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bp(GO:"anterograde axonal transport")

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Entity

Name
anterograde axonal transport
Namespace
go
Namespace Version
20180921
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/b46b65c3da259b6e86026514dfececab7c22a11b/external/go-names.belns

Appears in Networks 5

Analysis of Isoform-specific Tau Aggregates Suggests a Common Toxic Mechanism Involving Similar Pathological Conformations and Axonal Transport Inhibition v1.0.1

Tau Modifications v1.9.5

Tau Modifications Sections of NESTOR

Axonal Transport, Tau Protein, and Neurodegeneration in Alzheimer’s Disease v1.0.0

Carboxy terminus heat shock protein 70 interacting protein reduces tau-associated degenerative changes v1.0.0

Tau in physiology and pathology v1.0.0

In-Edges 16

a(HBP:"Tau aggregates") decreases bp(GO:"anterograde axonal transport") View Subject | View Object

Collectively, these studies indicate that inhibition of anterograde FAT represents a toxic effect common to all tau aggregates, regardless of isoform composition PubMed:27574109

Appears in Networks:

p(HBP:"Tau isoform B (381 aa)", pmod(HBP:"protein aggregation")) decreases bp(GO:"anterograde axonal transport") View Subject | View Object

Similarly, perfusion of squid axoplasms with hT39, hT37 and hT23 aggregates significantly impaired anterograde FAT (Fig. 4A) when compared to the respective monomers (all at 2 μM) PubMed:27574109

Appears in Networks:
Annotations
MeSH
Axons
MeSH
Cytoplasm

p(HBP:"Tau isoform C (410 aa)", pmod(HBP:"protein aggregation")) decreases bp(GO:"anterograde axonal transport") View Subject | View Object

Similarly, perfusion of squid axoplasms with hT39, hT37 and hT23 aggregates significantly impaired anterograde FAT (Fig. 4A) when compared to the respective monomers (all at 2 μM) PubMed:27574109

Appears in Networks:
Annotations
MeSH
Axons
MeSH
Cytoplasm

p(HBP:"Tau isoform C (410 aa)", pmod(HBP:"protein aggregation")) decreases bp(GO:"anterograde axonal transport") View Subject | View Object

Pairwise comparisons within tau species showed that hT24 aggregates produced significantly more inhibition of anterograde FAT when compared to hT34 and hT39 aggregates. PubMed:27574109

Appears in Networks:

p(HBP:"Tau isoform D (383 aa)", pmod(HBP:"protein aggregation")) decreases bp(GO:"anterograde axonal transport") View Subject | View Object

Perfusion of hT40, hT34 and hT24 aggregates into squid axoplasms significantly impaired anterograde transport (Fig. 4A) when compared to the respective monomers (all at 2 μM). PubMed:27574109

Appears in Networks:
Annotations
MeSH
Axons
MeSH
Cytoplasm

p(HBP:"Tau isoform D (383 aa)", pmod(HBP:"protein aggregation")) decreases bp(GO:"anterograde axonal transport") View Subject | View Object

Pairwise comparisons within tau species showed that hT24 aggregates produced significantly more inhibition of anterograde FAT when compared to hT34 and hT39 aggregates. PubMed:27574109

Appears in Networks:

p(HBP:"Tau isoform E (412 aa)", pmod(HBP:"protein aggregation")) decreases bp(GO:"anterograde axonal transport") View Subject | View Object

Perfusion of hT40, hT34 and hT24 aggregates into squid axoplasms significantly impaired anterograde transport (Fig. 4A) when compared to the respective monomers (all at 2 μM). PubMed:27574109

Appears in Networks:
Annotations
MeSH
Axons
MeSH
Cytoplasm

p(HBP:"Tau isoform E (412 aa)", pmod(HBP:"protein aggregation")) decreases bp(GO:"anterograde axonal transport") View Subject | View Object

Pairwise comparisons within tau species showed that hT24 aggregates produced significantly more inhibition of anterograde FAT when compared to hT34 and hT39 aggregates. PubMed:27574109

Appears in Networks:

p(HBP:"Tau isoform F (441 aa)", pmod(HBP:"protein aggregation")) decreases bp(GO:"anterograde axonal transport") View Subject | View Object

Perfusion of hT40, hT34 and hT24 aggregates into squid axoplasms significantly impaired anterograde transport (Fig. 4A) when compared to the respective monomers (all at 2 μM). PubMed:27574109

Appears in Networks:
Annotations
MeSH
Axons
MeSH
Cytoplasm

p(HBP:"Tau isoform Fetal-tau (352 aa)", pmod(HBP:"protein aggregation")) decreases bp(GO:"anterograde axonal transport") View Subject | View Object

Similarly, perfusion of squid axoplasms with hT39, hT37 and hT23 aggregates significantly impaired anterograde FAT (Fig. 4A) when compared to the respective monomers (all at 2 μM) PubMed:27574109

Appears in Networks:
Annotations
MeSH
Axons
MeSH
Cytoplasm

p(HGNC:MAPT, pmod(Ph, Ser, 422)) decreases bp(GO:"anterograde axonal transport") View Subject | View Object

Highlighting the relevance of these findings to human disease, pS422 tau was found to colocalize with tau oligomers and with a fraction of tau showing increased PAD exposure in the human AD brain. This study identifies novel effects of pS422 on tau biochemical properties, including prolonged nucleation and enhanced dimer formation, which correlate with a distinct inhibitory effect on FAT. PubMed:27373205

Appears in Networks:

p(HGNC:KLC1) increases bp(GO:"anterograde axonal transport") View Subject | View Object

Most recently, this role became even more puz- zling, since APP was implemented as a kinesin-1 receptor (Kamal et al., 2000; 2001). APP apparently binds to the light chain of kinesin-1, which itself is responsible for anterograde axonal transport and consists of two light chains (KLC) associated with two heavy chains (KIF5B). PubMed:12428809

Appears in Networks:

p(HGNC:APPL) increases bp(GO:"anterograde axonal transport") View Subject | View Object

Deletion of the C-terminus of APP695 or APPL, including the kinesin-binding region, disrupted axonal transport of APP695 and APPL. PubMed:12428809

Appears in Networks:

p(HGNC:MAPT) negativeCorrelation bp(GO:"anterograde axonal transport") View Subject | View Object

The overexpression of full-length tau in Chinese hamster ovary (CHO) cells [3], N2A cells [4], cultured retinal ganglion cells [4], NB2a/d1 cells [5] H4-cells [6], and primary cortical neuron cultures [6] led to an impairment of anterograde transport of a variety of kinesin cargos, including mitochondria PubMed:25374103

Appears in Networks:

composite(p(HGNC:MAPT), p(HGNC:MARK2)) positiveCorrelation bp(GO:"anterograde axonal transport") View Subject | View Object

Thies and Mandelkow [7] have shown previously that the co-expression of microtubule-associated protein/microtubule affinityregulating kinase 2 (MARK2) with tau can rescue these effects caused by tau overexpression in vitro. PubMed:25374103

Appears in Networks:

p(HGNC:MAPT) decreases bp(GO:"anterograde axonal transport") View Subject | View Object

First, tau competes with kinesin or dynein motors for binding to microtubules, reducing the binding frequency, motile fraction and run length of kinesin and dynein (without changing the motor velocity of kinesin and dynein), and thereby slowing down both anterograde and retrograde transport PubMed:26631930

Appears in Networks:

Out-Edges 3

bp(GO:"anterograde axonal transport") negativeCorrelation p(HGNC:MAPT) View Subject | View Object

The overexpression of full-length tau in Chinese hamster ovary (CHO) cells [3], N2A cells [4], cultured retinal ganglion cells [4], NB2a/d1 cells [5] H4-cells [6], and primary cortical neuron cultures [6] led to an impairment of anterograde transport of a variety of kinesin cargos, including mitochondria PubMed:25374103

Appears in Networks:

bp(GO:"anterograde axonal transport") decreases a(GO:microtubule) View Subject | View Object

This leads to accumulation of mitochondria in the cell body where they cluster near the microtubule center [6]. PubMed:25374103

Appears in Networks:
Annotations
MeSH
Cell Body

bp(GO:"anterograde axonal transport") positiveCorrelation composite(p(HGNC:MAPT), p(HGNC:MARK2)) View Subject | View Object

Thies and Mandelkow [7] have shown previously that the co-expression of microtubule-associated protein/microtubule affinityregulating kinase 2 (MARK2) with tau can rescue these effects caused by tau overexpression in vitro. PubMed:25374103

Appears in Networks:

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If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.