Evidence map›Paper›PMID 38596743›Full record

ArticleJournal of applied crystallography2024

Timothy R Stachowski, Marcus Fischer

Abstract read
In one paragraph

Article in Journal of applied crystallography, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Review
  2. Article
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

2 authors.

Timothy R StachowskiDepartment of Chemical Biology and Therapeutics, St Jude Children's Research Hospital, Memphis, TN 38105, USA.ORCID https://orcid.org/0000-0002-6097-4857
Marcus FischerDepartment of Chemical Biology and Therapeutics, St Jude Children's Research Hospital, Memphis, TN 38105, USA.ORCID https://orcid.org/0000-0002-7179-2581

Funding

Exploiting Water Network Perturbations in Protein Binding SitesR35GM142772 · NIGMS · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI FISCHER, MARCUS · 2021 to 2025
$2.2M
NIGMS NIH HHS R35 GM142772
6 · The paper itself

Abstract

Proteins are well known 'shapeshifters' which change conformation to function. In crystallography, multiple conformational states are often present within the crystal and the resulting electron-density map. Yet, explicitly incorporating alternative states into models to disentangle multi-conformer ensembles is challenging. We previously reported the tool

Indexed as

conformational heterogeneityCootelectron-density mapsflexibilityFLEXRgraphical user interfacesmodel buildingmulti-conformer modelsproteins

Identifiers

PMID38596743
PMCPMC11001397

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.