Evidence map›Paper›PMID 28525590›Full record

ArticleNucleic acids research2017

SDM: a server for predicting effects of mutations on protein stability.

Arun Prasad Pandurangan, Bernardo Ochoa-Montaño, David B Ascher, Tom L Blundell

Open access · goldAbstract readValidation Study
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 263 papers.

0numbers the graph read from it
0cells of the map it votes in
263citing papers in PubMed
23.2field-weighted citation impact, top 1% 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

263 citing papers in PubMed, 528 citations in OpenAlex.

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203 more citing papers are in PubMed but not listed here.

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

4 authors at 2 institutions in 2 countries.

Arun Prasad PanduranganDepartment of Biochemistry, University of Cambridge, Cambridge CB2 1GA, UK.
Bernardo Ochoa-MontañoDepartment of Biochemistry, University of Cambridge, Cambridge CB2 1GA, UK.
David B AscherDepartment of Biochemistry, University of Cambridge, Cambridge CB2 1GA, UK.
Tom L BlundellDepartment of Biochemistry, University of Cambridge, Cambridge CB2 1GA, UK.
University of Cambridge · GBThe University of Melbourne · AU

Funding

Medical Research Council MR/M026302/1Medical Research Council MR/N501864/1
6 · The paper itself

Abstract

Here, we report a webserver for the improved SDM, used for predicting the effects of mutations on protein stability. As a pioneering knowledge-based approach, SDM has been highlighted as the most appropriate method to use in combination with many other approaches. We have updated the environment-specific amino-acid substitution tables based on the current expanded PDB (a 5-fold increase in information), and introduced new residue-conformation and interaction parameters, including packing density and residue depth. The updated server has been extensively tested using a benchmark containing 2690 point mutations from 132 different protein structures. The revised method correlates well against the hypothetical reverse mutations, better than comparable methods built using machine-learning approaches, highlighting the strength of our knowledge-based approach for identifying stabilising mutations. Given a PDB file (a Protein Data Bank file format containing the 3D coordinates of the protein atoms), and a point mutation, the server calculates the stability difference score between the wildtype and mutant protein. The server is available at http://structure.bioc.cam.ac.uk/sdm2.

Indexed as

Point MutationProtein StabilitySoftwareAmino Acid SubstitutionInternetThermodynamics

Identifiers

PMID28525590
PMCPMC5793720
OpenAlexW2615841538

What Socratic 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 Socratic graph.