Evidence map›Paper›PMID 32145686›Full record

ReviewCurrent opinion in structural biology2020

Monobodies as enabling tools for structural and mechanistic biology.

Oliver Hantschel, Matthew Biancalana, Shohei Koide

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing 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

33 citing papers in PubMed.

  1. Review
  2. Article
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  6. Review
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  9. Article
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  11. Article
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  14. Article
  15. Probing RAS Function Using Monobody and NanoBiT Technologies.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  16. Chimeric Protein Switch Biosensors.Advances in biochemical engineering/biotechnology · 2024
    Review
  17. Article
  18. Article
  19. Article
  20. 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.

Oliver HantschelInstitute of Physiological Chemistry, Faculty of Medicine, Philipps-University of Marburg, Karl-von-Frisch-Straße 1, 35032 Marburg, Germany; Swiss Institute for Experimental Cancer Research (ISREC), School of Life Sciences, École polytechnique fédérale de Lausanne (EPFL), Station 19, 1015 Lausanne, Switzerland. Electronic address: oliver.hantschel@uni-marburg.de.
Matthew BiancalanaLaura and Isaac Perlmutter Cancer Center, New York University Langone Health, 522 1st Avenue, New York, NY 10016, USA.
Shohei KoideLaura and Isaac Perlmutter Cancer Center, New York University Langone Health, 522 1st Avenue, New York, NY 10016, USA; Department of Medicine and Department of Biochemistry and Molecular Pharmacology, New York University School of Medicine, 522 1st Avenue, New York, NY 10016, USA. Electronic address: Shohei.Koide@nyumc.org.

Funding

Probing RAS-mediated Signaling with Monobody InhibitorsR01CA212608 · NCI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI SHOHEI KOIDE, John P O'Bryan · 2017 to 2026
$5.8M
Molecular mechanisms of SHP2 signaling dissected with designer binding proteinsR01CA194864 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI KOIDE, SHOHEI · 2016 to 2020
$1.8M
NCI NIH HHS R01 CA194864NCI NIH HHS R01 CA212608
6 · The paper itself

Abstract

Monobodies, built with the scaffold of the fibronectin type III domain, are among the most well-established synthetic binding proteins. They promote crystallization of challenging molecular systems. They have strong tendency to bind to functional sites and thus serve as drug-like molecules that perturb the biological functions of their targets. Monobodies lack disulfide bonds and thus they are particularly suited as genetically encoded reagents to be used intracellularly. This article reviews recent monobody-enabled studies that reveal new structures, molecular mechanisms and potential therapeutic opportunities. A systematic analysis of the crystal structures of monobody-target complexes suggests important attributes that make monobodies effective crystallization chaperones.

Indexed as

Crystallography, X-RayFibronectinsHumansProtein DomainsSingle-Domain AntibodiesFibronectinsSingle-Domain Antibodies

Identifiers

PMID32145686
PMCPMC7370805

What OpenQuestion holds

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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.