Evidence map›Paper›PMID 28724630›Full record

ArticleThe Journal of biological chemistry2017

Altered Met receptor phosphorylation and LRP1-mediated uptake in cells lacking carbohydrate-dependent lysosomal targeting.

Megan Aarnio-Peterson, Peng Zhao, Seok-Ho Yu, Courtney Christian, Heather Flanagan-Steet, Lance Wells, Richard Steet

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2017. 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, top 88% 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  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

7 authors at 1 institution in 1 country.

Megan Aarnio-PetersonFrom the Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia 30602.
Peng ZhaoFrom the Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia 30602.
Seok-Ho YuFrom the Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia 30602.
Courtney ChristianFrom the Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia 30602.
Heather Flanagan-SteetFrom the Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia 30602.
Lance WellsFrom the Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia 30602.
Richard SteetFrom the Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia 30602 rsteet@ccrc.uga.edu.
University of Georgia · US

Funding

Recombinant Production of Glycosylation Enzymes for Biochem/Structural StudiesP01GM107012 · NIGMS · UNIVERSITY OF GEORGIA · PI PRESTEGARD, JAMES H. · 2013 to 2017
$7.5M
PATHOGENIC MECHANISMS OF LYSOSOMAL DISEASER01GM086524 · NIGMS · UNIVERSITY OF GEORGIA · PI STEET, RICHARD · 2009 to 2021
$4.0M
NIGMS NIH HHS P01 GM107012NIGMS NIH HHS R01 GM086524
6 · The paper itself

Abstract

Acid hydrolases utilize a carbohydrate-dependent mechanism for lysosomal targeting. These hydrolases acquire a mannose 6-phosphate tag by the action of the GlcNAc-1-phosphotransferase enzyme, allowing them to bind receptors and traffic to endosomes. Loss of GlcNAc-1-phosphotransferase results in hydrolase hypersecretion and profound lysosomal storage. Little, however, is known about how these cellular phenotypes affect the trafficking, activity, and localization of surface glycoproteins. To address this question, we profiled the abundance of surface glycoproteins in WT and CRISPR-mediated

Indexed as

CarbohydratesHeLa CellsHumansLow Density Lipoprotein Receptor-Related Protein-1LysosomesPhosphorylationProto-Oncogene Proteins c-metTransferases (Other Substituted Phosphate Groups)Tumor Cells, CulturedCarbohydratesGNPTAB protein, humanLow Density Lipoprotein Receptor-Related Protein-1LRP1 protein, humanProto-Oncogene Proteins c-metTransferases (Other Substituted Phosphate Groups)lysosomal storage diseaselysosomal storage disorderlysosomephosphatasereactive oxygen species (ROS)receptor recyclingreceptor tyrosine kinase

Identifiers

PMID28724630
PMCPMC5592684
OpenAlexW2739368509

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.