Loading…
C-terminal region of USP7/HAUSP is critical for deubiquitination activity and contains a second mdm2/p53 binding site
► Deletion of the N-terminal TRAF-like domain of USP7 has no effect on USP7 mediated deubiquitination of Ub n-mdm2 and Ub n-p53. ► Amino acids 208–1102 were identified to be the minimal length of USP7 that retains essentially full proteolytic activity. ► In contrast, the catalytic domain of USP7 (am...
Saved in:
Published in: | Archives of biochemistry and biophysics 2010-11, Vol.503 (2), p.207-212 |
---|---|
Main Authors: | , , , , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
cited_by | cdi_FETCH-LOGICAL-c450t-fe05a2713de94225931aa254a97e24b26deaaa8836599ef61b79f29e939f17ec3 |
---|---|
cites | cdi_FETCH-LOGICAL-c450t-fe05a2713de94225931aa254a97e24b26deaaa8836599ef61b79f29e939f17ec3 |
container_end_page | 212 |
container_issue | 2 |
container_start_page | 207 |
container_title | Archives of biochemistry and biophysics |
container_volume | 503 |
creator | Ma, Jianhong Martin, John D. Xue, Yu Lor, Leng A. Kennedy-Wilson, Karen M. Sinnamon, Robert H. Ho, Thau F. Zhang, Guofeng Schwartz, Benjamin Tummino, Peter J. Lai, Zhihong |
description | ► Deletion of the N-terminal TRAF-like domain of USP7 has no effect on USP7 mediated deubiquitination of Ub
n-mdm2 and Ub
n-p53. ► Amino acids 208–1102 were identified to be the minimal length of USP7 that retains essentially full proteolytic activity. ► In contrast, the catalytic domain of USP7 (amino acids 208–560) has 50–700 fold less proteolytic activity towards different substrates. ► Inhibition of the catalytic domain of USP7 by Ubal is also different from the full length or TRAF-like domain deleted proteins. ► C-terminal domain of USP7 contains additional binding sites, a.a. 801–1050 and a.a. 880–1050 for mdm2 and p53, respectively. ► The additional USP7 binding site on mdm2 is mapped to the C-terminal RING finger domain (a.a. 425–491).
USP7, also known as the hepes simplex virus associated ubiquitin-specific protease (HAUSP), deubiquitinates both mdm2 and p53, and plays an important role in regulating the level and activity of p53. Here, we report that deletion of the TRAF-like domain at the N-terminus of USP7, previously reported to contain the mdm2/p53 binding site, has no effect on USP7 mediated deubiquitination of Ub
n-mdm2 and Ub
n-p53. Amino acids 208–1102 were identified to be the minimal length of USP7 that retains proteolytic activity, similar to full length enzyme, towards not only a truncated model substrate Ub-AFC, but also Ub
n-mdm2, Ub
n-p53. In contrast, the catalytic domain of USP7 (amino acids 208–560) has 50–700 fold less proteolytic activity towards different substrates. Moreover, inhibition of the catalytic domain of USP7 by Ubal is also different from the full length or TRAF-like domain deleted proteins. Using glutathione pull-down methods, we demonstrate that the C-terminal domain of USP7 contains additional binding sites, a.a. 801–1050 and a.a. 880–1050 for mdm2 and p53, respectively. The additional USP7 binding site on mdm2 is mapped to be the C-terminal RING finger domain (a.a. 425–491). We propose that the C-terminal domain of USP7 is responsible for maintaining the active conformation for catalysis and inhibitor binding, and contains the prime side of the proteolytic active site. |
doi_str_mv | 10.1016/j.abb.2010.08.020 |
format | article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_847437826</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0003986110003668</els_id><sourcerecordid>847437826</sourcerecordid><originalsourceid>FETCH-LOGICAL-c450t-fe05a2713de94225931aa254a97e24b26deaaa8836599ef61b79f29e939f17ec3</originalsourceid><addsrcrecordid>eNqFkU1rGzEQhkVpaZy0P6CXoltPa-tr9UFPwbRJIdBCkrPQSrNBxqt1JG0g_74yTnJsT8MMz7wD8yD0hZI1JVRudms3DGtGWk_0mjDyDq0oMbIjXIv3aEUI4Z3Rkp6h81J2hFAqJPuIzhjRVCqhV2jZdhXyFJPb4wwPcU54HvH97R-1ub5sBceCfY41-gaMc8YBliE-Lm2SXD3iztf4FOszdilgP6fqYirY4QKtCXgKE9sceo6HmEJMD7jECp_Qh9HtC3x-qRfo_uePu-11d_P76tf28qbzoie1G4H0jinKAxjBWG84dY71whkFTAxMBnDOac1lbwyMkg7KjMyA4WakCjy_QN9OuYc8Py5Qqp1i8bDfuwTzUqwWSnClmfwvqfreKNpuN5KeSJ_nUjKM9pDj5PKzpcQetdidbVrsUYsl2jYtbefrS_oyTBDeNl49NOD7CYD2jacI2RYfIXkIMYOvNszxH_F_AZMqnGo</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>755971254</pqid></control><display><type>article</type><title>C-terminal region of USP7/HAUSP is critical for deubiquitination activity and contains a second mdm2/p53 binding site</title><source>Elsevier</source><creator>Ma, Jianhong ; Martin, John D. ; Xue, Yu ; Lor, Leng A. ; Kennedy-Wilson, Karen M. ; Sinnamon, Robert H. ; Ho, Thau F. ; Zhang, Guofeng ; Schwartz, Benjamin ; Tummino, Peter J. ; Lai, Zhihong</creator><creatorcontrib>Ma, Jianhong ; Martin, John D. ; Xue, Yu ; Lor, Leng A. ; Kennedy-Wilson, Karen M. ; Sinnamon, Robert H. ; Ho, Thau F. ; Zhang, Guofeng ; Schwartz, Benjamin ; Tummino, Peter J. ; Lai, Zhihong</creatorcontrib><description>► Deletion of the N-terminal TRAF-like domain of USP7 has no effect on USP7 mediated deubiquitination of Ub
n-mdm2 and Ub
n-p53. ► Amino acids 208–1102 were identified to be the minimal length of USP7 that retains essentially full proteolytic activity. ► In contrast, the catalytic domain of USP7 (amino acids 208–560) has 50–700 fold less proteolytic activity towards different substrates. ► Inhibition of the catalytic domain of USP7 by Ubal is also different from the full length or TRAF-like domain deleted proteins. ► C-terminal domain of USP7 contains additional binding sites, a.a. 801–1050 and a.a. 880–1050 for mdm2 and p53, respectively. ► The additional USP7 binding site on mdm2 is mapped to the C-terminal RING finger domain (a.a. 425–491).
USP7, also known as the hepes simplex virus associated ubiquitin-specific protease (HAUSP), deubiquitinates both mdm2 and p53, and plays an important role in regulating the level and activity of p53. Here, we report that deletion of the TRAF-like domain at the N-terminus of USP7, previously reported to contain the mdm2/p53 binding site, has no effect on USP7 mediated deubiquitination of Ub
n-mdm2 and Ub
n-p53. Amino acids 208–1102 were identified to be the minimal length of USP7 that retains proteolytic activity, similar to full length enzyme, towards not only a truncated model substrate Ub-AFC, but also Ub
n-mdm2, Ub
n-p53. In contrast, the catalytic domain of USP7 (amino acids 208–560) has 50–700 fold less proteolytic activity towards different substrates. Moreover, inhibition of the catalytic domain of USP7 by Ubal is also different from the full length or TRAF-like domain deleted proteins. Using glutathione pull-down methods, we demonstrate that the C-terminal domain of USP7 contains additional binding sites, a.a. 801–1050 and a.a. 880–1050 for mdm2 and p53, respectively. The additional USP7 binding site on mdm2 is mapped to be the C-terminal RING finger domain (a.a. 425–491). We propose that the C-terminal domain of USP7 is responsible for maintaining the active conformation for catalysis and inhibitor binding, and contains the prime side of the proteolytic active site.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/j.abb.2010.08.020</identifier><identifier>PMID: 20816748</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Motifs - genetics ; Amino acids ; Binding Sites - genetics ; Catalytic Domain - genetics ; Deubiquitination ; Genes, p53 ; HAUSP ; Humans ; mdm2 ; p53 ; Protein Binding - genetics ; Protein Structure, Tertiary - genetics ; Proto-Oncogene Proteins c-mdm2 - chemistry ; Recombinant Fusion Proteins - chemistry ; Recombinant Fusion Proteins - metabolism ; Second binding site ; Tumor Suppressor Protein p53 - chemistry ; Tumor Suppressor Protein p53 - genetics ; Tumor Suppressor Protein p53 - metabolism ; Ubiquitin Thiolesterase - chemistry ; Ubiquitin-Specific Peptidase 7 ; Ubiquitination ; USP7</subject><ispartof>Archives of biochemistry and biophysics, 2010-11, Vol.503 (2), p.207-212</ispartof><rights>2010 Elsevier Inc.</rights><rights>Copyright © 2010 Elsevier Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c450t-fe05a2713de94225931aa254a97e24b26deaaa8836599ef61b79f29e939f17ec3</citedby><cites>FETCH-LOGICAL-c450t-fe05a2713de94225931aa254a97e24b26deaaa8836599ef61b79f29e939f17ec3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20816748$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ma, Jianhong</creatorcontrib><creatorcontrib>Martin, John D.</creatorcontrib><creatorcontrib>Xue, Yu</creatorcontrib><creatorcontrib>Lor, Leng A.</creatorcontrib><creatorcontrib>Kennedy-Wilson, Karen M.</creatorcontrib><creatorcontrib>Sinnamon, Robert H.</creatorcontrib><creatorcontrib>Ho, Thau F.</creatorcontrib><creatorcontrib>Zhang, Guofeng</creatorcontrib><creatorcontrib>Schwartz, Benjamin</creatorcontrib><creatorcontrib>Tummino, Peter J.</creatorcontrib><creatorcontrib>Lai, Zhihong</creatorcontrib><title>C-terminal region of USP7/HAUSP is critical for deubiquitination activity and contains a second mdm2/p53 binding site</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>► Deletion of the N-terminal TRAF-like domain of USP7 has no effect on USP7 mediated deubiquitination of Ub
n-mdm2 and Ub
n-p53. ► Amino acids 208–1102 were identified to be the minimal length of USP7 that retains essentially full proteolytic activity. ► In contrast, the catalytic domain of USP7 (amino acids 208–560) has 50–700 fold less proteolytic activity towards different substrates. ► Inhibition of the catalytic domain of USP7 by Ubal is also different from the full length or TRAF-like domain deleted proteins. ► C-terminal domain of USP7 contains additional binding sites, a.a. 801–1050 and a.a. 880–1050 for mdm2 and p53, respectively. ► The additional USP7 binding site on mdm2 is mapped to the C-terminal RING finger domain (a.a. 425–491).
USP7, also known as the hepes simplex virus associated ubiquitin-specific protease (HAUSP), deubiquitinates both mdm2 and p53, and plays an important role in regulating the level and activity of p53. Here, we report that deletion of the TRAF-like domain at the N-terminus of USP7, previously reported to contain the mdm2/p53 binding site, has no effect on USP7 mediated deubiquitination of Ub
n-mdm2 and Ub
n-p53. Amino acids 208–1102 were identified to be the minimal length of USP7 that retains proteolytic activity, similar to full length enzyme, towards not only a truncated model substrate Ub-AFC, but also Ub
n-mdm2, Ub
n-p53. In contrast, the catalytic domain of USP7 (amino acids 208–560) has 50–700 fold less proteolytic activity towards different substrates. Moreover, inhibition of the catalytic domain of USP7 by Ubal is also different from the full length or TRAF-like domain deleted proteins. Using glutathione pull-down methods, we demonstrate that the C-terminal domain of USP7 contains additional binding sites, a.a. 801–1050 and a.a. 880–1050 for mdm2 and p53, respectively. The additional USP7 binding site on mdm2 is mapped to be the C-terminal RING finger domain (a.a. 425–491). We propose that the C-terminal domain of USP7 is responsible for maintaining the active conformation for catalysis and inhibitor binding, and contains the prime side of the proteolytic active site.</description><subject>Amino Acid Motifs - genetics</subject><subject>Amino acids</subject><subject>Binding Sites - genetics</subject><subject>Catalytic Domain - genetics</subject><subject>Deubiquitination</subject><subject>Genes, p53</subject><subject>HAUSP</subject><subject>Humans</subject><subject>mdm2</subject><subject>p53</subject><subject>Protein Binding - genetics</subject><subject>Protein Structure, Tertiary - genetics</subject><subject>Proto-Oncogene Proteins c-mdm2 - chemistry</subject><subject>Recombinant Fusion Proteins - chemistry</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Second binding site</subject><subject>Tumor Suppressor Protein p53 - chemistry</subject><subject>Tumor Suppressor Protein p53 - genetics</subject><subject>Tumor Suppressor Protein p53 - metabolism</subject><subject>Ubiquitin Thiolesterase - chemistry</subject><subject>Ubiquitin-Specific Peptidase 7</subject><subject>Ubiquitination</subject><subject>USP7</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><recordid>eNqFkU1rGzEQhkVpaZy0P6CXoltPa-tr9UFPwbRJIdBCkrPQSrNBxqt1JG0g_74yTnJsT8MMz7wD8yD0hZI1JVRudms3DGtGWk_0mjDyDq0oMbIjXIv3aEUI4Z3Rkp6h81J2hFAqJPuIzhjRVCqhV2jZdhXyFJPb4wwPcU54HvH97R-1ub5sBceCfY41-gaMc8YBliE-Lm2SXD3iztf4FOszdilgP6fqYirY4QKtCXgKE9sceo6HmEJMD7jECp_Qh9HtC3x-qRfo_uePu-11d_P76tf28qbzoie1G4H0jinKAxjBWG84dY71whkFTAxMBnDOac1lbwyMkg7KjMyA4WakCjy_QN9OuYc8Py5Qqp1i8bDfuwTzUqwWSnClmfwvqfreKNpuN5KeSJ_nUjKM9pDj5PKzpcQetdidbVrsUYsl2jYtbefrS_oyTBDeNl49NOD7CYD2jacI2RYfIXkIMYOvNszxH_F_AZMqnGo</recordid><startdate>20101115</startdate><enddate>20101115</enddate><creator>Ma, Jianhong</creator><creator>Martin, John D.</creator><creator>Xue, Yu</creator><creator>Lor, Leng A.</creator><creator>Kennedy-Wilson, Karen M.</creator><creator>Sinnamon, Robert H.</creator><creator>Ho, Thau F.</creator><creator>Zhang, Guofeng</creator><creator>Schwartz, Benjamin</creator><creator>Tummino, Peter J.</creator><creator>Lai, Zhihong</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>7TO</scope><scope>H94</scope></search><sort><creationdate>20101115</creationdate><title>C-terminal region of USP7/HAUSP is critical for deubiquitination activity and contains a second mdm2/p53 binding site</title><author>Ma, Jianhong ; Martin, John D. ; Xue, Yu ; Lor, Leng A. ; Kennedy-Wilson, Karen M. ; Sinnamon, Robert H. ; Ho, Thau F. ; Zhang, Guofeng ; Schwartz, Benjamin ; Tummino, Peter J. ; Lai, Zhihong</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c450t-fe05a2713de94225931aa254a97e24b26deaaa8836599ef61b79f29e939f17ec3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Amino Acid Motifs - genetics</topic><topic>Amino acids</topic><topic>Binding Sites - genetics</topic><topic>Catalytic Domain - genetics</topic><topic>Deubiquitination</topic><topic>Genes, p53</topic><topic>HAUSP</topic><topic>Humans</topic><topic>mdm2</topic><topic>p53</topic><topic>Protein Binding - genetics</topic><topic>Protein Structure, Tertiary - genetics</topic><topic>Proto-Oncogene Proteins c-mdm2 - chemistry</topic><topic>Recombinant Fusion Proteins - chemistry</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Second binding site</topic><topic>Tumor Suppressor Protein p53 - chemistry</topic><topic>Tumor Suppressor Protein p53 - genetics</topic><topic>Tumor Suppressor Protein p53 - metabolism</topic><topic>Ubiquitin Thiolesterase - chemistry</topic><topic>Ubiquitin-Specific Peptidase 7</topic><topic>Ubiquitination</topic><topic>USP7</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ma, Jianhong</creatorcontrib><creatorcontrib>Martin, John D.</creatorcontrib><creatorcontrib>Xue, Yu</creatorcontrib><creatorcontrib>Lor, Leng A.</creatorcontrib><creatorcontrib>Kennedy-Wilson, Karen M.</creatorcontrib><creatorcontrib>Sinnamon, Robert H.</creatorcontrib><creatorcontrib>Ho, Thau F.</creatorcontrib><creatorcontrib>Zhang, Guofeng</creatorcontrib><creatorcontrib>Schwartz, Benjamin</creatorcontrib><creatorcontrib>Tummino, Peter J.</creatorcontrib><creatorcontrib>Lai, Zhihong</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><jtitle>Archives of biochemistry and biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ma, Jianhong</au><au>Martin, John D.</au><au>Xue, Yu</au><au>Lor, Leng A.</au><au>Kennedy-Wilson, Karen M.</au><au>Sinnamon, Robert H.</au><au>Ho, Thau F.</au><au>Zhang, Guofeng</au><au>Schwartz, Benjamin</au><au>Tummino, Peter J.</au><au>Lai, Zhihong</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>C-terminal region of USP7/HAUSP is critical for deubiquitination activity and contains a second mdm2/p53 binding site</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>2010-11-15</date><risdate>2010</risdate><volume>503</volume><issue>2</issue><spage>207</spage><epage>212</epage><pages>207-212</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><abstract>► Deletion of the N-terminal TRAF-like domain of USP7 has no effect on USP7 mediated deubiquitination of Ub
n-mdm2 and Ub
n-p53. ► Amino acids 208–1102 were identified to be the minimal length of USP7 that retains essentially full proteolytic activity. ► In contrast, the catalytic domain of USP7 (amino acids 208–560) has 50–700 fold less proteolytic activity towards different substrates. ► Inhibition of the catalytic domain of USP7 by Ubal is also different from the full length or TRAF-like domain deleted proteins. ► C-terminal domain of USP7 contains additional binding sites, a.a. 801–1050 and a.a. 880–1050 for mdm2 and p53, respectively. ► The additional USP7 binding site on mdm2 is mapped to the C-terminal RING finger domain (a.a. 425–491).
USP7, also known as the hepes simplex virus associated ubiquitin-specific protease (HAUSP), deubiquitinates both mdm2 and p53, and plays an important role in regulating the level and activity of p53. Here, we report that deletion of the TRAF-like domain at the N-terminus of USP7, previously reported to contain the mdm2/p53 binding site, has no effect on USP7 mediated deubiquitination of Ub
n-mdm2 and Ub
n-p53. Amino acids 208–1102 were identified to be the minimal length of USP7 that retains proteolytic activity, similar to full length enzyme, towards not only a truncated model substrate Ub-AFC, but also Ub
n-mdm2, Ub
n-p53. In contrast, the catalytic domain of USP7 (amino acids 208–560) has 50–700 fold less proteolytic activity towards different substrates. Moreover, inhibition of the catalytic domain of USP7 by Ubal is also different from the full length or TRAF-like domain deleted proteins. Using glutathione pull-down methods, we demonstrate that the C-terminal domain of USP7 contains additional binding sites, a.a. 801–1050 and a.a. 880–1050 for mdm2 and p53, respectively. The additional USP7 binding site on mdm2 is mapped to be the C-terminal RING finger domain (a.a. 425–491). We propose that the C-terminal domain of USP7 is responsible for maintaining the active conformation for catalysis and inhibitor binding, and contains the prime side of the proteolytic active site.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>20816748</pmid><doi>10.1016/j.abb.2010.08.020</doi><tpages>6</tpages></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0003-9861 |
ispartof | Archives of biochemistry and biophysics, 2010-11, Vol.503 (2), p.207-212 |
issn | 0003-9861 1096-0384 |
language | eng |
recordid | cdi_proquest_miscellaneous_847437826 |
source | Elsevier |
subjects | Amino Acid Motifs - genetics Amino acids Binding Sites - genetics Catalytic Domain - genetics Deubiquitination Genes, p53 HAUSP Humans mdm2 p53 Protein Binding - genetics Protein Structure, Tertiary - genetics Proto-Oncogene Proteins c-mdm2 - chemistry Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - metabolism Second binding site Tumor Suppressor Protein p53 - chemistry Tumor Suppressor Protein p53 - genetics Tumor Suppressor Protein p53 - metabolism Ubiquitin Thiolesterase - chemistry Ubiquitin-Specific Peptidase 7 Ubiquitination USP7 |
title | C-terminal region of USP7/HAUSP is critical for deubiquitination activity and contains a second mdm2/p53 binding site |
url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-03T21%3A32%3A00IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=C-terminal%20region%20of%20USP7/HAUSP%20is%20critical%20for%20deubiquitination%20activity%20and%20contains%20a%20second%20mdm2/p53%20binding%20site&rft.jtitle=Archives%20of%20biochemistry%20and%20biophysics&rft.au=Ma,%20Jianhong&rft.date=2010-11-15&rft.volume=503&rft.issue=2&rft.spage=207&rft.epage=212&rft.pages=207-212&rft.issn=0003-9861&rft.eissn=1096-0384&rft_id=info:doi/10.1016/j.abb.2010.08.020&rft_dat=%3Cproquest_cross%3E847437826%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c450t-fe05a2713de94225931aa254a97e24b26deaaa8836599ef61b79f29e939f17ec3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=755971254&rft_id=info:pmid/20816748&rfr_iscdi=true |