Evidence map›Paper›PMID 34063488›Full record

ArticleMaterials (Basel, Switzerland)2021

Scaling Concepts in Serpin Polymer Physics.

Samuele Raccosta, Fabio Librizzi, Alistair M Jagger, Rosina Noto, Vincenzo Martorana, David A Lomas, James A Irving, Mauro Manno

Open access · goldAbstract read
In one paragraph

Article in Materials (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.3field-weighted citation impact, top 50% 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

3 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. αACS chemical neuroscience · 2023
    Article
  3. Neuroserpin: structure, function, physiology and pathology.Cellular and molecular life sciences : CMLS · 2021
    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

8 authors at 2 institutions in 2 countries.

Samuele RaccostaInstitute of Biophysics, National Research Council of Italy, via Ugo La Malfa 153, 90146 Palermo, Italy.ORCID 0000-0001-7775-5928
Fabio LibrizziInstitute of Biophysics, National Research Council of Italy, via Ugo La Malfa 153, 90146 Palermo, Italy.ORCID 0000-0003-4900-382X
Alistair M JaggerUCL Respiratory, University College London, 5 University Street, London WC1E 6JF, UK.ORCID 0000-0001-9680-254X
Rosina NotoInstitute of Biophysics, National Research Council of Italy, via Ugo La Malfa 153, 90146 Palermo, Italy.ORCID 0000-0001-6818-7981
Vincenzo MartoranaInstitute of Biophysics, National Research Council of Italy, via Ugo La Malfa 153, 90146 Palermo, Italy.ORCID 0000-0001-7092-6077
David A LomasUCL Respiratory, University College London, 5 University Street, London WC1E 6JF, UK.ORCID 0000-0003-2339-6979
James A IrvingUCL Respiratory, University College London, 5 University Street, London WC1E 6JF, UK.ORCID 0000-0003-3204-6356
Mauro MannoInstitute of Biophysics, National Research Council of Italy, via Ugo La Malfa 153, 90146 Palermo, Italy.ORCID 0000-0001-9843-0428
National Research Council · ITInstitute of Structural and Molecular Biology · GB

Funding

Medical Research Council MR/N024842/1
6 · The paper itself

Abstract

α1-Antitrypsin is a protease inhibitor belonging to the serpin family. Serpin polymerisation is at the core of a class of genetic conformational diseases called serpinopathies. These polymers are known to be unbranched, flexible, and heterogeneous in size with a beads-on-a-string appearance viewed by negative stain electron microscopy. Here, we use atomic force microscopy and time-lapse dynamic light scattering to measure polymer size and shape for wild-type (M) and Glu342→Lys (Z) α1-antitrypsin, the most common variant that leads to severe pathological deficiency. Our data for small polymers deposited onto mica and in solution reveal a power law relation between the polymer size, namely the end-to-end distance or the hydrodynamic radius, and the polymer mass, proportional to the contour length. We use the scaling concepts of polymer physics to assess that α1-antitrypsin polymers are random linear chains with a low persistence length.

Indexed as

atomic force microscopyconformational diseasedynamic light scatteringpolymer theoryserpin polymersserpins

Identifiers

PMID34063488
PMCPMC8156723
OpenAlexW3160205913

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.