Results 101 to 110 of about 61,632 (321)

Acanthamoeba Mannose and Laminin Binding Proteins Variation across Species and Genotypes

Microorganisms, 2022
Acanthamoeba is a ubiquitous free-living amoeba capable of being an opportunistic pathogen in humans and animals. A critical step in infection is the adhesion of the amoeba to host cells and tissues, and two major parasite adhesins, mannose-binding ...
Daniele Corsaro
doaj   +1 more source

Glycans and Chirality: Stereoselectivity at the Core of DC‐SIGN's Recognition. A Novel View of the Optimum Minimal Ligand Epitope

Chemistry – A European Journal, EarlyView.
The stereochemical diversity of the “glycan code” enables similar chiral motifs to arise from both D‐ and L‐sugars. Focused on DC‐SIGN–glycan recognition, two diverse monosaccharide scaffolds, D‐Man (D‐Rha) and L‐Gal (L‐Fuc), maintain the exquisite stereochemistry encoded in the minimal binding epitope.
J. Daniel Martínez, Reyes Núñez‐Franco, Pablo Valverde, Sandra Delgado, Ana Ardá, Jesús Jiménez‐Barbero, Gonzalo Jiménez‐Oses, F. Javier Cañada   +7 more
wiley   +1 more source

Molecular recognition of surface-immobilized carbohydrates by a synthetic lectin

Beilstein Journal of Organic Chemistry, 2014
The molecular recognition of carbohydrates and proteins mediates a wide range of physiological processes and the development of synthetic carbohydrate receptors (“synthetic lectins”) constitutes a key advance in biomedical technology.
Melanie Rauschenberg, Eva-Corrina Fritz, Christian Schulz, Tobias Kaufmann, Bart Jan Ravoo   +4 more
doaj   +1 more source

Structural basis for disparate sugar-binding specificities in the homologous cargo receptors ERGIC-53 and VIP36. [PDF]

PLoS ONE, 2014
ERGIC-53 and VIP36 are categorized as leguminous type (L-type) lectins, and they function as cargo receptors for trafficking certain N-linked glycoproteins in the secretory pathway in animal cells. They share structural similarities in their carbohydrate
Tadashi Satoh, Kousuke Suzuki, Takumi Yamaguchi, Koichi Kato   +3 more
doaj   +1 more source

Synthesis of Rhamnose‐Modified Lewis‐X‐Containing Saponins

European Journal of Organic Chemistry, EarlyView.
The synthesis of triterpenoid saponins bearing a Lewis‐X trisaccharide analogue, in which the fucose residue is replaced by a rhamnose, is presented. These saponins, designed as negative controls in dendritic cell‐specific intercellular adhesion molecule‐3‐grabbing nonintegrin‐targeted therapeutic applications, are prepared through iterative and ...
Oscar Javier Gamboa Marin, Nitish Verma, Maude Cloutier, Charles Gauthier   +3 more
wiley   +1 more source

A human mannose-binding protein is an acute-phase reactant that shares sequence homology with other vertebrate lectins [published erratum appears in J Exp Med 1991 Sep 1;174(3):753]

Journal of Experimental Medicine, 1988
Mannose-binding proteins have been isolated from the liver of rats and humans and subsequently been found in the serum of rats, rabbits, and humans. We report the isolation of cDNA clones isolated from a human liver cDNA library that encodes a human ...
By, B. Alan, Ezekowitz, E. Linda, Day, Gary, Herman   +6 more
semanticscholar   +1 more source

Possible role for cell-surface carbohydrate-binding molecules in lymphocyte recirculation. [PDF]

, 1983
We are investigating the hypothesis that carbohydrate-binding molecules on the cell surface are involved in the recirculation of lymphocytes from the bloodstream into lymphoid organs.
Rosen, SD, Stoolman, LM
core   +1 more source

Detection of Sugar-Lectin Interactions by Multivalent Dendritic Sugar Functionalized Single-Walled Carbon Nanotubes

, 2012
We show that single walled carbon nanotubes (SWNT) decorated with sugar functionalized poly (propyl ether imine) (PETIM) dendrimer is a very sensitive platform to quantitatively detect carbohydrate recognizing proteins, namely, lectins.
A. K. Sood, K. Naresh, K. S. Vasu, Lee Y. C., N. Jayaraman, R. S. Bagul, So L. L.   +6 more
core   +1 more source

Mannose-binding lectin and maladies of the bowel and liver

World Journal of Gastroenterology, 2006
Mannose-binding lectin (MBL) is a pattern-recognition molecule that binds to characteristic carbohydrate motifs present on the surface of many different pathogens. MBL binding stimulates the immune system via the lectin pathway of complement activation.
Worthley, D., Bardy, P., Gordon, D., Mullighan, C.   +3 more
openaire   +4 more sources

Characterization of the complex between mannose-binding lectin trimer and mannose-binding lectin-associated serine proteases [PDF]

Microbiology and Immunology, 2011
Mannose-binding lectin (MBL) is an oligomeric serum lectin involved in innate immunity. Human MBL is complexed with three types of serine proteases (MASP-1, MASP-2 and MASP-3) and two types of their truncated forms (sMAP and MAp44). When an MBL complex binds to carbohydrates of pathogens, the complement system is activated via the lectin pathway. Human
Teizo Fujita, Misao Matsushita, Koichiro Tateishi, Takahiro Kanemoto   +3 more
openaire   +3 more sources