Evidence map›Paper›PMID 33950384›Full record

ReviewMethods in molecular biology (Clifton, N.J.)2021

Methods for Molecular Modelling of Protein Complexes.

Tejashree Rajaram Kanitkar, Neeladri Sen, Sanjana Nair, Neelesh Soni, Kaustubh Amritkar, Yogendra Ramtirtha, M S Madhusudhan

Abstract readReview
PubMed Publisher
In one paragraph

Review in Methods in molecular biology (Clifton, N.J.), 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
6.3field-weighted citation impact, top 3% 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, 16 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. 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

7 authors at 1 institution in 1 country.

Tejashree Rajaram KanitkarIndian Institute of Science Education and Research Pune, Pashan, Pune, India.
Neeladri SenIndian Institute of Science Education and Research Pune, Pashan, Pune, India.
Sanjana NairIndian Institute of Science Education and Research Pune, Pashan, Pune, India.
Neelesh SoniIndian Institute of Science Education and Research Pune, Pashan, Pune, India.
Kaustubh AmritkarIndian Institute of Science Education and Research Pune, Pashan, Pune, India.
Yogendra RamtirthaIndian Institute of Science Education and Research Pune, Pashan, Pune, India.
M S MadhusudhanIndian Institute of Science Education and Research Pune, Pashan, Pune, India. madhusudhan@iiserpune.ac.in.
Indian Institute of Science Education and Research Pune · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Biological processes are often mediated by complexes formed between proteins and various biomolecules. The 3D structures of such protein-biomolecule complexes provide insights into the molecular mechanism of their action. The structure of these complexes can be predicted by various computational methods. Choosing an appropriate method for modelling depends on the category of biomolecule that a protein interacts with and the availability of structural information about the protein and its interacting partner. We intend for the contents of this chapter to serve as a guide as to what software would be the most appropriate for the type of data at hand and the kind of 3D complex structure required. Particularly, we have dealt with protein-small molecule ligand, protein-peptide, protein-protein, and protein-nucleic acid interactions.Most, if not all, model building protocols perform some sampling and scoring. Typically, several alternate conformations and configurations of the interactors are sampled. Each such sample is then scored for optimization. To boost the confidence in these predicted models, their assessment using other independent scoring schemes besides the inbuilt/default ones would prove to be helpful. This chapter also lists such software and serves as a guide to gauge the fidelity of modelled structures of biomolecular complexes.

Indexed as

Protein ConformationAlgorithmsComputational BiologyComputer SimulationLigandsMolecular Docking SimulationMultiprotein ComplexesNucleic AcidsPeptidesProtein BindingProtein Interaction Domains and MotifsSoftwareLigandsMultiprotein ComplexesNucleic AcidsPeptides3D structure modellingMolecular dockingProtein-biomolecular complexesScoring and sampling

Identifiers

PMID33950384
OpenAlexW3157915108

What OpenQuestion holds

Textmetadata
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.