Evidence map›Paper›PMID 24798811›Full record

ArticleMethods (San Diego, Calif.)2014

Isolation of serpin-interacting proteins in C. elegans using protein affinity purification.

Mark T Miedel, Xuemei Zeng, Nathan A Yates, Gary A Silverman, Cliff J Luke

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Methods (San Diego, Calif.), 2014. 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
–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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. Expanding the C. elegans toolbox into a toolshed.Methods (San Diego, Calif.) · 2014
    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.

Mark T MiedelDepartment of Pediatrics, Cell Biology and Physiology, University of Pittsburgh School of Medicine, Children's Hospital of Pittsburgh of UPMC, and Magee-Womens Hospital of UPMC, Pittsburgh, PA 15224, USA.
Xuemei ZengBiomedical Mass Spectrometry Center, University of Pittsburgh Schools of the Health Sciences, Pittsburgh, PA 15213, USA.
Nathan A YatesBiomedical Mass Spectrometry Center, University of Pittsburgh Schools of the Health Sciences, Pittsburgh, PA 15213, USA; Department of Cell Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15261, USA.
Gary A SilvermanDepartment of Pediatrics, Cell Biology and Physiology, University of Pittsburgh School of Medicine, Children's Hospital of Pittsburgh of UPMC, and Magee-Womens Hospital of UPMC, Pittsburgh, PA 15224, USA.
Cliff J LukeDepartment of Pediatrics, Cell Biology and Physiology, University of Pittsburgh School of Medicine, Children's Hospital of Pittsburgh of UPMC, and Magee-Womens Hospital of UPMC, Pittsburgh, PA 15224, USA. Electronic address: cliff.luke@chp.edu.

Funding

VECTOR CORE FACILITYP30CA047904 · NCI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI Jessie Nedrow · 1988 to 2026
$158.0M
Treating AT Deficiency with Drugs that Modulate the Proteostasis NetworkP01DK096990 · NIDDK · WASHINGTON UNIVERSITY · PI SILVERMAN, GARY ARTHUR · 2012 to 2023
$18.3M
High Throughput Genetic and Drug Screens for Alph-1-Antitrypsin DeficiencyR01DK079806 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI SILVERMAN, GARY ARTHUR · 2008 to 2011
$2.4M
Intracellular Serpin Regulation of Intestinal Cell NecrosisR01DK081422 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI SILVERMAN, GARY ARTHUR · 2009 to 2012
$1.6M
NCI NIH HHS P30 CA047904NCI NIH HHS P30CA047904NIDDK NIH HHS DK079806NIDDK NIH HHS DK081422NIDDK NIH HHS P01 DK096990NIDDK NIH HHS P01DK096990NIDDK NIH HHS R01 DK079806NIDDK NIH HHS R01 DK081422
6 · The paper itself

Abstract

Caenorhabditis elegans is a useful model organism for combining multiple imaging, genetic, and biochemical methodologies to gain more insight into the biological function of specific proteins. Combining both biochemical and genetic analyses can lead to a better understanding of how a given protein may function within the context of a network of other proteins or specific pathway. Here, we describe a protocol for the biochemical isolation of serpin-interacting proteins using affinity purification and proteomic analysis. As the knowledge of in vivo serpin interacting partners in C. elegans has largely been obtained using genetic and in vitro recombinant protein studies, this protocol serves as a complementary approach to provide insight into the biological function and regulation of serpins.

Indexed as

AnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsChromatography, AffinityProtein BindingProtein Interaction MapsProteomicsRecombinant ProteinsSerpinsCaenorhabditis elegans ProteinsRecombinant ProteinsSerpinsAffinity purificationCaenorhabditis elegansProteomicsSerpin

Identifiers

PMID24798811
PMCPMC4113314

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Registered trials

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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.