Evidence map›Paper›PMID 19326112›Full record

ArticleEuropean biophysics journal : EBJ2010

Identification of the folding inhibitors of hen-egg lysozyme: gathering the right tools.

Martina Caldarini, Ludovico Sutto, Carlo Camilloni, Francesca Vasile, Ricardo A Broglia, Guido Tiana

Abstract read
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In one paragraph

Article in European biophysics journal : EBJ, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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

6 authors.

Martina CaldariniDipartimento di Fisica, Universitá di Milano, via Celoria 16, Milan, Italy.
Ludovico Sutto
Carlo Camilloni
Francesca Vasile
Ricardo A Broglia
Guido Tiana

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The unfolded state of proteins displays a surprisingly rich amount of local native structure, which appears to be critical for driving the protein to its native state. Peptides with the same sequence of the corresponding structured segments can be used to interfere with the correct folding of the protein. Using model simulations, we investigate the folding of hen-egg lysozyme, identifying its key segments. Activity assays, NMR and circular dichroism experiments are used to screen the peptides which are able to inhibit the folding of lysozyme. Few peptides, corresponding to the segments of the protein which are structured in the unfolded state, are identified to have significant inhibitory effects.

Indexed as

Amino Acid SequenceAnimalsCircular DichroismCrystallography, X-RayMagnetic Resonance SpectroscopyMuramidaseProtein ConformationProtein Foldinghen egg lysozymeMuramidase

Identifiers

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.