Results 201 to 210 of about 50,143 (258)

Integrative transcriptomic and machine learning approaches reveal candidate genes for silk and venom production in Bibionomorpha (Diptera)

open access: yesInsect Molecular Biology, EarlyView.
Multi‐species transcriptomics and deep learning identified candidate genes associated with silk and venom production in Bibionomorpha. Venom‐associated genes were enriched in proteases, inhibitors and pore‐forming proteins, whereas silk‐related genes showed chitin‐binding and peritrophin domains. Integrating co‐expression networks, machine learning and
Daniel Kenji Matuo   +2 more
wiley   +1 more source

Siglec Expression Patterns in Food Allergy Reveal Altered Intensity but Not Frequency

open access: yes
Clinical &Experimental Allergy, EarlyView.
J. S. H. Schaapherder   +5 more
wiley   +1 more source
Some of the next articles are maybe not open access.

Related searches:

Lectins

Current Opinion in Structural Biology, 1999
Lectins - carbohydrate-binding proteins involved in a variety of recognition processes - exhibit considerable structural diversity. Three new lectin folds and further elaborations of known folds have been described recently. Large variability in quaternary association resulting from small alterations in essentially the same tertiary structure is a ...
Vijayan, M, Chandra, Nagasuma
openaire   +2 more sources

Cold Lectins

Vox Sanguinis, 1963
SummaryPlant agglutinins are described which act more strongly as temperature is decreased. Crotalaria mucronata as well as variants of Phaseolus lunatus contain pronounced cold agglutinins against B cells while their action on A1‐cells is not enhanced with decreasing temperature.
F, OTTENSOOSER, M, SATO
openaire   +2 more sources

Lectins and Biocontrol

Critical Reviews in Biotechnology, 1997
The harmful effects of chemical pesticides on the environment and human health have inspired a search for safer, environmentally-friendly control alternatives. The great advances in biotechnology, supported by basic studies utilizing molecular biology tools, have made biological control (i.e., the use of antagonistic microorganisms, fungi, or bacteria ...
J, Inbar, I, Chet
openaire   +2 more sources

Synthetic Lectins

Organic & Biomolecular Chemistry, 2009
Carbohydrate recognition presents a difficult challenge to supramolecular chemists, especially in the natural medium of water. After two decades of research, it has at last been possible to develop biomimetic receptors which perform well in aqueous solution.
openaire   +5 more sources

Nucleocytoplasmic lectins

Biochimica et Biophysica Acta (BBA) - General Subjects, 2004
This review summarizes studies on lectins that have been documented to be in the cytoplasm and nucleus of cells. Of these intracellular lectins, the most extensively studied are members of the galectin family. Galectin-1 and galectin-3 have been identified as pre-mRNA splicing factors in the nucleus, in conjunction with their interacting ligand, Gemin4.
John L, Wang   +3 more
openaire   +2 more sources

LECTINS*

Annals of the New York Academy of Sciences, 1970
SUMMARYBlood group specific plant agglutinins (named lectins by the present author) were discovered in 1945, first mentioned in 1947, and described in detail by Renkonen in 1948 and by Boyd in 1949. Similar agglutinins have since been found in some invertebrates. Thousands of species have now been screened for such activity.
openaire   +2 more sources

Bifunctional properties of lectins: lectins redefined

Trends in Biochemical Sciences, 1988
Abstract Both ‘classical' lectins, originally identified as cell agglutinins, and other carbohydrate-binding proteins that were identified by different means, may contain a second type of binding site that is specific for a non-carbohydrate ligand.
openaire   +2 more sources

Lectins in the unicellular Tetrahymena. I. Lectin detection with FITC-labeled anti-lectins

Acta Histochemica, 1983
FITC-labeled antibodies prepared in rabbits to bean, pea, lens, datura, and snail lectin indicated by immunological reaction presence in the Tetrahymena of corresponding lectin-like components. The latter localized partly on the surface, partly inside the body of the unicellular.
G, Csaba, P, Kovács
openaire   +2 more sources

Home - About - Disclaimer - Privacy