Evidence map›Paper›PMID 23624418›Full record

ReviewAdvanced drug delivery reviews2013

Emerging mass spectrometry-based approaches to probe protein-receptor interactions: focus on overcoming physiological barriers.

Igor A Kaltashov, Cedric E Bobst, Son N Nguyen, Shunhai Wang

Abstract readReview
In one paragraph

Review in Advanced drug delivery reviews, 2013. 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. Hydrogen Exchange Mass Spectrometry.Methods in enzymology · 2016
    Article
  4. Article
  5. Article
  6. Article
  7. 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

4 authors.

Igor A KaltashovDepartment of Chemistry, University of Massachusetts-Amherst, Amherst, MA 01003, USA. Kaltashov@chem.umass.edu
Cedric E Bobst
Son N Nguyen
Shunhai Wang

Funding

PROTEIN FOLDING DYNAMICS BY MASS SPECTROMETRYR01GM061666 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI KALTASHOV, IGOR A · 2000 to 2013
$3.4M
NIGMS NIH HHS R01 GM061666
6 · The paper itself

Abstract

Physiological barriers, such as the blood-brain barrier and intestinal epithelial barrier, remain significant obstacles towards wider utilization of biopharmaceutical products. Receptor-mediated transcytosis has long been viewed as an attractive means of crossing such barriers, but successful exploitation of this route requires better understanding of the interactions between the receptors and protein-based therapeutics. Detailed characterization of such processes at the molecular level is challenging due to the very large physical size and heterogeneity of these species, which makes use of many state-of-the art analytical techniques, such as high-resolution NMR and X-ray crystallography impractical. Mass spectrometry has emerged in the past decade as a powerful tool to study protein-receptor interactions, although its applications to investigate interaction of biopharmaceuticals with their physiological partners are still limited. We highlight the potential of this technique by considering several recent examples where it had been instrumental for understanding molecular mechanisms critical for receptor-mediated transcytosis of transferrin-based therapeutics.

Indexed as

Biological TransportBlood-Brain BarrierIntestinal MucosaMass SpectrometryMuramidaseProtein BindingReceptors, Cell SurfaceTransferrinMuramidaseReceptors, Cell SurfaceTransferrinBBBBlood–brain barriercentral nervous systemcerebrospinal fluidCNSCSFelectrospray ionizationESIFusion proteinsGHTGrowth hormonegrowth hormone-transferrin fusion proteinHDXhydrogen/deuterium exchangeIntestinal epithelial barrierlysozymeLysozymelysozyme–transferrin conjugateLzLzTmass spectrometryMSProtein aggregationProtein–drug conjugateProtein therapeuticsReceptor-mediated transcytosisTfTfRtransferrinTransferrintransferrin receptorTransferrin receptor

Identifiers

PMID23624418
PMCPMC3737317

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.