Evidence map›Paper›PMID 27668215›Full record

ReviewFrontiers in molecular biosciences2016

Identifying and Visualizing Macromolecular Flexibility in Structural Biology.

Martina Palamini, Anselmo Canciani, Federico Forneris

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in molecular biosciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
7.3field-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

27 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Modeling of Protein Complexes.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  9. Article
  10. Leveraging intrinsic flexibility to engineer enhanced enzyme catalytic activity.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  11. Review
  12. Wavelet invariants for statistically robust multi-reference alignment.Information and inference : a journal of the IMA · 2021
    Article
  13. Identifying the origin of local flexibility in a carbohydrate polymer.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  14. Article
  15. Article
  16. Light-coupled cryo-plunger for time-resolved cryo-EM.Journal of structural biology · 2020
    Article
  17. Discriminating changes in protein structure using tyrosine conjugation.Protein science : a publication of the Protein Society · 2020
    Article
  18. Article
  19. Review
  20. Probing the Structural Dynamics of theFrontiers in molecular biosciences · 2020
    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

3 authors at 1 institution in 1 country.

Martina PalaminiThe Armenise-Harvard Laboratory of Structural Biology, Department of Biology and Biotechnology, University of Pavia Pavia, Italy.
Anselmo CancianiThe Armenise-Harvard Laboratory of Structural Biology, Department of Biology and Biotechnology, University of Pavia Pavia, Italy.
Federico FornerisThe Armenise-Harvard Laboratory of Structural Biology, Department of Biology and Biotechnology, University of Pavia Pavia, Italy.
University of Pavia · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Structural biology comprises a variety of tools to obtain atomic resolution data for the investigation of macromolecules. Conventional structural methodologies including crystallography, NMR and electron microscopy often do not provide sufficient details concerning flexibility and dynamics, even though these aspects are critical for the physiological functions of the systems under investigation. However, the increasing complexity of the molecules studied by structural biology (including large macromolecular assemblies, integral membrane proteins, intrinsically disordered systems, and folding intermediates) continuously demands in-depth analyses of the roles of flexibility and conformational specificity involved in interactions with ligands and inhibitors. The intrinsic difficulties in capturing often subtle but critical molecular motions in biological systems have restrained the investigation of flexible molecules into a small niche of structural biology. Introduction of massive technological developments over the recent years, which include time-resolved studies, solution X-ray scattering, and new detectors for cryo-electron microscopy, have pushed the limits of structural investigation of flexible systems far beyond traditional approaches of NMR analysis. By integrating these modern methods with powerful biophysical and computational approaches such as generation of ensembles of molecular models and selective particle picking in electron microscopy, more feasible investigations of dynamic systems are now possible. Using some prominent examples from recent literature, we review how current structural biology methods can contribute useful data to accurately visualize flexibility in macromolecular structures and understand its important roles in regulation of biological processes.

Indexed as

cryo-electron microscopyensemblesmolecular recognitionnuclear magnetic resonanceprotein flexibilitySmall-angle scatteringstructural biologyX-ray crystallography

Identifiers

PMID27668215
PMCPMC5016524
OpenAlexW2515002494

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.