Results 51 to 60 of about 243,058 (345)

Structurally Robust and Functionally Highly Versatile—C-Type Lectin (-Related) Proteins in Snake Venoms

open access: yesToxins, 2019
Snake venoms contain an astounding variety of different proteins. Among them are numerous C-type lectin family members, which are grouped into classical Ca2+- and sugar-binding lectins and the non-sugar-binding snake venom C-type lectin-related proteins (
Johannes A. Eble
doaj   +1 more source

Crystal Structure of the Cysteine-Rich Domain of Mannose Receptor Complexed with a Sulfated Carbohydrate Ligand [PDF]

open access: yes, 2000
The macrophage and epithelial cell mannose receptor (MR) binds carbohydrates on foreign and host molecules. Two portions of MR recognize carbohydrates: tandemly arranged C-type lectin domains facilitate carbohydrate-dependent macrophage uptake of ...
Bjorkman, Pamela J.   +6 more
core   +2 more sources

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

Detection of inflammation- and neoplasia-associated alterations in human large intestine using plant/invertebrate lectins, galectin-1 and neoglycoproteins [PDF]

open access: yes, 1998
Commonly, plant and invertebrate lectins are accepted glycohistochemical tools for the analysis of normal and altered structures of glycans in histology and pathology.
Bosbach, R.   +3 more
core   +1 more source

C-type lectins facilitate tumor metastasis

open access: yesOncology Letters, 2016
Metastasis, a life-threatening complication of cancer, leads to the majority of cases of cancer-associated mortality. Unfortunately, the underlying molecular and cellular mechanisms of cancer metastasis remain to be fully elucidated. C-type lectins are a large group of proteins, which share structurally homologous carbohydrate-recognition domains (CRDs)
Ding, Dongbing   +4 more
openaire   +3 more sources

C-Type Lectin Receptors in Host Defense Against Bacterial Pathogens

open access: yesFrontiers in Cellular and Infection Microbiology, 2020
Antigen-presenting cells (APCs) are present throughout the human body—in tissues, at barrier sites and in the circulation. They are critical for processing external signals to instruct both local and systemic responses toward immune tolerance or immune ...
Malgorzata E. Mnich   +4 more
doaj   +1 more source

Signaling pathways for transduction of the initial message of the glycocode into cellular responses [PDF]

open access: yes, 1998
The sugar units of glycan structures store information and establish an alphabet of life. The language of the oligosaccharide coding units is deciphered by receptors such as lectins and the decoded message can be transduced by multiple signaling pathways.
Gabius, Hans-Joachim, Villalobo, A.
core   +2 more sources

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

Differing Expression and Potential Immunological Role of C-Type Lectin Receptors of Two Different Chicken Breeds against Low Pathogenic H9N2 Avian Influenza Virus

open access: yesPathogens
Diverse immune responses in different chicken lines can result in varying clinical consequences following avian influenza virus (AIV) infection. We compared two widely used layer breeds, Lohmann Brown (LB) and Lohmann White (LW), to examine virus ...
Sungsu Youk   +2 more
doaj   +1 more source

Cytotoxicity and Glycan-Binding Properties of an 18 kDa Lectin Isolated from the Marine Sponge <em>Halichondria </em><em>o</em><em>kadai</em>

open access: yesToxins, 2012
A divalent cation-independent lectin—HOL-18, with cytotoxic activity against leukemia cells, was purified from a demosponge, <em>Halichondria okadai</em>. HOL-18 is a 72 kDa tetrameric lectin that consists of four non-covalently bonded 18 kDa
Yasuhiro Ozeki   +15 more
doaj   +1 more source

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