Evidence map›Paper›PMID 23179057›Full record

ArticleBiomolecular NMR assignments2013

¹H, ¹³C and ¹⁵N resonance assignments of human BASP1.

Leonhard Geist, Anna Zawadzka-Kazimierczuk, Saurabh Saxena, Szymon Żerko, Wiktor Koźmiński, Robert Konrat

Open access · hybridAbstract read
In one paragraph

Article in Biomolecular NMR assignments, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.7field-weighted citation impact, top 31% 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

6 citing papers in PubMed, 9 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Protonation-dependent conformational variability of intrinsically disordered proteins.Protein science : a publication of the Protein Society · 2013
    Article
  5. Article
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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 at 3 institutions in 2 countries.

Leonhard GeistDepartment of Computational and Structural Biology, Max F. Perutz Laboratories, University of Vienna, Campus Vienna Biocenter 5, 1030 Vienna, Austria.
Anna Zawadzka-Kazimierczuk
Saurabh Saxena
Szymon Żerko
Wiktor Koźmiński
Robert Konrat
Vienna Biocenter · ATUniversity of Warsaw · PLMax Perutz Labs · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Brain acid-soluble protein 1 (BASP1, CAP-23, NAP-22) appears to be implicated in diverse cellular processes. An N-terminally myristoylated form of BASP1 has been discovered to participate in the regulation of actin cytoskeleton dynamics in neurons, whereas non-myristoylated nuclear BASP1 acts as co-suppressor of the potent transcription regulator WT1 (Wilms' Tumor suppressor protein 1). Here we report NMR chemical shift assignment of recombinant human BASP1 fused to an N-terminal cleavable His6-tag.

Indexed as

Nuclear Magnetic Resonance, BiomolecularProtonsAmino Acid SequenceCarbon IsotopesHumansMembrane ProteinsNerve Tissue ProteinsNitrogen IsotopesProtein Structure, SecondaryRepressor ProteinsBASP1 protein, humanCarbon IsotopesMembrane ProteinsNerve Tissue ProteinsNitrogen IsotopesProtonsRepressor Proteins

Identifiers

PMID23179057
PMCPMC3758512
OpenAlexW2063927440

What OpenQuestion holds

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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.