User:Hzeidieh/sandbox

"Article Evaluation"

Article title: Antibody.

Everything in the article is relevant to the article topic and there is nothing distracted me. I think the article is well structured and organized. it includes relevant information that all related to the same topic which is antibody. the article is neutral and there is no biased toward a particular position. there are no viewpoints that are overreresented or underrepresented.

the sources that are used in this article are referenced with an appropriate, reliable reference and they are neutral.

there are no massages in the talk page for this article.

"Article selection"

article 1: "Isomaltose"

Article 2: "Gelatinase"

Article 3: "hemagglutininesterase"

The three articles are enzyme related and they are a stub articles. they have very little information and need to be expanded.

Lead section:

Hemagglutinin esterase (HEs) is a glycoprotein that certain enveloped viruses possess and use as invading mechanism. HEs helps in the attachment and destruction of certain sialic acid receptors that are found on the host cell surface. Viruses that possess HEs include influenza C, Toro-viruses, and coronaviruses. HEs is a dimer transmembrane protein consisting of two monomers, each monomer is made of three domains. The three domains are: membrane fusion, esterase, and receptor binding domains.

The different HEs enzyme activities include: receptor binding activity, receptor hydrolysis (esterase) activity, and membrane fusion activity. The receptor binding activity involve the attachment of HEs to N-acetyl-9-O-acetylneuraminic acid (9-O-Ac- Neu5Ac) of glycolipids and glycoproteins and in turn serve as viral receptor. Receptor hydrolysis (esterase) activity allows virus particles to escape the infected cell by removing an acetyl group from the C9 position of terminal 9-O-Ac-Neu5Ac residues. Membrane fusion activity helps in incorporation viral genome into the host cell cytoplasm by enhancing the attachment between the viral envelope and host cell membrane.

drafting:

Structure of Hemagglutinin Esterase:

Certain studies reveled that coronavirus and Toro-viruses HE was originated from HEF glycoprotein that is found in influenza C viruses which resulted from alteration of Hemagglutinin esterase from a trimer into a dimer glycoprotein. During this process, the Receptor destroying enzyme acetyl esterase domain stayed unchanged. However, the HE receptor binding domain has been altered in which that the ligand is bound in opposite orientation than before. Both coronavirus and Toro-viruses HE monomers are made up of the same three domains which are:  central esterase/hydrolase domain, receptor binding lectin domain, and membrane proximal domain which is small.

Both coronavirus (CoV) and Toro-viruses (ToV) HE monomers are made up of the same three domains which are:  central esterase/hydrolase domain, receptor binding lectin domain, and membrane proximal domain which is small. The two monomers of HE dimer in both CoV and ToV involve the same two contact regions 1 that contain the receptor binding domain and Contact region 2 that contain membrane proximal domain. Yet, ToV HE contacts region 2 contain additional esterase domain. As a result, the CR2 surface is larger in ToV HEs than in CoV HEs. However, Close to the carboxylic terminal membrane anchor, there are number of disulfide bridges between Cys385of Coronavirus HE that in turn keep the HE dimers connected to each other.