Evidence map›Paper›PMID 26677230›Full record

ReviewThe Journal of biological chemistry2016

Nanobodies as Probes for Protein Dynamics in Vitro and in Cells.

Oleg Y Dmitriev, Svetlana Lutsenko, Serge Muyldermans

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
10.3field-weighted citation impact, top 1% 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

48 citing papers in PubMed, 98 citations in OpenAlex.

  1. Review
  2. Review
  3. Structural insights into the role and targeting of EGFRvIII.Structure (London, England : 1993) · 2024
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Biomarkers and Detection Platforms for Human Health and Performance Monitoring: A Review.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022
    Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Direct Immobilization of Engineered Nanobodies on Gold Sensors.ACS applied materials & interfaces · 2021
    Article
  16. 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 at 3 institutions in 3 countries.

Oleg Y DmitrievFrom the Department of Biochemistry, University of Saskatchewan, Saskatoon, Saskatchewan S7N 5E5, Canada, Oleg.Dmitriev@usask.ca.
Svetlana Lutsenkothe Department of Physiology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, and.
Serge Muyldermansthe Unit of Cellular and Molecular Immunology, Vrije Universiteit Brussel, 1050, Brussels, Belgium.
Johns Hopkins Medicine · USUniversity of Saskatchewan · CAVrije Universiteit Brussel · BE

Funding

The role of transferrin receptor 2 in iron homeostasisP01GM067166 · NIGMS · OREGON HEALTH & SCIENCE UNIVERSITY · PI UNGER, VINZENZ · 2003 to 2013
$14.6M
Translational Research Enhancement CoreP30DK089502 · NIDDK · JOHNS HOPKINS UNIVERSITY · PI ZACHOS, NICHOLAS CONSTANTINE · 2011 to 2020
$12.0M
Canadian Institutes of Health ResearchNIDDK NIH HHS P30 DK089502NIGMS NIH HHS GM067166NIGMS NIH HHS P01 GM067166
6 · The paper itself

Abstract

Nanobodies are the recombinant antigen-recognizing domains of the minimalistic heavy chain-only antibodies produced by camels and llamas. Nanobodies can be easily generated, effectively optimized, and variously derivatized with standard molecular biology protocols. These properties have triggered the recent explosion in the nanobody use in basic and clinical research. This review focuses on the emerging use of nanobodies for understanding and monitoring protein dynamics on the scales ranging from isolated protein domains to live cells, from nanoseconds to hours. The small size and high solubility make nanobodies uniquely suited for studying protein dynamics by NMR. The ability to produce conformation-sensitive nanobodies in cells enables studies that link structural dynamics of a target protein to its cellular behavior. The link between in vitro and in-cell dynamics, afforded by nanobodies, brings the analysis of such important events as receptor signaling, membrane protein trafficking, and protein interactions to the next level of resolution.

Indexed as

AnimalsHumansMembrane ProteinsMolecular ProbesNuclear Magnetic Resonance, BiomolecularProtein Structure, TertiaryProtein TransportSignal TransductionSingle-Domain AntibodiesMembrane ProteinsMolecular ProbesSingle-Domain Antibodiesnanobodynuclear magnetic resonance (NMR)protein domainprotein dynamicprotein dynamicsprotein engineeringprotein structuresingle-domain antibody (sdAb, nanobody)X-ray crystallography

Identifiers

PMID26677230
PMCPMC4759159
OpenAlexW2214960714

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.