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Protein tyrosine phosphatase 69D is a substrate of protein O-mannosyltransferases 1-2 that is required for the wiring of sensory axons in Drosophila

Journal of Biological Chemistry(2023)10.1016/j.jbc.2023.102890Source: DataRank Database

Protein tyrosine phosphatase 69D is a substrate of protein O-mannosyltransferases 1-2 that is required for the wiring of sensory axons in Drosophila is a research paper published in Journal of Biological Chemistry (2023). On theSindex it has a DataRank of 0. It has been cited 1 time.

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Open Access1 citations

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Enrichment:Funding (13 grants)Impact (FWCI 0.18)OA: goldTopics (47)IDs (PubMed, PMC, OpenAlex)Annotations (1)

FAIR Checklist

Context only (not used in score)

Findable (1/2)

Has DOI

Accessible (1/2)

Open Access

Interoperable (0/2)

Reusable (0/3)

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Authors (8)

Robert Bridger ORCID,Ishita Chandel ORCID,Melissa Koff,Boris Novikov ORCID,Patrick Schroeder

Live enrichment

PubMed:36634851 PMC:PMC9950532 OpenAlex:https://openalex.org/W4313856890

National Institutes of Health

Grant: NS099409

National Institutes of Health

Grant: NS075534

National Institutes of Health

Grant: P40-OD-018537

Consejo Nacional de Ciencia y Tecnología

Grant: 2012-037

NINDS NIH HHS

Grant: R01 NS099409

NINDS NIH HHS

Grant: R01 NS075534

NIGMS NIH HHS

Grant: R01 GM111939

NIGMS NIH HHS

Grant: T32 GM135748

Fundação para a Ciência e a Tecnologia, I.P.

Grant: PTDC/CCI-INF/6762/2020

MS3: New foundations for micro-services and serverless systems

National Institutes of Health

Grant: 5R01NS099409-02

Functional mechanisms underlying Dystroglycan-dependent and independent roles of protein O-mannosylation in the nervous system

National Institutes of Health

Grant: 3P40OD018537-04S1

Bloomington Drosophila Stock Center at Indiana University

National Institutes of Health

Grant: 5R01NS075534-04

The control of neural transmission by glycosylation

Indiana University

FWCI

0.18

Citation Percentile

0.4%

Citation Trend

2023

2026

goldLicense: cc-by

journalhttp://www.jbc.org/article/S0021925823000224/pdf

publisherhttp://www.jbc.org/article/S0021925823000224/pdf

publisherhttps://api.elsevier.com/content/article/PII:S0021925823000224?httpAccept=text/xml

publisherhttps://api.elsevier.com/content/article/PII:S0021925823000224?httpAccept=text/plain

journalhttps://doi.org/10.1016/j.jbc.2023.102890

Fields of Study

Protein Tyrosine PhosphatasesInvertebrate Immune Response MechanismsGlycosylation and Glycoproteins Research0301 basic medicine0303 health sciences03 medical and health sciences

MeSH Terms

AnimalsAxonsDrosophilaMammalsMannosyltransferasesProtein Tyrosine PhosphatasesDrosophila ProteinsDystroglycansReceptor-Like Protein Tyrosine Phosphatases

Keywords

Protein tyrosine phosphatasePhosphataseDrosophila (subgenus)TyrosineSubstrate (aquarium)Sensory systemBiochemistryChemistryCell biologyBiologyEnzymeNeuroscienceGeneReceptor Protein Tyrosine PhosphataseDystroglycanProtein O-mannosylationProtein O-mannosyltransferaseTwistedPtp69dAxon WiringRotated AbdomenDrosophila Sensory NeuronsMammalsAnimalsDrosophila ProteinsReceptor-Like Protein Tyrosine PhosphatasesDrosophilaProtein Tyrosine PhosphatasesDystroglycansMannosyltransferasesAxonsResearch Article