Evidence map›Paper›PMID 23023928›Full record

ReviewBiopolymers2013

Studying and polishing the PDB's macromolecules.

Jane S Richardson, David C Richardson

Abstract readReview
In one paragraph

Review in Biopolymers, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Crystal structures of main protease (MMolecular biomedicine · 2023
    Article
  2. Article
  3. A rotamer library to enable modeling and design of peptoid foldamers.Journal of the American Chemical Society · 2014
    Article
  4. Article
  5. Article
  6. Seeing the PDB.The Journal of biological chemistry
    Review
  7. 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.

Jane S RichardsonDepartment of Biochemistry, Duke University, Durham, North Carolina, USA. jsr@kinemage.biochem.duke.edu
David C Richardson

Funding

MolProbity Validation & Corrections: for Crystallography, PDB & BiomedicineR01GM073919 · NIGMS · DUKE UNIVERSITY · PI RICHARDSON, DAVID CLAUDE · 2006 to 2018
$3.7M
New Kind of Quality Management for X-ray &NMR ModelsR01GM073930 · NIGMS · DUKE UNIVERSITY · PI RICHARDSON, DAVID CLAUDE · 2005 to 2013
$2.3M
CRYSTALLOGRAPHIC ANALYSIS OF PROTEIN STRUCTURESR01GM015000 · NIGMS · DUKE UNIVERSITY · PI RICHARDSON, DAVID C. · 1985 to 2002
$1.0M
NIGMS NIH HHS GM073919NIGMS NIH HHS GM073930NIGMS NIH HHS GM15000NIGMS NIH HHS R01 GM015000NIGMS NIH HHS R01 GM073919NIGMS NIH HHS R01 GM073930
6 · The paper itself

Abstract

Macromolecular crystal structures are among the best of scientific data, providing detailed insight into these complex and biologically important molecules with a relatively low level of error and subjectivity. However, there are two notable problems with getting the most information from them. The first is that the models are not perfect: there is still opportunity for improving them, and users need to evaluate whether the local reliability in a structure is up to answering their question of interest. The second is that protein and nucleic acid molecules are highly complex and individual, inherently handed and three-dimensional, and the cooperative and subtle interactions that govern their detailed structure and function are not intuitively evident. Thus there is a real need for graphical representations and descriptive classifications that enable molecular 3D literacy. We have spent our career working to understand these elegant molecules ourselves, and building tools to help us and others determine and understand them better. The Protein Data Bank (PDB) has of course been vital and central to this undertaking. Here we combine some history of our involvement as depositors, illustrators, evaluators, and end-users of PDB structures with commentary on how best to study and draw scientific inferences from them.

Indexed as

Databases, ProteinModels, MolecularCrystallography, X-RayMacromolecular SubstancesMicrococcal NucleaseProteinsStaphylococcaceaeMacromolecular SubstancesMicrococcal NucleaseProteins

Identifiers

PMID23023928
PMCPMC3535681

What OpenQuestion 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 OpenQuestion graph.