Results 71 to 80 of about 115,349 (202)

The lectin receptor kinase LecRK-I.9 is a novel Phytophthora resistance component and a potential host target for a RXLR effector

open access: yes, 2011
In plants, an active defense against biotrophic pathogens is dependent on a functional continuum between the cell wall (CW) and the plasma membrane (PM). It is thus anticipated that proteins maintaining this continuum also function in defense. The legume-
Sofieke Klamer   +21 more
core   +1 more source

Deletion of haematopoietic Dectin-2 or CARD9 does not protect from atherosclerosis development under hyperglycaemic conditions

open access: yesDiabetes & Vascular Disease Research, 2020
Background: C-type lectin receptors, including Dectin-2, are pattern recognition receptors on monocytes and macrophages that mainly recognize sugars and sugar-like structures present on fungi.
Kathrin Thiem   +17 more
doaj   +1 more source

Sensing of cell death by myeloid C-type lectin receptors [PDF]

open access: yesCurrent Opinion in Immunology, 2013
Molecules associated with dead or dying cells can be detected by receptors on macrophages and dendritic cells. Signals from these receptors impact myeloid cell function and play a role in determining whether death is silent or proinflammatory, tolerogenic or immunogenic. Prominent among myeloid receptors detecting dead cells are C-type lectin receptors
David Sancho, Caetano Reis e Sousa
openaire   +2 more sources

Detecção por abordagem molecular de uma lectina tipo-c na vieira Nodipecten nodosus (Bivalvia: pectinidae) [PDF]

open access: yes, 2015
TCC(graduação) - Universidade Federal de Santa Catarina. Centro de Ciências Biológicas. Biologia.Lectinas tipo-C ou CTLs são proteínas dependentes de Ca2+, capazes de reconhecer açúcares específicos da superfície de células e causar sua aglutinação ...
Rizzato, Gabrielle Azevedo
core  

Molecular insights into the transport lectin function of ERGIC-53 [PDF]

open access: yes, 2004
Secretion of proteins is an essential function of eukaryotic cells. The secretory proteins’ journey along the organelles of the exocytic pathway is initiated by the exit from the endoplasmic reticulum (ER), which defines a major rate-limiting step for ...
Appenzeller-Herzog, Christian
core   +1 more source

Towards defining the role of glycans as hardware in information storage and transfer: Basic principles, experimental approaches and recent progress [PDF]

open access: yes, 2001
The term `code' in biological information transfer appears to be tightly and hitherto exclusively connected with the genetic code based on nucleotides and translated into functional activities via proteins.
Jiménez-Barbero, J.   +6 more
core   +1 more source

ABO Antigens Active Tri- and Disaccharides Microarray to Evaluate C-type Lectin Receptor Binding Preferences

open access: yes, 2018
Understanding blood group antigen binding preferences for C-type lectin receptors holds promise for modulating immune responses, since several Gram-negative bacteria express blood group antigens as molecular mimicry to evade immune responses.
Balamurugan Subramani   +8 more
core   +1 more source

Comparative genomics of natural killer cell receptor gene clusters.

open access: yesPLoS Genetics, 2005
Many receptors on natural killer (NK) cells recognize major histocompatibility complex class I molecules in order to monitor unhealthy tissues, such as cells infected with viruses, and some tumors.
James Kelley   +2 more
doaj   +2 more sources

Protocol to identify the ligand binding site of Mincle using NMR spectroscopy

open access: yesSTAR Protocols
Summary: Mincle (macrophage-inducible C-type lectin, CLEC4E) is a C-type lectin immune-stimulatory receptor that can be targeted for inducing potent adjuvant effects. Mincle can recognize trehalose dimycolate and related glycolipids.
Atsushi Furukawa   +3 more
doaj   +1 more source

New Binding Face of C-type Lectin-like Domains

open access: yes, 2014
C-type lectin-like receptor 2 (CLEC-2) is a member of the C-type lectin (like) receptor (CLR) family that uses a Ca2+ binding domain to bind specific glycans.
Fukuhara, Hideo   +2 more
core   +1 more source

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