Results 51 to 60 of about 69,976 (338)

Endogenous mammalian lectin localized extracellularly in lung elastic fibers. [PDF]

open access: yes, 1984
An affinity-purified antibody preparation raised against a beta-galactoside-binding lectin from bovine lung was used to localize a similar lectin in rat lung by immunofluorescence and by electron microscopy after on-grid staining visualized with ...
Barondes, SH   +2 more
core   +3 more sources

High Bacterial Agglutination Activity in a Single-CRD C-Type Lectin from Spodoptera exigua (Lepidoptera: Noctuidae)

open access: yesBiosensors, 2017
Lectins are carbohydrate-interacting proteins that play a pivotal role in multiple physiological and developmental aspects of all organisms. They can specifically interact with different bacterial and viral pathogens through carbohydrate-recognition ...
Leila Gasmi   +2 more
doaj   +1 more source

Transgenic Expression of Human C-Type Lectin Protein CLEC18A Reduces Dengue Virus Type 2 Infectivity in Aedes aegypti

open access: yesFrontiers in Immunology, 2021
The C-type lectins, one family of lectins featuring carbohydrate binding domains which participate in a variety of bioprocesses in both humans and mosquitoes, including immune response, are known to target DENV.
Lie Cheng   +18 more
doaj   +1 more source

Human Galectins Induce Conversion of Dermal Fibroblasts into Myofibroblasts and Production of Extracellular Matrix: Potential Application in Tissue Engineering and Wound Repair [PDF]

open access: yes, 2011
Members of the galectin family of endogenous lectins are potent adhesion/growth-regulatory effectors. Their multi-functionality opens possibilities for their use in bioapplications. We studied whether human galectins induce the conversion of human dermal
André A., S.   +47 more
core   +1 more source

Drosophila C-type lectins enhance cellular encapsulation [PDF]

open access: yesMolecular Immunology, 2007
C-type lectins are calcium-dependent carbohydrate binding proteins, and animal C-type lectins participate in innate immunity and cell-cell interactions. In the fruit fly Drosophila melanogaster, more than 30 genes encode C-type lectin domains. However, functions of Drosophila C-type lectins in innate immunity are not well understood.
Jingqun, Ao, Erjun, Ling, Xiao-Qiang, Yu
openaire   +2 more sources

Lectins bring benefits to bones

open access: yeseLife, 2016
The discovery that proteins called c-type lectins promote bone growth could lead to new treatments for age-related bone disorders.
Charles KF Chan   +2 more
doaj   +1 more source

Evolution of plant ribosome-inactivating proteins [PDF]

open access: yes, 2010
This contribution presents an updated analysis of the evolution of ribosome-inactivating proteins (RIPs) in plants. All evidence suggests that an ancestor of modern seed plants developed the RIP domain at least 300 million years ago.
Peumans, Willy J, Van Damme, Els
core   +1 more source

Supplementary Figure S6 from Elevated Expression of the C-Type Lectin CD93 in the Glioblastoma Vasculature Regulates Cytoskeletal Rearrangements That Enhance Vessel Function and Reduce Host Survival [PDF]

open access: gold, 2023
Elise Langenkamp   +12 more
openalex   +2 more sources

RIPK4 function interferes with melanoma cell adhesion and metastasis

open access: yesMolecular Oncology, EarlyView.
RIPK4 promotes melanoma growth and spread. RIPK4 levels increase as skin lesions progress to melanoma. CRISPR/Cas9‐mediated deletion of RIPK4 causes melanoma cells to form less compact spheroids, reduces their migratory and invasive abilities and limits tumour growth and dissemination in mouse models.
Norbert Wronski   +9 more
wiley   +1 more source

Evolution and Immune Function of Fish Lectins [PDF]

open access: yes, 2016
Lectins are sugar-binding proteins widely distributed among animals, plants, and microbial taxon, involved in diverse biological processes. In both invertebrates and vertebrates, they play key roles in nonself recognition and immune responses, such as ...
Ahmad   +95 more
core   +1 more source

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