Evidence map›Paper›PMID 25443957›Full record

ReviewAdvances in protein chemistry and structural biology2014

Recent advances in transferable coarse-grained modeling of proteins.

Parimal Kar, Michael Feig

Abstract readReview
In one paragraph

Review in Advances in protein chemistry and structural biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. One bead per residue can describe all-atom protein structures.Structure (London, England : 1993) · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Computational and structural biotechnology journal · 2022
    Review
  14. Review
  15. Article
  16. Article
  17. Consistent Force Field Captures Homologue-Resolved HP1 Phase Separation.Journal of chemical theory and computation · 2021
    Article
  18. Temperature and Phase Transferable Bottom-up Coarse-Grained Models.Journal of chemical theory and computation · 2020
    Article
  19. Article
  20. Whole-Cell Models and Simulations in Molecular Detail.Annual review of cell and developmental biology · 2019
    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

2 authors.

Parimal KarDepartment of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan, USA.
Michael FeigDepartment of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan, USA; Department of Chemistry, Michigan State University, East Lansing, Michigan, USA. Electronic address: feig@msu.edu.

Funding

Protein structure refinement through effective sampling and scoringR01GM084953 · NIGMS · MICHIGAN STATE UNIVERSITY · PI FEIG, MICHAEL · 2008 to 2017
$2.5M
Multiscale modeling of supramolecular protein-DNA assembliesR01GM092949 · NIGMS · MICHIGAN STATE UNIVERSITY · PI FEIG, MICHAEL · 2010 to 2013
$1.1M
NIGMS NIH HHS GM084953NIGMS NIH HHS GM092949NIGMS NIH HHS R01 GM084953NIGMS NIH HHS R01 GM092949
6 · The paper itself

Abstract

Computer simulations are indispensable tools for studying the structure and dynamics of biological macromolecules. Biochemical processes occur on different scales of length and time. Atomistic simulations cannot cover the relevant spatiotemporal scales at which the cellular processes occur. To address this challenge, coarse-grained (CG) modeling of the biological systems is employed. Over the last few years, many CG models for proteins continue to be developed. However, many of them are not transferable with respect to different systems and different environments. In this review, we discuss those CG protein models that are transferable and that retain chemical specificity. We restrict ourselves to CG models of soluble proteins only. We also briefly review recent progress made in the multiscale hybrid all-atom/CG simulations of proteins.

Indexed as

Molecular Dynamics SimulationThermodynamicsAnimalsHumansModels, MolecularProtein ConformationProteinsSolventsProteinsSolventsCoarse grainingForce fieldMolecular dynamicsMultiscaleProtein foldingProtein–protein interactions

Identifiers

PMID25443957
PMCPMC5366245

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Registered trials

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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.