Rachel Ann Hoyhtya
Counselor/Therapist
480 EAST AGATE AVE GRANBY CO, 80446About
Rachel Hoyhtya is a counselor in GRANBY, CO. Rachel evaluates patients using many different procedures, in order to determine what treatments must be carried out in order to properly assess their symptoms. Counselors provide consultation for each patient and their families.
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Expert Publications
Data provided by the National Library of Medicine- Structural characterization of rabbit brain ubiquitin.
- Characterization of two platelet aggregation inhibitor-like polypeptides from
- Reptilian alcohol dehydrogenase. Heterogeneity relevant to class multiplicity of the mammalian enzyme.
- Purification and characterization of a Kunitz-type trypsin inhibitor from Leaf-nosed viper venom.
- Purification and characterization of two highly different group II phospholipase A2 isozymes from a single viperid (Eristocophis macmahoni) venom.
- Characterization of phospholipase A2 from the venom of Horned viper (Cerastes cerastes).
- Extensive multiplicity of the miscellaneous type of neurotoxins from the venom of the cobra Naja naja naja and structural characterization of major components.
- Poster 114 Atypical Upper Extremity Weakness After a Fall: A Case Report.
- Alcohol dehydrogenase of class III: consistent patterns of structural and functional conservation in relation to class I and other proteins.
- Regulation of phospholipase D in HL60 cells. Evidence for a cytosolic phospholipase D.
- Regulation of MHC class I membrane expression by beta 2-microglobulin.
- Major histocompatibility complex class I-binding peptides are recycled to the cell surface after internalization.
- Linking of isozyme and class variability patterns in the emergence of novel alcohol dehydrogenase functions. Characterization of isozymes in Uromastix hardwickii.
- Tissue-specific distribution and subcellular distribution of phospholipase D in rat: evidence for distinct RhoA- and ADP-ribosylation factor (ARF)-regulated isoenzymes.
- Analysis of heparin-binding sites in human lipoprotein lipase using synthetic peptides.
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