Results 51 to 60 of about 51,218 (319)

ALT-C, a disintegrin-like Cys-rich protein from Bothrops alternatus, increases skeletal myoblast viability

Journal of Venomous Animals and Toxins including Tropical Diseases, 2009
ALT-C, an ECD motif (glutamic acid, cysteine, aspartic acid) disintegrin from Bothrops alternatus snake venom, induces α2β1 integrin-mediated signaling and neutrophil chemotaxis.
RA Mesquita-Ferrari, CK de Moraes, KC Micocci, HS Selistre-de-Araújo   +3 more
doaj   +1 more source

Removal of extracellular human amyloid beta aggregates by extracellular proteases in C. elegans

eLife, 2023
The amyloid beta (Aβ) plaques found in Alzheimer’s disease (AD) patients’ brains contain collagens and are embedded extracellularly. Several collagens have been proposed to influence Aβ aggregate formation, yet their role in clearance is unknown.
Elisabeth Jongsma, Anita Goyala, José Maria Mateos, Collin Yvès Ewald   +3 more
doaj   +1 more source

A Disintegrin and Metalloproteases (ADAMs) in Cardiovascular, Metabolic and Inflammatory Diseases: Aspects for Theranostic Approaches

Thrombosis and Haemostasis, 2018
A disintegrin and metalloproteases (ADAMs) are membrane-bound enzymes responsible for the shedding or cleavage of various cell surface molecules, such as adhesion molecules, cytokines/chemokines and growth factors. This shedding can result in the release
Emiel P. C. van der Vorst, C. Weber, M. Donners   +2 more
semanticscholar   +1 more source

Antitumor and anti-angiogenic activity of the recombinant human disintegrin domain of A disintegrin and metalloproteinase 15

Molecular Medicine Reports, 2015
A disintegrin and metalloproteinases (ADAMs), a family of transmembrane glycoproteins, are expressed in numerous tissues and organs, and have been implicated in a variety of physiological and pathological processes. ADAM15 is unique among the ADAMs in having an Arg-Gly-Asp motif in its disintegrin domain.
Xin Ma, Yun Chen, Yanfei Cai, Min Chu, Ying Hou, Jian Jin, Ruiyu Zhu, Jianyong Lei, Xiaohai Gong   +8 more
openaire   +4 more sources

Tissue Localization and Extracellular Matrix Degradation by PI, PII and PIII Snake Venom Metalloproteinases: Clues on the Mechanisms of Venom-Induced Hemorrhage [PDF]

, 2015
20 páginas, 4 figuras, 3 tablas y 7 tablas en material suplementario.Snake venom hemorrhagic metalloproteinases (SVMPs) of the PI, PII and PIII classes were compared in terms of tissue localization and their ability to hydrolyze basement membrane ...
A Osaka, A Rucavado, A Rucavado, AF Pinto, AK Oliveira, Alexandra Rucavado, AM Moura-da-Silva, AM Moura-da-Silva, Ana Moura, BG Fry, C Baldo, Cristina Herrera, DB Gould, Diego Morazán, E Camacho, EN Baramova, EN Baramova, EN Baramova, J Durban, Jay W. Fox, JJ Calvete, JM Gutiérrez, JM Gutiérrez, JM Gutiérrez, JM Gutiérrez, José María Gutiérrez, Juan J. Calvete, JW Fox, Jéssica Kele A. Macêdo, K Kühn, K Kühn, L Watanabe, Libia Sanz, Mathieu-Benoit Voisin, N Jiménez, NR Casewell, NR Casewell, NR Casewell, PD Yurchenco, PD Yurchenco, R Timpl, SM Serrano, SM Serrano, SM Serrano, Sussan Nourshargh, SV Costes, T Escalante, T Escalante, T Escalante, T Nikai, Teresa Escalante, UK Laemmli, WJ Wang   +52 more
core   +4 more sources

The Anti-Cancer Potency and Mechanism of a Novel Tumor-Activated Fused Toxin, DLM

Toxins, 2015
Melittin, which acts as a membrane-disrupting lytic peptide, is not only cytotoxic to tumors, but also vital to normal cells. Melittin had low toxicity when coupled with target peptides.
Dejun Sun, Miaonan Sun, Wenhe Zhu, Zhiding Wang, Yuefei Li, Jie Ma   +5 more
doaj   +1 more source

ADAMTS -1 and -4 are up-regulated following transient middle cerebral artery occlusion in the rat and their expression is modulated by TNF in cultured astrocytes [PDF]

, 2006
ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) enzymes are a recently described group of metalloproteinases. The substrates degraded by ADAMTS-1, -4 and -5 suggests that they play a role in turnover of extracellular matrix in the
A.K. Cross, Abbaszzade, Asher, Bandtlow, Buttini, C.J. Stock, Cardenas, Clark, Clausen, Collins-Racie, D.J. Buttle, Eddleston, G. Haddock, Hashimoto, Inatani, J. Surr, Jiang, Jones, Krekoski, Krupinski, Kuno, Kuno, Kurazono, Legos, M.N. Woodroofe, Medina-Flores, Miguel, Mulcahy, Nedergaard, Novak, Ohtaki, Pangalos, Pekny, Plumb, Porter, R.A.D. Bunning, Rawlings, Rhodes, Rosenberg, Rosenberg, Rothwell, S. Allan, Satoh, Smith, Sobel, Somerville, Tang, Tsuzaki, Vankemmelbeke, Vazquez, Wang, Yamaguchi, Yu   +52 more
core   +1 more source

Expression of ADAMs (“a disintegrin and metalloprotease”) in the human lung [PDF]

Virchows Archiv, 2009
In view of the associations of "a disintegrin and metalloprotease" (ADAM) with respiratory diseases, we assessed the expression of various ADAMs in human lung tissue. Lung tissue was obtained from nine individuals who underwent surgery for lung cancer or underwent lung transplantation for emphysema.
Antoon Dijkstra, Wim Timens, Dirkje S. Postma, Jacobien A. Noordhoek, Monique E. Lodewijk, Henk F. Kauffman, Nick H. T. ten Hacken   +6 more
openaire   +4 more sources

Immuno Magnetic Thermosensitive Liposomes For Cancer Therapy [PDF]

, 2019
The present work describes the encapsulation of the drug doxorubicin (DOX) in immuno paramagnetic thermosensitive liposomes. DOX is the most common chemotherapeutic agent for the treatment of a variety of carcinomas.
Alawak, Mohamad
core   +1 more source

Alternagin-C (ALT-C), a Disintegrin-Like Cys-Rich Protein Isolated from the Venom of the Snake Rhinocerophis alternatus, Stimulates Angiogenesis and Antioxidant Defenses in the Liver of Freshwater Fish, Hoplias malabaricus

Toxins, 2017
Alternagin-C (ALT-C) is a disintegrin-like protein isolated from Rhinocerophis alternatus snake venom, which induces endothelial cell proliferation and angiogenesis.
Diana Amaral Monteiro, Heloisa Sobreiro Selistre-de-Araújo, Driele Tavares, Marisa Narciso Fernandes, Ana Lúcia Kalinin, Francisco Tadeu Rantin   +5 more
doaj   +1 more source