factor More Than a Biomarker.International journal of molecular sciences · 2023
    Review
  4. Computer-Aided Drug Design: An Update.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  5. 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

6 authors at 1 institution in 1 country.

Brianna D YoungDepartment of Biochemistry and Molecular Biology, University of Maryland School of Medicine, 108 N. Greene St., Baltimore, MD 21201, USA.ORCID 0000-0002-7742-8860
Wenbo YuCenter for Biomolecular Therapeutics (CBT), Baltimore, MD 21201, USA.ORCID 0000-0001-6962-5314
Darex J Vera RodríguezDepartment of Biochemistry and Molecular Biology, University of Maryland School of Medicine, 108 N. Greene St., Baltimore, MD 21201, USA.
Kristen M VarneyDepartment of Biochemistry and Molecular Biology, University of Maryland School of Medicine, 108 N. Greene St., Baltimore, MD 21201, USA.
Alexander D MacKerellCenter for Biomolecular Therapeutics (CBT), Baltimore, MD 21201, USA.ORCID 0000-0001-8287-6804
David J WeberDepartment of Biochemistry and Molecular Biology, University of Maryland School of Medicine, 108 N. Greene St., Baltimore, MD 21201, USA.ORCID 0000-0002-8824-1110
University of Maryland, Baltimore · US

Funding

Interdisciplinary Training Program Muscle BiologyT32AR007592 · NIAMS · UNIVERSITY OF MARYLAND BALTIMORE · PI Aikaterini Kontrogianni-Konstantopoulos · 1996 to 2026
$11.7M
Macromolecular Conformational HeterogeneityR35GM131710 · NIGMS · UNIVERSITY OF MARYLAND BALTIMORE · PI ALEXANDER D MACKERELL · 2019 to 2026
$6.2M
Signal Propagation in Protein Allostery: Mechanism and EvolutionR01GM129327 · NIGMS · UNIV OF MARYLAND, COLLEGE PARK · PI WEBER, DAVID JOSEPH · 2019 to 2022
$1.3M
NIAMS NIH HHS T32 AR007592NIGMS NIH HHS R01 GM129327NIGMS NIH HHS R35 GM131710NIH HHS CA107999
6 · The paper itself

Abstract

S100B, a biomarker of malignant melanoma, interacts with the p53 protein and diminishes its tumor suppressor function, which makes this S100 family member a promising therapeutic target for treating malignant melanoma. However, it is a challenge to design inhibitors that are specific for S100B in melanoma versus other S100-family members that are important for normal cellular activities. For example, S100A1 is most similar in sequence and structure to S100B, and this S100 protein is important for normal skeletal and cardiac muscle function. Therefore, a combination of NMR and computer aided drug design (CADD) was used to initiate the design of specific S100B inhibitors. Fragment-based screening by NMR, also termed "SAR by NMR," is a well-established method, and was used to examine spectral perturbations in 2D [

Indexed as

Nuclear Magnetic Resonance, BiomolecularCompetitive BiddingHumansLigandsS100 Calcium Binding Protein beta SubunitS100 ProteinsSmall Molecule LibrariesLigandsS100A1 proteinS100B protein, humanS100 Calcium Binding Protein beta SubunitS100 ProteinsSmall Molecule LibrariescalciumNMRS100A1S100BSILCS

Identifiers

PMID33450915
PMCPMC7828390
OpenAlexW3118401492

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.