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Evidence that the pathway of transferrin receptor mRNA degradation involves an endonucleolytic cleavage within the 3′ UTR and does not involve poly(A) tail shortening.
- R. Binder, J. Horowitz, J. Basilion, D. Koeller, R. Klausner, J. Harford
- Biology, MedicineThe EMBO journal
- 1 April 1994
Site‐directed mutagenesis demonstrates that the sequence surrounding the mapped endonuclease cleavage site is required for both iron‐regulated mRNA turnover and generation of the truncated degradation intermediate of the transferrin receptor mRNA.
Translation and the stability of mRNAs encoding the transferrin receptor and c-fos.
- D. Koeller, J. Horowitz, J. Casey, R. Klausner, J. Harford
- Biology, MedicineProceedings of the National Academy of Sciences…
- 1 September 1991
A model in which a trans-acting labile protein is necessary for the turnover of these mRNAs rather than there being a requirement for the translation of the m RNAs themselves is supported.
Nuclear domains in skeletal myotubes: the localization of transferrin receptor mRNA is independent of its half-life and restricted by binding to ribosomes.
The results suggest that TfR mRNA may associate with RER subdomains by specific targeting, and differential effects of the protein synthesis inhibitors puromycin and cycloheximide suggest that the mRNA is retained in position by its association with ribosomes.
Characterization and localization of cAMP-dependent protein kinases in rat caudal epididymal sperm.
A new Acanthamoeba myosin heavy chain. Cloning of the gene and immunological identification of the polypeptide.
Sequence analysis indicates that the tail domain of this new myosin is incapable of forming a myOSin II-like coiled-coil structure, implying that the protein is single-headed and nonfilamentous, and is tentatively classified as a high molecular weight form of myos in I (HMWMI).
Interaction of the regulatory subunit of a type II cAMP-dependent protein kinase with mammalian sperm flagellum.
- J. Horowitz, W. Wasco, M. Leiser, G. Orr
- Biology, MedicineThe Journal of biological chemistry
- 5 February 1988
Flagellar polypeptides which are capable of forming tight complexes with the regulatory subunit of type II cAMP-dependent protein kinase (RII) are identified and it is proposed that RII is released from the flagellum, a highly disulfide cross-linked structure, due to structural changes in the flagesllum which disrupts the interaction between RII and its binding proteins.
Biochemical and immunological characterization of the flagellar-associated regulatory subunit of a type II cyclic adenosine 5'-monophosphate-dependent protein kinase.
The secondary structure of the regulatory region of the transferrin receptor mRNA deduced by enzymatic cleavage.
The secondary structure of the portion of the transferrin receptor mRNA responsible for the regulation of the transcript's half-life has been deduced by ribonuclease H cleavage directed by antisense…
Failure in beta-amyloid degradation in the endosomal/lysosomal pathway results in intracellular beta-amyloid accumulation within lipid rafts