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Large FK506-Binding Proteins Shape the Pharmacology of Rapamycin
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title
Large FK506-Binding Proteins Shape the Pharmacology of Rapamycin
(English)
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main subject
cell biology
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pharmacology
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based on heuristic
inferred from title
sirolimus
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based on heuristic
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author name string
Andreas M März
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Anne-Katrin Fabian
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2
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Christian Kozany
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3
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Andreas Bracher
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4
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Felix Hausch
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5
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language of work or name
English
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publication date
April 2013
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published in
Molecular and Cellular Biology
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volume
33
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issue
7
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page(s)
1357-67
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cites work
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Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton
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The 25-kDa FK506-binding protein is localized in the nucleus and associates with casein kinase II and nucleolin
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A Novel FK506 Binding Protein Can Mediate the Immunosuppressive Effects of FK506 and Is Associated with the Cardiac Ryanodine Receptor
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Overview of the CCP4 suite and current developments
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Rapamycin (AY-22,989), a new antifungal antibiotic. I. Taxonomy of the producing streptomycete and isolation of the active principle
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Fighting neurodegeneration with rapamycin: mechanistic insights
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Prolonged rapamycin treatment inhibits mTORC2 assembly and Akt/PKB
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Characterization of the FKBP.rapamycin.FRB ternary complex
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Rapamycin and less immunosuppressive analogs are toxic to Candida albicans and Cryptococcus neoformans via FKBP12-dependent inhibition of TOR
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Tissue distribution and abundance of human FKBP51, and FK506-binding protein that can mediate calcineurin inhibition
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Identification of an 11-kDa FKBP12-rapamycin-binding domain within the 289-kDa FKBP12-rapamycin-associated protein and characterization of a critical serine residue
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Targets for Cell Cycle Arrest by the Immunosuppressant Rapamycin in Yeast
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Distinct pathways involving the FK506-binding proteins 12 and 12.6 underlie IL-2-versus IL-15-mediated proliferation of T cells
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Inhibition of FK506 binding proteins reduces alpha-synuclein aggregation and Parkinson's disease-like pathology.
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Oral rapamycin to inhibit restenosis after stenting of de novo coronary lesions: the Oral Rapamune to Inhibit Restenosis (ORBIT) study
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Identifiers
DOI
10.1128/MCB.00678-12
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4093558
OpenCitations bibliographic resource ID
4093558
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4093558
PMC publication ID
3624267
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4093558
PubMed publication ID
23358420
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4093558
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