Results 1 to 10 of about 75,275 (165)

Lectins as Natural Antibiofilm Agents in the Fight Against Antibiotic Resistance: A Review [PDF]

open access: yesMolecules
Biofilms are complex microbial communities embedded in a self-produced extracellular polymeric matrix. These structures confer increased resistance/tolerance to antimicrobial agents and immune responses, posing a serious challenge in both clinical and ...
Thiago Henrique Napoleão   +4 more
doaj   +2 more sources

Lectins with Potential for Anti-Cancer Therapy

open access: yesMolecules, 2015
This article reviews lectins of animal and plant origin that induce apoptosis and autophagy of cancer cells and hence possess the potential of being developed into anticancer drugs. Apoptosis-inducing lectins encompass galectins, C-type lectins, annexins,
Xiuli Dan, Tzi Bun Ng
exaly   +3 more sources

An Update of Lectins from Marine Organisms: Characterization, Extraction Methodology, and Potential Biofunctional Applications

open access: yesMarine Drugs, 2022
Lectins are a unique group of nonimmune carbohydrate-binding proteins or glycoproteins that exhibit specific and reversible carbohydrate-binding activity in a non-catalytic manner.
Mirja Kaizer Ahmmed   +16 more
doaj   +1 more source

Man-Specific Lectins from Plants, Fungi, Algae and Cyanobacteria, as Potential Blockers for SARS-CoV, MERS-CoV and SARS-CoV-2 (COVID-19) Coronaviruses: Biomedical Perspectives

open access: yesCells, 2021
Betacoronaviruses, responsible for the “Severe Acute Respiratory Syndrome” (SARS) and the “Middle East Respiratory Syndrome” (MERS), use the spikes protruding from the virion envelope to attach and subsequently infect the host cells.
Annick Barre   +7 more
doaj   +1 more source

Can Plant Lectins Help to Elucidate Insect Lectin-Mediated Immune Response?

open access: yesInsects, 2021
Lectins are carbohydrate-binding proteins that recognize and selectively bind to specific sugar structures. This group of proteins is widespread in plants, animals, and microorganisms, and exerts a broad range of functions.
Pengyu Chen   +3 more
doaj   +1 more source

Russulaceae FAMILY MUSHROOMS LECTINS: FUNCTION, PURIFICATION, STRUCTURAL FEATURES AND POSSIBILITIES OF PRACTICAL APPLICATIONS [PDF]

open access: yesBiotechnologia Acta, 2019
The purpose of this paper was to analise the results of own author’s research and literature date of other authors that concerned lectins of Russulaceae family mushrooms, which, despite their widespread, are still poorly investigated. Most studies merely
Panchak L. V.
doaj   +1 more source

Antioxidant and antimicrobial activities of Penicillium sp. lectins [PDF]

open access: yesArchives of Biological Sciences, 2019
Lectins are a diverse group of proteins of non-immune origin that interact specifically with glycans. Owing to their specificity, they can mediate various cellular and molecular recognition processes.
Singh Ram S., Walia Amandeep K.
doaj   +1 more source

Characterization and antimicrobial activity of lectins purified from three Egyptian leguminous seeds

open access: yesAMB Express, 2020
Lectins are carbohydrate-binding proteins that play vital roles in many biological processes. In this study, lectins from three Egyptian cultivars (fava bean, lentil, and pea) were isolated by precipitation with different concentrations of ammonium ...
Magda M. El-Araby   +3 more
doaj   +1 more source

Partial Purification and Characterization of the Lectins of Two Varieties of Phaseolus coccineus (Ayocote Bean)

open access: yesAgronomy, 2022
In this study, a partial purification and characterization of the lectins from two varieties of Phaseolus coccineus (black and purple ayocote bean) was carried out.
Leopoldo González-Cruz   +5 more
doaj   +1 more source

Lectins with Anti-HIV Activity: A Review

open access: yesMolecules, 2015
Lectins including flowering plant lectins, algal lectins, cyanobacterial lectins, actinomycete lectin, worm lectins, and the nonpeptidic lectin mimics pradimicins and benanomicins, exhibit anti-HIV activity.
Ouafae Akkouh   +7 more
doaj   +1 more source

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