Evidence map›Paper›PMID 30562001›Full record

ArticleBiochemistry2019

Tuning Protein Diffusivity with Membrane Tethers.

David Mörsdorf, Patrick Müller

Abstract read
In one paragraph

Article in Biochemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Exploring cellular biochemistry with nanobodies.The Journal of biological chemistry · 2020
    Review
  6. Article
  7. 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.

David MörsdorfFriedrich Miescher Laboratory of the Max Planck Society , Max-Planck-Ring 9 , 72076 Tübingen , Germany.ORCID 0000-0001-8982-2155
Patrick MüllerFriedrich Miescher Laboratory of the Max Planck Society , Max-Planck-Ring 9 , 72076 Tübingen , Germany.ORCID 0000-0002-0702-6209

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Diffusion is essential for biochemical processes because it dominates molecular movement on small scales. Enzymatic reactions, for example, require fast exchange of substrate and product molecules in the local environment of the enzyme to ensure efficient turnover. On larger spatial scales, diffusion of secreted signaling proteins is thought to limit the spatial extent of tissue differentiation during embryonic development. While it is possible to measure diffusion in vivo, specifically interfering with diffusion processes and testing diffusion models directly remains challenging. The development of genetically encoded nanobodies that bind specific proteins has provided the opportunity to alter protein localization and reduce protein mobility. Here, we extend the nanobody toolbox with a membrane-tethered low-affinity diffusion regulator that can be used to tune the effective diffusivity of extracellular molecules over an order of magnitude in living embryos. This opens new avenues for future applications to functionally interfere with diffusion-dependent processes.

Indexed as

AnimalsAnimals, Genetically ModifiedBiochemistryCell MembraneDiffusionDrosophila ProteinsEmbryo, NonmammalianGreen Fluorescent ProteinsImmobilized ProteinsLuminescent ProteinsProteinsRed Fluorescent ProteinSignal TransductionSingle-Domain AntibodiesZebrafishdpp protein, DrosophilaDrosophila ProteinsGreen Fluorescent ProteinsImmobilized ProteinsLuminescent ProteinsProteinsRed Fluorescent ProteinSingle-Domain Antibodies

Identifiers

PMID30562001
PMCPMC6344912

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.