Insights into the Role of Proteolytic and Adhesive Domains of Snake Venom Metalloproteinases from Bothrops spp. in the Control of Toxoplasma gondii Infection

Authors: Samuel C. Teixeira, Thales A. M. Fernandes, Guilherme de Souza, Luana C. Luz, Marina Paschoalino, Joed P. de L. Junior, Alessandra M. Rosini, Aryani F. F. Martínez, Vitor de Freitas, Daiana S. Lopes, Patrícia B. Clissa, Vinícius C. de Souza, Milton Y. Nishiyama-Jr., Bellisa F. Barbosa, Eloisa A. V. Ferro, Veridiana de M. R. Ávila

Source: Toxins, Vol 17, Iss 2, p 95 (2025)

Subject Terms: toxoplasmosis, Toxoplasma gondii, snake venom metalloproteinases, Medicine

File Description: electronic resource

Relation: https://www.mdpi.com/2072-6651/17/2/95; https://doaj.org/toc/2072-6651

Access URL: https://doaj.org/article/7ddf88f8b19d4e82b5c1fea90b60c652

Toxicological analyses of the venoms of Nigerian vipers Echis ocellatus and Bitis arietans

Authors: Emeka John Dingwoke, Fatima Adis Adamude, Aliyu Salihu, Mujitaba Suleiman Abubakar, Abdullahi Balarabe Sallau

Source: Tropical Medicine and Health, Vol 52, Iss 1, Pp 1-13 (2024)

Subject Terms: Snake venom, Snake venom metalloproteinases, Snake venom serine proteases, Snake venom phospholipase A2, Toxicological assay, Arctic medicine. Tropical medicine, RC955-962

File Description: electronic resource

Relation: https://doaj.org/toc/1349-4147

Access URL: https://doaj.org/article/3d5f4404eeac488293571af95ecccf2a

Atrase A, a P-III class metalloproteinase purified from cobra venom, exhibits potent anticoagulant activity by inhibiting coagulation pathway and activating the fibrinolytic system

Authors: Zhong, Xin-Jie ^{a, b, c}, Wang, Cai-E ^{c, d}, Li, Ya-Nan ^{a, c}, Zhang, Qi-Yun ^{a, c}, Sun, Qian-Yun ^{a, b, c, ⁎}

Source: In Heliyon 30 May 2024 10(10)

Importance of the Cysteine-Rich Domain of Snake Venom Prothrombin Activators: Insights Gained from Synthetic Neutralizing Antibodies

Authors: Laetitia E. Misson Mindrebo, Jeffrey T. Mindrebo, Quoc Tran, Mark C. Wilkinson, Jessica M. Smith, Megan Verma, Nicholas R. Casewell, Gabriel C. Lander, Joseph G. Jardine

Source: Toxins, Vol 16, Iss 8, p 361 (2024)

Subject Terms: snake venom metalloproteinases, prothrombin activator, Echis, recombinant antivenom, neutralizing antibody, cysteine-rich domain, Medicine

File Description: electronic resource

Relation: https://www.mdpi.com/2072-6651/16/8/361; https://doaj.org/toc/2072-6651

Access URL: https://doaj.org/article/50e022fa1a7441a6b54a54493eb0306b

Comparison of Protein Variation in Protobothrops mucrosquamatus Venom between Northern and Southeast Taiwan and Association with Human Envenoming Effects

Authors: Liao-Chun Chiang, Kun-Yi Chien, Hung-Yuan Su, Yen-Chia Chen, Yan-Chiao Mao, Wen-Guey Wu

Source: Toxins, Vol 14, Iss 9, p 643 (2022)

Subject Terms: Protobothrops mucrosquamatus, inter-population venom variation, snake venom metalloproteinases, phospholipase A2, venom-induced blistering, Medicine

File Description: electronic resource

Relation: https://www.mdpi.com/2072-6651/14/9/643; https://doaj.org/toc/2072-6651

Access URL: https://doaj.org/article/5f52be9e35dd439889305add706ae762

Serum-based inhibition of pitviper venom by eastern indigo snakes (Drymarchon couperi)

Authors: Scott M. Goetz, Sara Piccolomini, Michelle Hoffman, James Bogan, Matthew L. Holding, Mary T. Mendonça, David A. Steen

Source: Biology Open, Vol 8, Iss 3 (2019)

Subject Terms: Agkistrodon, Antagonistic interactions, Hemolytic, Reptile, Snake venom metalloproteinases, Science, Biology (General), QH301-705.5

File Description: electronic resource

Relation: http://bio.biologists.org/content/8/3/bio040964; https://doaj.org/toc/2046-6390

Access URL: https://doaj.org/article/e31843f2a7b4406db0745a410e15a120

Proteomic Analysis of Human Blister Fluids Following Envenomation by Three Snake Species in India: Differential Markers for Venom Mechanisms of Action

Authors: Jéssica K. A. Macêdo, Joseph K. Joseph, Jaideep Menon, Teresa Escalante, Alexandra Rucavado, José María Gutiérrez, Jay W. Fox

Source: Toxins, Vol 11, Iss 5, p 246 (2019)

Subject Terms: proteomics, blister fluid, wound exudate, snake venom, inflammation, extracellular matrix, snake venom metalloproteinases (SVMP), Medicine

File Description: electronic resource

Relation: https://www.mdpi.com/2072-6651/11/5/246; https://doaj.org/toc/2072-6651

Access URL: https://doaj.org/article/245bdc8803bb40f8a482ff13d60338ec

Action of neuwiedase, a metalloproteinase isolated from Bothrops neuwiedi venom, on skeletal muscle: an ultrastructural and immunocytochemistry study

Authors: Baldo, C, Ferreira, MJ, Lopes, DS, Izidoro, LFM, Gomes, AO, Ferro, EAV, Hamaguchi, A, Homsi-Brandeburgo, MI, Rodrigues, VM

Source: Journal of Venomous Animals and Toxins including Tropical Diseases. January 2010 16(3)

Subject Terms: skeletal muscle, neuwiedase, snake venom metalloproteinases, Bothrops neuwiedi

File Description: text/html

Access URL: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992010000300013

Ontogenetic Change in the Venom of Mexican Black-Tailed Rattlesnakes (Crotalus molossus nigrescens)

Authors: Miguel Borja, Edgar Neri-Castro, Rebeca Pérez-Morales, Jason L. Strickland, Roberto Ponce-López, Christopher L. Parkinson, Jorge Espinosa-Fematt, Jorge Sáenz-Mata, Esau Flores-Martínez, Alejandro Alagón, Gamaliel Castañeda-Gaytán

Source: Toxins, Vol 10, Iss 12, p 501 (2018)

Subject Terms: antivenom, crotamine-like myotoxins, life history, phenotypic variability, sexual maturity, snake venom metalloproteinases, snake venom serine proteinases, Medicine

File Description: electronic resource

Relation: https://www.mdpi.com/2072-6651/10/12/501; https://doaj.org/toc/2072-6651

Access URL: https://doaj.org/article/55c27062a09c40c8b40e3df005e6b54b

Why is Skeletal Muscle Regeneration Impaired after Myonecrosis Induced by Viperid Snake Venoms?

Authors: José María Gutiérrez, Teresa Escalante, Rosario Hernández, Stefano Gastaldello, Patricia Saravia-Otten, Alexandra Rucavado

Source: Toxins, Vol 10, Iss 5, p 182 (2018)

Subject Terms: snake venom, myonecrosis, envenoming, muscle regeneration, vasculature, extracellular matrix, snake venom metalloproteinases, phospholipases A2, Medicine

File Description: electronic resource

Relation: http://www.mdpi.com/2072-6651/10/5/182; https://doaj.org/toc/2072-6651

Access URL: https://doaj.org/article/ee1ac99b8fd44ea7968c893559df379f

Action of neuwiedase, a metalloproteinase isolated from Bothrops neuwiedi venom, on skeletal muscle: an ultrastructural and immunocytochemistry study

Authors: C Baldo, MJ Ferreira, DS Lopes, LFM Izidoro, AO Gomes, EAV Ferro, A Hamaguchi, MI Homsi-Brandeburgo, VM Rodrigues

Source: Journal of Venomous Animals and Toxins including Tropical Diseases, Vol 16, Iss 3, Pp 462-469 (2010)

Subject Terms: skeletal muscle, neuwiedase, snake venom metalloproteinases, Bothrops neuwiedi, Arctic medicine. Tropical medicine, RC955-962, Toxicology. Poisons, RA1190-1270, Zoology, QL1-991

File Description: electronic resource

Relation: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992010000300013; https://doaj.org/toc/1678-9199

Access URL: https://doaj.org/article/70f08337aac74713a044f26b3e38e393

Snake Venom Metalloproteinases and Their Peptide Inhibitors from Myanmar Russell’s Viper Venom

Authors: Khin Than Yee, Morgan Pitts, Pumipat Tongyoo, Ponlapat Rojnuckarin, Mark C. Wilkinson

Source: Toxins, Vol 9, Iss 1, p 15 (2016)

Subject Terms: snake venom metalloproteinases, snake venom metalloproteinase inhibitors, Russell’s viper, viper venom, Medicine

File Description: electronic resource

Relation: http://www.mdpi.com/2072-6651/9/1/15; https://doaj.org/toc/2072-6651

Access URL: https://doaj.org/article/5260590f572b4f46b6a48d78ae1f9a69

Viperid Envenomation Wound Exudate Contributes to Increased Vascular Permeability via a DAMPs/TLR-4 Mediated Pathway

Authors: Alexandra Rucavado, Carolina A. Nicolau, Teresa Escalante, Junho Kim, Cristina Herrera, José María Gutiérrez, Jay W. Fox

Source: Toxins, Vol 8, Iss 12, p 349 (2016)

Subject Terms: snake venom metalloproteinases (SVMPs), TLR4, damage associated molecular pattern molecules (DAMPs), exudate, increased vascular permeability, Medicine

File Description: electronic resource

Relation: http://www.mdpi.com/2072-6651/8/12/349; https://doaj.org/toc/2072-6651

Access URL: https://doaj.org/article/d82e8b57cd564f05926f2105bcbc66de

A Comprehensive View of the Structural and Functional Alterations of Extracellular Matrix by Snake Venom Metalloproteinases (SVMPs): Novel Perspectives on the Pathophysiology of Envenoming

Authors: José María Gutiérrez, Teresa Escalante, Alexandra Rucavado, Cristina Herrera, Jay W. Fox

Source: Toxins, Vol 8, Iss 10, p 304 (2016)

Subject Terms: proteomics, exudate, extracellular matrix, basement membrane, hemorrhage, snake venom metalloproteinases, FACITs, Medicine

File Description: electronic resource

Relation: http://www.mdpi.com/2072-6651/8/10/304; https://doaj.org/toc/2072-6651

Access URL: https://doaj.org/article/db92a2fc6930484fb815551e2a9476d6

Novel Catalytically-Inactive PII Metalloproteinases from a Viperid Snake Venom with Substitutions in the Canonical Zinc-Binding Motif

Authors: Erika Camacho, Libia Sanz, Teresa Escalante, Alicia Pérez, Fabián Villalta, Bruno Lomonte, Ana Gisele C. Neves-Ferreira, Andrés Feoli, Juan J. Calvete, José María Gutiérrez, Alexandra Rucavado

Source: Toxins, Vol 8, Iss 10, p 292 (2016)

Subject Terms: snake venom metalloproteinases, PII SVMP homologues, disintegrin domain, zinc-binding motif, hemorrhagic activity, platelet aggregation, proteinase activity, Medicine

File Description: electronic resource

Relation: http://www.mdpi.com/2072-6651/8/10/292; https://doaj.org/toc/2072-6651

Access URL: https://doaj.org/article/cc0167de629043a38f54f1fe7c2da0e1

This result is not displayed to guests.
Login for full access.

This result is not displayed to guests.
Login for full access.

This result is not displayed to guests.
Login for full access.

This result is not displayed to guests.
Login for full access.

This result is not displayed to guests.
Login for full access.