Glycoproteins Stocks List

Related ETFs - A few ETFs which own one or more of the above listed Glycoproteins stocks.

Symbol Grade Name Weight

View all Glycoproteins related ETFs...

Compare ETFs

    Recent Signals

    Date Stock Signal Type
    2021-05-13 BVXP Crossed Above 50 DMA Bullish
    2021-05-13 BVXP 200 DMA Resistance Bearish
    2021-05-13 BVXP NR7 Range Contraction
    2021-05-13 BVXP Narrow Range Bar Range Contraction
    2021-05-13 BVXP Stochastic Reached Overbought Strength
    2021-05-13 BVXP Non-ADX 1,2,3,4 Bullish Bullish Swing Setup
    2021-05-13 FAB Bollinger Band Squeeze Range Contraction
    2021-05-13 FAB Fell Below 50 DMA Bearish
    2021-05-13 FAB Narrow Range Bar Range Contraction
    2021-05-13 ODX Lizard Bullish Bullish Day Trade Setup
    2021-05-13 ODX 200 DMA Resistance Bearish
    2021-05-13 ODX Hammer Candlestick Bullish
    2021-05-13 ODX Doji - Bullish? Reversal

    Recent News for Glycoproteins Stocks

    Date Stock Title

    Glycoproteins are proteins which contain oligosaccharide chains (glycans) covalently attached to amino acid side-chains. The carbohydrate is attached to the protein in a cotranslational or posttranslational modification. This process is known as glycosylation. Secreted extracellular proteins are often glycosylated.
    In proteins that have segments extending extracellularly, the extracellular segments are also often glycosylated. Glycoproteins are also often important integral membrane proteins, where they play a role in cell–cell interactions. It is important to distinguish endoplasmic reticulum-based glycosylation of the secretory system from reversible cytosolic-nuclear glycosylation. Glycoproteins of the cytosol and nucleus can be modified through the reversible addition of a single GlcNAc residue that is considered reciprocal to phosphorylation and the functions of these are likely to be additional regulatory mechanism that controls phosphorylation-based signalling. In contrast, classical secretory glycosylation can be structurally essential. For example, inhibition of asparagine-linked, i.e. N-linked, glycosylation can prevent proper glycoprotein folding and full inhibition can be toxic to an individual cell. In contrast, perturbation of glycan processing (enzymatic removal/addition of carbohydrate residues to the glycan), which occurs in both the endoplastic reticulum and Golgi apparatus, is dispensable for isolated cells (as evidence by survival with glycosides inhibitors) but can lead to human disease (congenital disorders of glycosylation) and can be lethal in animal models. It is therefore likely that the fine processing of glycans is important for endogenous functionality, such as cell trafficking, but that this is likely to have been secondary to its role in host-pathogen interactions. A famous example of this latter effect is the ABO blood group system.

    More about Glycoproteins
    Browse All Tags