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M

My G. Mahoney

Researcher at University of Pennsylvania

Publications -  17
Citations -  1433

My G. Mahoney is an academic researcher from University of Pennsylvania. The author has contributed to research in topics: Biology & Pemphigus vulgaris. The author has an hindex of 8, co-authored 10 publications receiving 1352 citations. Previous affiliations of My G. Mahoney include Thomas Jefferson University.

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Explanations for the clinical and microscopic localization of lesions in pemphigus foliaceus and vulgaris

TL;DR: It is suggested that pemphigus autoantibodies inhibit the adhesive function of desmoglein proteins, and it is demonstrated that either Dsg1 or Dsg3 alone is sufficient to maintain keratinocyte adhesion.
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Targeted Disruption of the Pemphigus Vulgaris Antigen (Desmoglein 3) Gene in Mice Causes Loss of Keratinocyte Cell Adhesion with a Phenotype Similar to Pemphigus Vulgaris

TL;DR: It is suggested that pemphigus autoantibodies might interfere directly with such a function of DSG3, and the critical importance of Dsg3 for adhesion in deep stratified squamous epithelia is demonstrated.
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Pemphigus vulgaris (PV) antigen (desmoglein 3) anchors telogen hair in the follicle

TL;DR: The authors showed that desmoglein 3 is not only critical for cell adhesion in the deep stratified squamous epithelium, but also for anchoring the telogen hair to the outer root sheath of the follicle and underscore the importance of desmosomes in maintaining the normal structure and function of hair.
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Desmoglein 3 anchors telogen hair in the follicle

TL;DR: Data demonstrate that desmoglein 3 is not only critical for cell adhesion in the deep stratified squamous epithelium, but also for anchoring the telogen hair to the outer root sheath of the follicle and underscore the importance of desmosomes in maintaining the normal structure and function of hair.
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The Members of the Plakin Family of Proteins Recognized by Paraneoplastic Pemphigus Antibodies Include Periplakin

TL;DR: It is indicated that a homologous region in the carboxy-terminus of plakins, including the newly characterized periplakin, serves as an antigenic site in PNP.