Evidence map›Paper›PMID 22738176›Full record

ArticleBiochemistry2012

Structural organization of the nine spectrin repeats of Kalirin.

K S Vishwanatha, Y P Wang, H T Keutmann, R E Mains, B A Eipper

Abstract read
In one paragraph

Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

10 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. A Novel Long Non-coding RNA,Frontiers in molecular neuroscience · 2017
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Kalirin promotes neointimal hyperplasia by activating Rac in smooth muscle cells.Arteriosclerosis, thrombosis, and vascular biology · 2013
    Article
  10. 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

5 authors at 2 institutions in 1 country.

K S VishwanathaDepartment of Neuroscience, University of Connecticut Health Center, Farmington, CT 06030, USA.
Y P Wang
H T Keutmann
R E Mains
B A Eipper
Harvard University · USUConn Health · US

Funding

CELL BIOLOGY OF BIOACTIVE PEPTIDE SECRETIONR01DK032948 · NIDDK · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI EIPPER, ELIZABETH ANNE, MAINS, RICHARD E · 1986 to 2019
$7.3M
Cell Biology of Bioactive Peptide SecretionR56DK032948 · NIDDK · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI MAINS, RICHARD E · 2008 to 2008
$303k
CELL BIOLOGY OF BIOACTIVE PEPTIDE SECRETIONR37DK032948 · NIDDK · JOHNS HOPKINS UNIVERSITY · PI MAINS, RICHARD E · 1990 to 1998
–
NIDDK NIH HHS DK-32948NIDDK NIH HHS R01 DK032948NIDDK NIH HHS R56 DK032948
6 · The paper itself

Abstract

Sequence analysis suggests that KALRN, a Rho GDP/GTP exchange factor genetically linked to schizophrenia, could contain as many as nine tandem spectrin repeats (SRs). We expressed and purified fragments of Kalirin containing from one to five putative SRs to determine whether they formed nested structures that could endow Kalirin with the flexible rodlike properties characteristic of spectrin and dystrophin. Far-UV circular dichroism studies indicated that Kalirin contains nine SRs. On the basis of thermal denaturation, sensitivity to chemical denaturants, and the solubility of pairs of repeats, the nine SRs of Kalirin form nested structures. Modeling studies confirmed this conclusion and identified an exposed loop in SR5; consistent with the modeling, this loop was extremely labile to proteolytic cleavage. Analysis of a direpeat fragment (SR4:5) encompassing the region of Kalirin known to interact with NOS2, DISC-1, PAM, and Arf6 identified this as the least stable region. Analytical ultracentrifugation indicated that SR1:3, SR4:6, and SR7:9 were monomers and adopted an extended conformation. Gel filtration suggested that ΔKal7, a natural isoform that includes SR5:9, was monomeric and was not more extended than SR5:9. Similarly, the nine SRs of Kal7, which was also monomeric, were not more extended than SR5:9. The rigidity and flexibility of the nine SRs of Kal7, which separate its essential N-terminal Sec14p domain from its catalytic domain, play an essential role in its contribution to the formation and function of dendritic spines.

Indexed as

Repetitive Sequences, Amino AcidAnimalsChromatography, GelCircular DichroismGuanine Nucleotide Exchange FactorsModels, MolecularProtein IsoformsProtein Structure, SecondaryProtein Structure, TertiaryProtein UnfoldingRatsRecombinant ProteinsUltracentrifugationGuanine Nucleotide Exchange FactorsKalrn protein, ratProtein IsoformsRecombinant Proteins

Identifiers

PMID22738176
PMCPMC3447990
OpenAlexW2061420463

What OpenQuestion holds

Textmetadata
LicenceTDM
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.