FKBPs: at the crossroads of folding and transduction. (Q34360728)

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11 November 2019

review article

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title

FKBPs: at the crossroads of folding and transduction (English)

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11 November 2019

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11 November 2019

Y Harrar

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11 November 2019

J D Faure

series ordinal

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11 November 2019

publication date

1 September 2001

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11 November 2019

published in

Trends in Plant Science

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11 November 2019

volume

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11 November 2019

issue

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11 November 2019

page(s)

426-431

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Immunophilins: switched on protein binding domains?

11 November 2019

cites work

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Chemistry and Biology of the Immunophilins and Their Immunosuppressive Ligands

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FK506, an immunosuppressant targeting calcineurin function

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The target of rapamycin (TOR) proteins

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Immunophilin ligands as a novel treatment of neurological disorders

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Molecular cloning, characterization, and chromosomal localization of FKBP23, a novel FK506-binding protein with Ca2+-binding ability

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Mechanism of TGFβ receptor inhibition by FKBP12

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Stabilization of calcium release channel (ryanodine receptor) function by FK506-binding protein

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FKBP12 Binds the Inositol 1,4,5-Trisphosphate Receptor at Leucine-Proline (1400–1401) and Anchors Calcineurin to this FK506-like Domain

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PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): defective regulation in failing hearts

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Coupled gating between individual skeletal muscle Ca2+ release channels (ryanodine receptors)

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All cyclophilins and FK506 binding proteins are, individually and collectively, dispensable for viability in Saccharomyces cerevisiae

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Cardiac defects and altered ryanodine receptor function in mice lacking FKBP12

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FKBP12, the 12-kDa FK506-binding protein, is a physiologic regulator of the cell cycle

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Chaperone function of Hsp90-associated proteins

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Different regions of the immunophilin FKBP52 determine its association with the glucocorticoid receptor, hsp90, and cytoplasmic dynein

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Rabbit FKBP59-heat shock protein binding immunophillin (HBI) is a calmodulin binding protein

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FAP48, a new protein that forms specific complexes with both immunophilins FKBP59 and FKBP12. Prevention by the immunosuppressant drugs FK506 and rapamycin

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Immunophilins, Refsum disease, and lupus nephritis: the peroxisomal enzyme phytanoyl-COA alpha-hydroxylase is a new FKBP-associated protein

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Posttranslational regulation of IRF-4 activity by the immunophilin FKBP52

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Molecular characterization of a FKBP-type immunophilin from higher plants

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A novel plant peptidyl-prolyl-cis-trans-isomerase (PPIase): cDNA cloning, structural analysis, enzymatic activity and expression

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7 January 2021

Mutation in the Arabidopsis PASTICCINO1 gene, which encodes a new FK506-binding protein-like protein, has a dramatic effect on plant development

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7 January 2021

A maize FK506-sensitive immunophilin, mzFKBP-66, is a peptidylproline cis-trans-isomerase that interacts with calmodulin and a 36-kDa cytoplasmic protein

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The wheat peptidyl prolyl cis-trans-isomerase FKBP77 is heat induced and developmentally regulated

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7 January 2021

Binding of immunophilins to the 90 kDa heat shock protein (hsp90) via a tetratricopeptide repeat domain is a conserved protein interaction in plants

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High-molecular-weight FK506-binding proteins are components of heat-shock protein 90 heterocomplexes in wheat germ lysate

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7 January 2021

Molecular characterization of a plant FKBP12 that does not mediate action of FK506 and rapamycin.

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7 January 2021

An Arabidopsis immunophilin, AtFKBP12, binds to AtFIP37 (FKBP interacting protein) in an interaction that is disrupted by FK506

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7 January 2021

FK506 and the role of immunophilins in nerve regeneration

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Expression analysis with oligonucleotide microarrays reveals that MYC regulates genes involved in growth, cell cycle, signaling, and adhesion

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7 January 2021

Molecular cloning and overexpression of the human FK506-binding protein FKBP

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7 January 2021

10.1016/S1360-1385(01)02044-1

Identifiers

DOI

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11544132%20AND%20SRC:MED&resulttype=core&format=json

11 November 2019

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