Evidence map›Paper›PMID 31457277›Full record

ArticleACS omega2017

Single-Molecule Force Spectroscopy Study on Modular Resilin Fusion Protein.

Alessandra Griffo, Hendrik Hähl, Samuel Grandthyll, Frank Müller, Arja Paananen, Marja Ilmén, Géza R Szilvay, Christopher P Landowski, Merja Penttilä, Karin Jacobs and 1 more

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in ACS omega, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.7field-weighted citation impact, top 26% 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

4 citing papers in PubMed, 13 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. 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

11 authors at 3 institutions in 2 countries.

Alessandra GriffoDepartment of Bioproducts and Biosystems BIO, Aalto University, P.O. Box 16100, FI-00076 Aalto, Finland.
Hendrik HählDepartment of Experimental Physics, Saarland University, 66123 Saarbrücken, Germany.
Samuel GrandthyllDepartment of Experimental Physics, Saarland University, 66123 Saarbrücken, Germany.
Frank MüllerDepartment of Experimental Physics, Saarland University, 66123 Saarbrücken, Germany.
Arja PaananenVTT Technical Research Centre of Finland, Tietotie 2, P.O. Box 1000, FI-02044 Espoo, Finland.
Marja IlménVTT Technical Research Centre of Finland, Tietotie 2, P.O. Box 1000, FI-02044 Espoo, Finland.
Géza R SzilvayVTT Technical Research Centre of Finland, Tietotie 2, P.O. Box 1000, FI-02044 Espoo, Finland.
Christopher P LandowskiVTT Technical Research Centre of Finland, Tietotie 2, P.O. Box 1000, FI-02044 Espoo, Finland.
Merja PenttiläDepartment of Bioproducts and Biosystems BIO, Aalto University, P.O. Box 16100, FI-00076 Aalto, Finland.
Karin JacobsDepartment of Experimental Physics, Saarland University, 66123 Saarbrücken, Germany.
Päivi LaaksonenDepartment of Bioproducts and Biosystems BIO, Aalto University, P.O. Box 16100, FI-00076 Aalto, Finland.
Tieto (Finland) · FISaarland University · DEAalto University · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The adhesive and mechanical properties of a modular fusion protein consisting of two different types of binding units linked together via a flexible resilin-like-polypeptide domain are quantified. The adhesive domains have been constructed from fungal cellulose-binding modules (CBMs) and an amphiphilic hydrophobin HFBI. This study is carried out by single-molecule force spectroscopy, which enables stretching of single molecules. The fusion proteins are designed to self-assemble on the cellulose surface, leading into the submonolayer of proteins having the HFBI pointing away from the surface. A hydrophobic atomic force microscopy (AFM) tip can be employed for contacting and lifting the single fusion protein from the HFBI-functionalized terminus by the hydrophobic interaction between the tip surface and the hydrophobic patch of the HFBI. The work of rupture, contour length at rupture and the adhesion forces of the amphiphilic end domains are evaluated under aqueous environment at different pHs.

Identifiers

PMID31457277
PMCPMC6644949
OpenAlexW2766027770

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.