Glycoproteins Stocks List

Recent Signals

Date Stock Signal Type
2019-08-16 ADMA Shooting Star Candlestick Bearish
2019-08-16 ADMA MACD Bullish Centerline Cross Bullish
2019-08-16 ADMA Stochastic Sell Signal Bearish
2019-08-16 ADMA NR7 Range Contraction
2019-08-16 BCEL Pocket Pivot Bullish Swing Setup
2019-08-16 BCEL Stochastic Reached Overbought Strength
2019-08-16 CBPO MACD Bullish Signal Line Cross Bullish
2019-08-16 EQ Narrow Range Bar Range Contraction
2019-08-16 EQ NR7 Range Contraction
2019-08-16 EQ Non-ADX 1,2,3,4 Bearish Bearish Swing Setup
2019-08-16 MNTA NR7 Range Contraction
2019-08-16 XNCR New Uptrend Bullish
2019-08-16 XNCR 50 DMA Support Bullish
2019-08-16 XNCR 20 DMA Resistance Bearish
2019-08-16 ZYME Upper Bollinger Band Walk Strength
2019-08-16 ZYME Stochastic Reached Overbought Strength
2019-08-16 ZYME New 52 Week Closing High Bullish
2019-08-16 ZYME New 52 Week High Strength
2019-08-16 ZYME Pocket Pivot Bullish Swing Setup

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.

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