Evidence map›Paper›PMID 18058125›Full record

ReviewPflugers Archiv : European journal of physiology2008

Pulling single molecules of titin by AFM--recent advances and physiological implications.

Wolfgang A Linke, Anika Grützner

Open access · bronzeAbstract readReview
PubMed Publisher
In one paragraph

Review in Pflugers Archiv : European journal of physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
8.1field-weighted citation impact, top 2% 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

39 citing papers in PubMed, 121 citations in OpenAlex.

  1. Article
  2. Computed Vibrational Heat Capacities for Gas-Phase Biomolecular Ions.Journal of the American Society for Mass Spectrometry · 2025
    Article
  3. Article
  4. Amyloidogenesis: What Do We Know So Far?International journal of molecular sciences · 2022
    Review
  5. Article
  6. Article
  7. Review
  8. A multiscale sliding filament model of lymphatic muscle pumping.Biomechanics and modeling in mechanobiology · 2021
    Article
  9. Article
  10. Article
  11. Force generation by titin folding.Protein science : a publication of the Protein Society · 2017
    Article
  12. A HaloTag Anchored Ruler for Week-Long Studies of Protein Dynamics.Journal of the American Chemical Society · 2016
    Article
  13. Article
  14. Probing muscle ankyrin-repeat protein (MARP) structure and function.Anatomical record (Hoboken, N.J. : 2007) · 2014
    Article
  15. Article
  16. Mechano-signaling in heart failure.Pflugers Archiv : European journal of physiology · 2014
    Review
  17. Article
  18. Article
  19. Article
  20. Mechanical unfolding studies of protein molecules.Biophysics (Nagoya-shi, Japan) · 2012
    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 at 1 institution in 1 country.

Wolfgang A LinkePhysiology and Biophysics Unit, University of Muenster, Schlossplatz 5, 48149 Muenster, Germany. wlinke@uni-muenster.de
Anika Grützner
University of Münster · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Perturbation of a protein away from its native state by mechanical stress is a physiological process immanent to many cells. The mechanical stability and conformational diversity of proteins under force therefore are important parameters in nature. Molecular-level investigations of "mechanical proteins" have enjoyed major breakthroughs over the last decade, a development to which atomic force microscopy (AFM) force spectroscopy has been instrumental. The giant muscle protein titin continues to be a paradigm model in this field. In this paper, we review how single-molecule mechanical measurements of titin using AFM have served to elucidate key aspects of protein unfolding-refolding and mechanisms by which biomolecular elasticity is attained. We outline recent work combining protein engineering and AFM force spectroscopy to establish the mechanical behavior of titin domains using molecular "fingerprinting." Furthermore, we summarize AFM force-extension data demonstrating different mechanical stabilities of distinct molecular-spring elements in titin, compare AFM force-extension to novel force-ramp/force-clamp studies, and elaborate on exciting new results showing that AFM force clamp captures the unfolding and refolding trajectory of single mechanical proteins. Along the way, we discuss the physiological implications of the findings, not least with respect to muscle mechanics. These studies help us understand how proteins respond to forces in cells and how mechanosensing and mechanosignaling events may proceed in vivo.

Indexed as

Microscopy, Atomic ForceAnimalsBiomechanical PhenomenaConnectinElasticityHumansMolecular StructureMuscle ProteinsProtein FoldingProtein KinasesSarcomeresConnectinMuscle ProteinsProtein KinasesTTN protein, human

Identifiers

PMID18058125
OpenAlexW1972210588

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.