Evidence map›Paper›PMID 33539887›Full record

ArticleJournal of molecular biology2021

ADDRESS: A Database of Disease-associated Human Variants Incorporating Protein Structure and Folding Stabilities.

Jaie Woodard, Chengxin Zhang, Yang Zhang

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

16 citing papers in PubMed, 26 citations in OpenAlex.

  1. MAVISp: A modular structure-based framework for protein variant effects.Protein science : a publication of the Protein Society · 2026
    Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Recent Progress of Protein Tertiary Structure Prediction.Molecules (Basel, Switzerland) · 2024
    Review
  9. Review
  10. On the linkage of thermodynamics and pathogenicity.Current opinion in structural biology · 2023
    Review
  11. Article
  12. Article
  13. How Functional Genomics Can Keep Pace With VUS Identification.Frontiers in cardiovascular medicine · 2022
    Review
  14. Article
  15. Article
  16. Toward the solution of the protein structure prediction problem.The Journal of biological chemistry · 2021
    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

3 authors at 1 institution in 1 country.

Jaie WoodardDepartment of Computational Medicine and Bioinformatics, University of Michigan, Ann Arbor, MI 48109, USA.
Chengxin ZhangDepartment of Computational Medicine and Bioinformatics, University of Michigan, Ann Arbor, MI 48109, USA.
Yang ZhangDepartment of Computational Medicine and Bioinformatics, University of Michigan, Ann Arbor, MI 48109, USA; Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA. Electronic address: zhng@umich.edu.
University of Michigan · US

Funding

Structure-based functional annotation of microbial genomesR01AI134678 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Lydia Petra Freddolino, SCOTT J. HULTGREN · 2018 to 2026
$6.5M
Advanced approaches to protein structure predictionR35GM136422 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI ZHANG, YANG · 2020 to 2021
$946k
High-Performance Computing Cluster for Biomedical ResearchS10OD026825 · OD · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI ATHEY, BRIAN DAVID · 2020 to 2020
$600k
NIAID NIH HHS R01 AI134678NIGMS NIH HHS R35 GM136422NIH HHS S10 OD026825
6 · The paper itself

Abstract

Numerous human diseases are caused by mutations in genomic sequences. Since amino acid changes affect protein function through mechanisms often predictable from protein structure, the integration of structural and sequence data enables us to estimate with greater accuracy whether and how a given mutation will lead to disease. Publicly available annotated databases enable hypothesis assessment and benchmarking of prediction tools. However, the results are often presented as summary statistics or black box predictors, without providing full descriptive information. We developed a new semi-manually curated human variant database presenting information on the protein contact-map, sequence-to-structure mapping, amino acid identity change, and stability prediction for the popular UniProt database. We found that the profiles of pathogenic and benign missense polymorphisms can be effectively deduced using decision trees and comparative analyses based on the presented dataset. The database is made publicly available through https://zhanglab.ccmb.med.umich.edu/ADDRESS.

Indexed as

Databases, ProteinGenetic VariationProtein FoldingAmino AcidsDiseaseHumansPolymorphism, Single NucleotideProteinsProtein StabilityUser-Computer InterfaceAmino AcidsProteinsdatabasedisease variantpathogenicity predictionSingle-nucleotide polymorphism

Identifiers

PMID33539887
PMCPMC8119349
OpenAlexW3127266583

What Socratic holds

Textmetadata
LicenceTDM
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 Socratic graph.