Inhibitory Effect of Snake Venom Toxin on Colorectal Cancer HCT116 Cells Growth through Induction of Intrinsic or Extrinsic Apoptosis&lt;sup&gt;※&lt;/sup&gt;

An efficient one-pot chemical synthesis of snake venom toxin Mambalgin-1 was achieved using an azide-switch strategy combined with hydrazide-based native chemical ligation.

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The mechanism of Ca2+ releasing action of a snake venom toxin in sarcoplasmic reticulum

The Japanese Journal of Pharmacology ◽

10.1016/s0021-5198(19)49124-5 ◽

1992 ◽

Vol 58 ◽

pp. 208

Author(s):

Kaori Funayama ◽

Ken-Ichi Furukawa ◽

Yoshiteru Ohshima ◽

Anthony T. Tu ◽

Yasushi Ohizumi

Keyword(s):

Sarcoplasmic Reticulum ◽

Snake Venom ◽

Venom Toxin ◽

Snake Venom Toxin

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Snake venom toxin from vipera lebetina turanicainduces apoptosis of colon cancer cells via upregulation of ROS- and JNK-mediated death receptor expression

BMC Cancer ◽

10.1186/1471-2407-12-228 ◽

2012 ◽

Vol 12 (1) ◽

Cited By ~ 34

Author(s):

Mi Hee Park ◽

MiRan Jo ◽

Dohee Won ◽

Ho Sueb Song ◽

Sang Bae Han ◽

...

Keyword(s):

Colon Cancer ◽

Cancer Cells ◽

Snake Venom ◽

Death Receptor ◽

Receptor Expression ◽

Colon Cancer Cells ◽

Venom Toxin ◽

Snake Venom Toxin ◽

Vipera Lebetina

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P-788 The snake venom toxin taipoxin confers specific toxicity to smallcell lung cancer cell lines

Lung Cancer ◽

10.1016/s0169-5002(05)81281-4 ◽

2005 ◽

Vol 49 ◽

pp. S326-S327

Author(s):

T. Poulsen ◽

N. Pedersen ◽

M. Pedersen ◽

H. Poulsen

Keyword(s):

Lung Cancer ◽

Cell Lines ◽

Cancer Cell ◽

Snake Venom ◽

Cancer Cell Lines ◽

Lung Cancer Cell ◽

Venom Toxin ◽

Snake Venom Toxin

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Amino acid sequence of a snake venom toxin that binds to the muscarinic acetylcholine receptor

Toxicon ◽

10.1016/0041-0101(91)90027-o ◽

1991 ◽

Vol 29 (4-5) ◽

pp. 521-526 ◽

Cited By ~ 33

Author(s):

Evert Karlsson ◽

Carl Risinger ◽

Mikael Jolkkonen ◽

Christer Wernstedt ◽

Abdu Adem

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Acetylcholine Receptor ◽

Snake Venom ◽

Muscarinic Acetylcholine Receptor ◽

Muscarinic Acetylcholine ◽

Venom Toxin ◽

Snake Venom Toxin

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Characterization of inflamin, the first member of a new family of snake venom proteins that induces inflammation

Biochemical Journal ◽

10.1042/bj20130599 ◽

2013 ◽

Vol 455 (2) ◽

pp. 239-250 ◽

Cited By ~ 3

Author(s):

Bhaskar Barnwal ◽

R. Manjunatha Kini

Keyword(s):

Phospholipase A2 ◽

Snake Venom ◽

Calcium Dependent ◽

Venom Toxin ◽

New Family ◽

Snake Venom Toxin ◽

Venom Proteins

Inflamin, a novel snake venom toxin from Aipysurus eydouxii, leads to the activation of calcium-dependent phospholipase A2 by phosphorylation at Ser505, resulting in inflammation and pain.

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