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Joseph W. Burnett

Researcher at University of Maryland, Baltimore

Publications -  207
Citations -  4966

Joseph W. Burnett is an academic researcher from University of Maryland, Baltimore. The author has contributed to research in topics: Chrysaora quinquecirrha & Venom. The author has an hindex of 38, co-authored 207 publications receiving 4833 citations. Previous affiliations of Joseph W. Burnett include University of Maryland, College Park & University of Maryland Medical System.

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Book

Venomous and Poisonous Marine Animals: A Medical and Biological Handbook

TL;DR: Cnidarians - animals with endogenous cnidae echinoderms, molluscs and sponges toxic (venomous and poisonous) marine vertebrates further international studies on toxic marine animals special considerations to finish.
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Teledermatology and in-person examinations: a comparison of patient and physician perceptions and diagnostic agreement.

TL;DR: Physicians and patients were satisfied with teledermatology examinations and diagnostic agreement between in-person and video dermatologists was high.
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Herpes simplex virus (HSV)-associated erythema multiforme (HAEM): A viral disease with an autoimmune component.

TL;DR: It is the thesis that the polymerase chain reaction (PCR) assay for HSV DNA detection in lesional skin and staining with antibodies to IFN-gamma and TNF-alpha, are important criteria for the diagnosis of skin eruptions and improved patient management.
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Partial purification of box jellyfish (Chironex fleckeri) nematocyst venom isolated at the beachside.

TL;DR: It is shown that lyophilization of autolysis isolated nematocysts is an effective method of transporting the venom and retained lethality and native polyacrylamide gel electrophoresis (NPAGE) are used in this study.
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The chemistry and toxicology of some venomous pelagic coelenterates.

TL;DR: No consistency between the severity of the sting and the abundance of these substances is apparent and the pain in humans produced by the venoms of these animals may be induced by a large molecular weight polypeptide which has a kinin-like action.