<?xml version="1.0" encoding="UTF-8"?><?xml-stylesheet type="text/xsl" href="static/style.xsl"?><OAI-PMH xmlns="http://www.openarchives.org/OAI/2.0/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/ http://www.openarchives.org/OAI/2.0/OAI-PMH.xsd"><responseDate>2026-09-20T17:47:08Z</responseDate><request verb="GetRecord" identifier="oai:dspace.mit.edu:1721.1/45309" metadataPrefix="dim">https://dspace.mit.edu/server/oai/request</request><GetRecord><record><header><identifier>oai:dspace.mit.edu:1721.1/45309</identifier><datestamp>2022-01-13T07:54:15Z</datestamp><setSpec>com_1721.1_7582</setSpec><setSpec>com_1721.1_7581</setSpec><setSpec>col_1721.1_131023</setSpec></header><metadata><dim:dim xmlns:dim="http://www.dspace.org/xmlns/dspace/dim" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns:doc="http://www.lyncode.com/xoai" xsi:schemaLocation="http://www.dspace.org/xmlns/dspace/dim http://www.dspace.org/schema/dim.xsd">
   <dim:field mdschema="dc" element="contributor" qualifier="advisor" lang="en_US">Peter K. Sorger.</dim:field>
   <dim:field mdschema="dc" element="contributor" qualifier="author" lang="en_US">Lu, Kuojung Gordon</dim:field>
   <dim:field mdschema="dc" element="contributor" qualifier="other" lang="en_US">Massachusetts Institute of Technology. Dept. of Biology.</dim:field>
   <dim:field mdschema="dc" element="contributor" qualifier="department">Massachusetts Institute of Technology. Department of Biology</dim:field>
   <dim:field mdschema="dc" element="date" qualifier="accessioned">2009-04-29T17:23:44Z</dim:field>
   <dim:field mdschema="dc" element="date" qualifier="available">2009-04-29T17:23:44Z</dim:field>
   <dim:field mdschema="dc" element="date" qualifier="copyright" lang="en_US">2008</dim:field>
   <dim:field mdschema="dc" element="date" qualifier="issued" lang="en_US">2008</dim:field>
   <dim:field mdschema="dc" element="identifier" qualifier="uri">http://hdl.handle.net/1721.1/45309</dim:field>
   <dim:field mdschema="dc" element="identifier" qualifier="oclc" lang="en_US">313410867</dim:field>
   <dim:field mdschema="dc" element="description" lang="en_US">Thesis (S.M.)--Massachusetts Institute of Technology, Dept. of Biology, 2008.</dim:field>
   <dim:field mdschema="dc" element="description" lang="en_US">Includes bibliographical references (leaves 39-43).</dim:field>
   <dim:field mdschema="dc" element="description" qualifier="abstract" lang="en_US">Protein phosphatases regulate the phosphorylation state of intracellular signaling molecules in conjunction with protein kinases. In order to better understand the role of phosphatases in the ErbB signaling network, experimental studies were carried out to validate assays and phosphatase inhibitors for gathering dynamic, system-wide data of phosphatase activity. We verified the use of In-Cell Westerns and phospho-ErbB ELISAs for these studies, as well as the use of different cell lines and both general and specific phosphatase inhibitors in system-wide experiments. The phosphatase inhibitors we used perturbed cellular systems in complex ways that can help elucidate the regulation and activity of specific phosphatases in the ErbB signaling pathway in the future.</dim:field>
   <dim:field mdschema="dc" element="description" qualifier="statementofresponsibility" lang="en_US">by Kuojung Gordon Lu.</dim:field>
   <dim:field mdschema="dc" element="description" qualifier="degree" lang="en_US">S.M.</dim:field>
   <dim:field mdschema="dc" element="format" qualifier="extent" lang="en_US">61 leaves</dim:field>
   <dim:field mdschema="dc" element="language" qualifier="iso" lang="en_US">eng</dim:field>
   <dim:field mdschema="dc" element="publisher" lang="en_US">Massachusetts Institute of Technology</dim:field>
   <dim:field mdschema="dc" element="rights" lang="en_US">M.I.T. theses are protected by 
copyright. They may be viewed from this source for any purpose, but 
reproduction or distribution in any format is prohibited without written 
permission. See provided URL for inquiries about permission.</dim:field>
   <dim:field mdschema="dc" element="rights" qualifier="uri" lang="en_US">http://dspace.mit.edu/handle/1721.1/7582</dim:field>
   <dim:field mdschema="dc" element="subject" lang="en_US">Biology.</dim:field>
   <dim:field mdschema="dc" element="title" lang="en_US">Investigations into the role of protein phosphatases in the EGFR signaling network</dim:field>
   <dim:field mdschema="dc" element="type" lang="en_US">Thesis</dim:field>
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   	&lt;Title>Investigations into the role of protein phosphatases in the EGFR signaling network&lt;/Title>
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   	&lt;PublicationDate>2008&lt;/PublicationDate>
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        	&lt;DisplayName>Lu, Kuojung Gordon&lt;/DisplayName>
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            &lt;DisplayName>Massachusetts Institute of Technology&lt;/DisplayName>
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    &lt;Keyword>Biology.&lt;/Keyword>
   	&lt;Abstract>Protein phosphatases regulate the phosphorylation state of intracellular signaling molecules in conjunction with protein kinases. In order to better understand the role of phosphatases in the ErbB signaling network, experimental studies were carried out to validate assays and phosphatase inhibitors for gathering dynamic, system-wide data of phosphatase activity. We verified the use of In-Cell Westerns and phospho-ErbB ELISAs for these studies, as well as the use of different cell lines and both general and specific phosphatase inhibitors in system-wide experiments. The phosphatase inhibitors we used perturbed cellular systems in complex ways that can help elucidate the regulation and activity of specific phosphatases in the ErbB signaling pathway in the future.&lt;/Abstract>
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