Viper Venoms

"Viper Venoms" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure, which enables searching at various levels of specificity.

MeSH information

Definition | Details | More General Concepts | Related Concepts | More Specific Concepts

Venoms from SNAKES of the viperid family. They tend to be less toxic than elapid or hydrophid venoms and act mainly on the vascular system, interfering with coagulation and capillary membrane integrity and are highly cytotoxic. They contain large amounts of several enzymes, other factors, and some toxins.

Descriptor ID

D014757

MeSH Number(s)

D20.888.850.960

D23.946.833.850.960

Concept/Terms

Viper Venoms

Egyptian Sand Viper Venom

Viperotoxin

Cerastes Venoms

Below are MeSH descriptors whose meaning is more general than "Viper Venoms".

Chemicals and Drugs [D]
Complex Mixtures [D20]
Venoms [D20.888]
Snake Venoms [D20.888.850]
Viper Venoms [D20.888.850.960]
Biological Factors [D23]
Toxins, Biological [D23.946]
Venoms [D23.946.833]
Snake Venoms [D23.946.833.850]
Viper Venoms [D23.946.833.850.960]

Below are MeSH descriptors whose meaning is related to "Viper Venoms".

Below are MeSH descriptors whose meaning is more specific than "Viper Venoms".

Viper Venoms
Crotalid Venoms

publications

Timeline | Most Recent

This graph shows the total number of publications written about "Viper Venoms" by people in Harvard Catalyst Profiles by year, and whether "Viper Venoms" was a major or minor topic of these publication.

Bar chart showing 9 publications over 7 distinct years, with a maximum of 2 publications in 2013 and 2014

To see the data from this visualization as text, click here.

Year	Major Topic	Minor Topic	Total
1994	1	0	1
1995	0	1	1
2002	0	1	1
2013	1	1	2
2014	1	1	2
2016	1	0	1
2019	0	1	1

Below are the most recent publications written about "Viper Venoms" by people in Profiles.

Proteomic Analysis of Human Blister Fluids Following Envenomation by Three Snake Species in India: Differential Markers for Venom Mechanisms of Action. Toxins (Basel). 2019 04 30; 11(5).

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Structural and functional characterization of complex formation between two Kunitz-type serine protease inhibitors from Russell's Viper venom. Biochimie. 2016 Sep-Oct; 128-129:138-47.

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Galatrox is a C-type lectin in Bothrops atrox snake venom that selectively binds LacNAc-terminated glycans and can induce acute inflammation. Glycobiology. 2014 Nov; 24(11):1010-21.

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Downregulation of microvascular endothelial type B endothelin receptor is a central vascular mechanism in hypertensive pregnancy. Hypertension. 2014 Sep; 64(3):632-43.

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Inhibitory effects of recombinant RTS-jerdostatin on integrin a1ß1 function during adhesion, migration and proliferation of rat aortic smooth muscle cells and angiogenesis. Toxicon. 2014 Mar; 79:45-54.

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A beneficial role for immunoglobulin E in host defense against honeybee venom. Immunity. 2013 Nov 14; 39(5):963-75.

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Myocarditis along with acute ischaemic cerebellar, pontine and lacunar infarction following viper bite. BMJ Case Rep. 2013 Sep 06; 2013.

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Purification, characterization and molecular cloning of chymotrypsin inhibitor peptides from the venom of Burmese Daboia russelii siamensis. Peptides. 2013 May; 43:126-32.

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Recombinant expression of mutants of the Frankenstein disintegrin, RTS-ocellatusin. Evidence for the independent origin of RGD and KTS/RTS disintegrins. Toxicon. 2012 Sep 15; 60(4):665-75.

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Accidents caused by Bothrops and Bothropoides in the State of Paraiba: epidemiological and clinical aspects. Rev Soc Bras Med Trop. 2010 Nov-Dec; 43(6):662-7.

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