Danielle Mckeon MSW
Social Worker
4211 AVALON BLVD LOS ANGELES CA, 90011About
Danielle Mckeon MSW is a top Social Worker in LOS ANGELES, CA. With a passion for the field and an unwavering commitment to their specialty, Danielle Mckeon MSW is an expert in changing the lives of their patients for the better. Through their designated cause and expertise in the field, Danielle Mckeon MSW is a prime example of a true leader in health care. As a leader and expert in their field, Danielle Mckeon MSW is passionate about enhancing patient quality of life. They embody the values of communication, safety, and trust when dealing directly with patients. In LOS ANGELES, CA, Danielle Mckeon MSW 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- MHC allele-specific molecular features determine peptide/HLA-A2 conformations that are recognized by HLA-A2-restricted T cell receptors.
- Thermodynamic and kinetic analysis of a peptide-class I MHC interaction highlights the noncovalent nature and conformational dynamics of the class I heterotrimer.
- Strategic mutations in the class I major histocompatibility complex HLA-A2 independently affect both peptide binding and T cell receptor recognition.
- Full-length influenza hemagglutinin HA2 refolds into the trimeric low-pH-induced conformation.
- Poor immunogenicity of a self/tumor antigen derives from peptide-MHC-I instability and is independent of tolerance.
- Two different T cell receptors use different thermodynamic strategies to recognize the same peptide/MHC ligand.
- Increased immunogenicity of an anchor-modified tumor-associated antigen is due to the enhanced stability of the peptide/MHC complex: implications for vaccine design.
- Interactions between CLIP-170, tubulin, and microtubules: implications for the mechanism of Clip-170 plus-end tracking behavior.
- Unraveling a hotspot for TCR recognition on HLA-A2: evidence against the existence of peptide-independent TCR binding determinants.
- T cell receptor recognition via cooperative conformational plasticity.
- T cell receptor binding transition states and recognition of peptide/MHC.
- A comprehensive calorimetric investigation of an entropically driven T cell receptor-peptide/major histocompatibility complex interaction.
- Structures of MART-126/27-35 Peptide/HLA-A2 complexes reveal a remarkable disconnect between antigen structural homology and T cell recognition.
- Kinetics of thermal unfolding of phenylalanine hydroxylase variants containing different metal cofactors (FeII, CoII, and ZnII) and their isokinetic relationship.
- Thermodynamics of T-cell receptor-peptide/MHC interactions: progress and opportunities.
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