Dane Fowler B.A.
Social Worker | Clinical
5554 S PRINCE ST LITTLETON CO, 80120About
Dane Fowler B.A. is a top Social Worker in LITTLETON, CO. With a passion for the field and an unwavering commitment to their specialty, Dane Fowler B.A. is an expert in changing the lives of their patients for the better. Through their designated cause and expertise in the field, Dane Fowler B.A. is a prime example of a true leader in health care. As a leader and expert in their field, Dane Fowler B.A. is passionate about enhancing patient quality of life. They embody the values of communication, safety, and trust when dealing directly with patients. In LITTLETON, CO, Dane Fowler B.A. is a true asset to their field and dedicated to the profession of medicine.
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Expert Publications
Data provided by the National Library of Medicine- Serologic and biochemical studies of the Ia system of the mouse H-2 gene complex. Further evidence for I-C subregion.
- Characterization of fragments of the murine Ia-associated invariant chain.
- Serological and biochemical identification of theH-2K(p) (H 2.16) andH-2D (p) (H-2.22) gene products.
- Biosynthesis and intracellular transport of MHC class II molecules associated with a mutated, glycosaminoglycan-negative invariant chain.
- Internalization of Ia molecules by antigen-presenting B cells is limited.
- The role of the Ia-invariant chain complex in the posttranslational processing and transport of Ia and invariant chain glycoproteins.
- Insertion of Ia and H-2 alloantigens into model membranes.
- Insertion of Ia and H-2 alloantigens into model membranes.
- Molecular mapping of murine I region recombinants. II. Crossing over in the E beta gene is restricted to a 4.5 kb stretch of DNA that excludes the beta 1 exon.
- Molecular mapping of murine I region recombinants: crossing over in the E beta gene.
- Fatty acylation of murine Ia alpha, beta, and invariant chains.
- Identification of the glycosaminoglycan-attachment site of mouse invariant-chain proteoglycan core protein by site-directed mutagenesis.
- Inhibition of proteoglycan synthesis eliminates the proteoglycan form of Ia-associated invariant chain and depresses antigen presentation.
- Slower processing, weaker beta 2-M association, and lower surface expression of H-2Ld are influenced by its amino terminus.
- Structural characterization of murine Ia antigen N-linked oligosaccharides and localization of specific structures to two unique alpha-chain glycosylation sites.
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