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	<Article> 

	<Journal> 

	<PublisherName>International Science Community Association</PublisherName>

	<JournalTitle>International Research Journal of Biological Sciences</JournalTitle> 

	<Issn>2278 - 3202</Issn>

	<Volume>6</Volume>

	<Issue>6</Issue>

	<PubDate PubStatus="ppublish"> 

	<Year>2017</Year> 

	<Month>06</Month> 

	<Day>10</Day> 

	</PubDate>

	</Journal>



	<ArticleTitle>Comparative analysis of Homo sapiens ERBB2 erb-b2 receptor tyrosine kinase 2</ArticleTitle> 


	<FirstPage>1</FirstPage>

	<LastPage>6</LastPage>



	<ELocationID EIdType="pii"></ELocationID>

	<Language>EN</Language> 
	<AuthorList>

	
		<Author> 

		<FirstName>Raza</FirstName>

		<MiddleName> </MiddleName>

		<LastName>Shahid </LastName>

		<Suffix>1</Suffix>

		<Affiliation>Lahore Garrison University, Lahore Pakistan</Affiliation>

		</Author>
		<Author> 

		<FirstName>Shoaib</FirstName>

		<MiddleName> </MiddleName>

		<LastName>Muhammad Waseem </LastName>

		<Suffix>2</Suffix>

		<Affiliation>District Head Quarter Hospital (DHQ), Faisalabad, Pakistan</Affiliation>

		</Author>
		<Author> 

		<FirstName>Mubeen </FirstName>

		<MiddleName> </MiddleName>

		<LastName>Hira </LastName>

		<Suffix>3</Suffix>

		<Affiliation>Lahore Garrison University, Lahore Pakistan</Affiliation>

		</Author>

	<Author>

	<CollectiveName></CollectiveName>>

	</Author>

	</AuthorList>


	<PublicationType>Research Paper</PublicationType>


	<History>  
	<PubDate PubStatus="received">
	<Year>2016</Year>
	<Month>5</Month>
	<Day>28</Day>
	</PubDate>
	<PubDate PubStatus="accepted">										
	<Year>2017</Year> 
	<Month>06</Month>									
	<Day>10</Day> 
	</PubDate>

	</History>
	<Abstract>Growth factors are special proteins which help to stimulate proliferation and differentiation in both normal and malignant cells. The first growth factor was epidermal growth factor. The receptor tyrosine kinases includes the receptor epidermal growth factor receptor EFGR. They have many other members like erbB2/HER-2, erbB3/HER-3, and erbB4/HER. These receptors are anchored in the cytoplasmic membrane and share a similar structure that is composed of an extracellular ligand-binding domain, a short hydrophobic transmembrane region, and an intracytoplasmic tyrosine kinase domain. Activation of these receptor leads to the phosphorylation of important tyrosine residues within the COOH-terminal portion of EGFR resulting in specific docking sites for cytoplasmic proteins. To overcome various problems associated with ERBB gene mutations, prior identification and analysis of these mutations is necessary. In this study, we have analyzed the ERBB receptor tyrosine kinase, its structural classification and various protein domains by using bioinformatics tools.</Abstract>

	<CopyrightInformation>Copyright@ International Science Community Association</CopyrightInformation>

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