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p(HBP:"tubulin-binding repeat 3")

Equivalencies: 1 | Classes: 0 | Children: 0 | Explore

Entity

Name
tubulin-binding repeat 3
Namespace
HBP
Namespace Version
20181119
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/90e1cb9e5e882703380c9db8d4915ac6f3cba137/export/hbp-names.belns

Appears in Networks 2

Tau Biochemistry v1.2.5

Tau Biochemistry Section of NESTOR

Tau Modifications v1.9.5

Tau Modifications Sections of NESTOR

In-Edges 4

p(HBP:"Tau isoform F (441 aa)", frag("306_336")) equivalentTo p(HBP:"tubulin-binding repeat 3") View Subject | View Object

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p(HBP:"VQIVYK motif") partOf p(HBP:"tubulin-binding repeat 3") View Subject | View Object

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p(HBP:"VQIVYK motif") partOf p(HBP:"tubulin-binding repeat 3") View Subject | View Object

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act(p(INTERPRO:"FKBP-type peptidyl-prolyl cis-trans isomerase domain")) directlyDecreases p(HBP:"tubulin-binding repeat 3") View Subject | View Object

We then investigated the function of FK506-binding protein (FKBP) 12, which is known to accumulate in neurofibrillary tangles in vivo, on aggregation of the R3 peptide and found that FKBP12 completely prevented the peptide from aggregating at a concentration ratio of 1 : 4 (peptide:FKBP12). FKBP12 also restored the oligomer of the peptide to its monomeric status. Mutational studies on the catalytic center of FKBP12 indicated that peptidyl-prolyl isomerase activity of FKBP12 was essential for prevention of aggregation. Assuming that the propensity of aggregation of the peptide is different in each cis-/trans-isomer, we propose that the aggregation behavior of the R3 peptide can be theoretically described with a simple kinetic scheme, in which only the cis-isomer can aggregate and FKBP12 catalyzes isomerization of the peptide in both the monomeric and aggregative states. PubMed:23832849

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Out-Edges 6

p(HBP:"tubulin-binding repeat 3") partOf a(HBP:"microtubule-binding region") View Subject | View Object

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p(HBP:"tubulin-binding repeat 3") equivalentTo p(HBP:"Tau isoform F (441 aa)", frag("306_336")) View Subject | View Object

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p(HBP:"tubulin-binding repeat 3") partOf p(HBP:"4R tau") View Subject | View Object

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p(HBP:"tubulin-binding repeat 3") partOf p(HBP:"3R tau") View Subject | View Object

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p(HBP:"tubulin-binding repeat 3") partOf a(HBP:"microtubule-binding region") View Subject | View Object

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p(HBP:"tubulin-binding repeat 3") increases a(HBP:"Tau aggregates") View Subject | View Object

We then investigated the function of FK506-binding protein (FKBP) 12, which is known to accumulate in neurofibrillary tangles in vivo, on aggregation of the R3 peptide and found that FKBP12 completely prevented the peptide from aggregating at a concentration ratio of 1 : 4 (peptide:FKBP12). FKBP12 also restored the oligomer of the peptide to its monomeric status. Mutational studies on the catalytic center of FKBP12 indicated that peptidyl-prolyl isomerase activity of FKBP12 was essential for prevention of aggregation. Assuming that the propensity of aggregation of the peptide is different in each cis-/trans-isomer, we propose that the aggregation behavior of the R3 peptide can be theoretically described with a simple kinetic scheme, in which only the cis-isomer can aggregate and FKBP12 catalyzes isomerization of the peptide in both the monomeric and aggregative states. PubMed:23832849

Appears in Networks:

About

BEL Commons is developed and maintained in an academic capacity by Charles Tapley Hoyt and Daniel Domingo-Fernández at the Fraunhofer SCAI Department of Bioinformatics with support from the IMI project, AETIONOMY. It is built on top of PyBEL, an open source project. Please feel free to contact us here to give us feedback or report any issues. Also, see our Publishing Notes and Data Protection information.

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.