RP101 (brivudine) binds to heat shock protein HSP27 (HSPB1) and enhances survival in animals and pancreatic cancer patients
Background Several reports describe the importance of the chaperone HSP27 (HSPB1) in cancer progression, and the demand for drugs that modulate HSPB1-activity is increasing rapidly. We reported earlier that RP101 (Bromovinyldeoxyuridine, BVDU, Brivudine) improves the efficacy of chemotherapy in panc...
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| Veröffentlicht in: | Journal of cancer research and clinical oncology 2011-09, Vol.137 (9), p.1349-1361 |
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| container_title | Journal of cancer research and clinical oncology |
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| creator | Heinrich, Jörg-Christian Tuukkanen, Anne Schroeder, Michael Fahrig, Torsten Fahrig, Rudolf |
| description | Background
Several reports describe the importance of the chaperone HSP27 (HSPB1) in cancer progression, and the demand for drugs that modulate HSPB1-activity is increasing rapidly. We reported earlier that RP101 (Bromovinyldeoxyuridine, BVDU, Brivudine) improves the efficacy of chemotherapy in pancreatic cancer.
Methods
Chemistry
: Binding of RP101 and HSPB1 was discovered by affinity chromatography.
Molecular and cell biology
: HSPB1 in vitro transcription/translation (TNT), Pull down using RP101-coupled magnetic beads, Immuno Co-precipitations, Structural modeling of HSP27 (HSPB1), Introduction of point mutations into linear expression templates by PCR, Heat shock, Tumor Invasion.
Animal experiments:
Treatment of AH13r Sarcomas in SD-rats.
Clinical Studies with late-stage pancreatic cancer patients:
Pilot study, Dose finding study, Phase II study (NCT00550004).
Results
Here, we report that RP101 binds in vitro to the heat shock protein HSPB1 and inhibits interaction with its binding partners. As a result, more activated CASP9 was detected in RP101-treated cancer cells. We modeled HSPB1-structure and identified the RP101 binding site. When we tested RP101 as an anti-cancer drug in a rat model, we found that it improved chemotherapy. In clinical studies with late-stage pancreatic cancer patients, the dose of 500 mg/day was safe and efficient, but 760 mg/day turned out to be too high for lightweight patients.
Conclusions
The development of RP101 as a cancer drug represents a truly novel approach for prevention of chemoresistance and enhancement of chemosensitivity. |
| doi_str_mv | 10.1007/s00432-011-1005-1 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_journals_883053393</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2423179841</sourcerecordid><originalsourceid>FETCH-LOGICAL-c514t-2dd2c37bb9912f4b65e037349384d2175c235610c151849160bcdd9789d360433</originalsourceid><addsrcrecordid>eNp1kE1rGzEQhkVoiJ00P6CXIgqB-LDtjLTaj2Ni8gWGmrY5L7uSXMu1tY60ayj585mN3eTU0_DOPPP1MvYJ4SsC5N8iQCpFAogJaZXgERvjkEEp1Qc2BswxUQKzETuNcQWkVS5O2EhgIWUuYMyef8wRkF82we1647yd8MZ5E3nX8qWtOx6Xrf7Dt6HtrPP8_udc5PySwjVOeO0Nt35Ze20jj33YuV295oTV3m3qdXwFtlQONMlprgcyUKZz1nfxIzteEGXPD_GMPd7e_JreJ7Pvdw_Tq1miFaZdIowRWuZNU5YoFmmTKQsyl2kpi9QIekkLqTIEjQqLtMQMGm1MmRelkRkZJM_Yl_1c-uKpt7GrVm0fPK2sikKCkrIcINxDOrQxBruotoGeCH8rhGpwu9q7XZHbg1YVUs_nw-C-2Vjz1vHPXgIuDkAddb1eBDLAxXcupesABk7suUgl_9uG9wv_v_0FM_aTfg</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>883053393</pqid></control><display><type>article</type><title>RP101 (brivudine) binds to heat shock protein HSP27 (HSPB1) and enhances survival in animals and pancreatic cancer patients</title><source>MEDLINE</source><source>SpringerLink (Online service)</source><creator>Heinrich, Jörg-Christian ; Tuukkanen, Anne ; Schroeder, Michael ; Fahrig, Torsten ; Fahrig, Rudolf</creator><creatorcontrib>Heinrich, Jörg-Christian ; Tuukkanen, Anne ; Schroeder, Michael ; Fahrig, Torsten ; Fahrig, Rudolf</creatorcontrib><description>Background
Several reports describe the importance of the chaperone HSP27 (HSPB1) in cancer progression, and the demand for drugs that modulate HSPB1-activity is increasing rapidly. We reported earlier that RP101 (Bromovinyldeoxyuridine, BVDU, Brivudine) improves the efficacy of chemotherapy in pancreatic cancer.
Methods
Chemistry
: Binding of RP101 and HSPB1 was discovered by affinity chromatography.
Molecular and cell biology
: HSPB1 in vitro transcription/translation (TNT), Pull down using RP101-coupled magnetic beads, Immuno Co-precipitations, Structural modeling of HSP27 (HSPB1), Introduction of point mutations into linear expression templates by PCR, Heat shock, Tumor Invasion.
Animal experiments:
Treatment of AH13r Sarcomas in SD-rats.
Clinical Studies with late-stage pancreatic cancer patients:
Pilot study, Dose finding study, Phase II study (NCT00550004).
Results
Here, we report that RP101 binds in vitro to the heat shock protein HSPB1 and inhibits interaction with its binding partners. As a result, more activated CASP9 was detected in RP101-treated cancer cells. We modeled HSPB1-structure and identified the RP101 binding site. When we tested RP101 as an anti-cancer drug in a rat model, we found that it improved chemotherapy. In clinical studies with late-stage pancreatic cancer patients, the dose of 500 mg/day was safe and efficient, but 760 mg/day turned out to be too high for lightweight patients.
Conclusions
The development of RP101 as a cancer drug represents a truly novel approach for prevention of chemoresistance and enhancement of chemosensitivity.</description><identifier>ISSN: 0171-5216</identifier><identifier>EISSN: 1432-1335</identifier><identifier>DOI: 10.1007/s00432-011-1005-1</identifier><identifier>PMID: 21833720</identifier><identifier>CODEN: JCROD7</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer-Verlag</publisher><subject>Adenocarcinoma - drug therapy ; Adenocarcinoma - metabolism ; Adenocarcinoma - mortality ; Animals ; Antineoplastic agents ; Antineoplastic Agents - administration & dosage ; Antineoplastic Agents - metabolism ; Antineoplastic Agents - pharmacology ; Biological and medical sciences ; Bromodeoxyuridine - administration & dosage ; Bromodeoxyuridine - analogs & derivatives ; Bromodeoxyuridine - metabolism ; Bromodeoxyuridine - pharmacology ; Cancer Research ; Chemotherapy ; Disease Models, Animal ; Dose-Response Relationship, Drug ; Double-Blind Method ; Drug Evaluation, Preclinical ; Female ; Gastroenterology. Liver. Pancreas. Abdomen ; Heat shock proteins ; Hematology ; HSP27 Heat-Shock Proteins - metabolism ; Humans ; Internal Medicine ; Liver. Biliary tract. Portal circulation. Exocrine pancreas ; Male ; Medical sciences ; Medicine ; Medicine & Public Health ; Middle Aged ; Models, Molecular ; Oncology ; Original Paper ; Pancreatic cancer ; Pancreatic Neoplasms - drug therapy ; Pancreatic Neoplasms - metabolism ; Pancreatic Neoplasms - mortality ; Pharmacology. Drug treatments ; Pilot Projects ; Placebos ; Rats ; Rats, Sprague-Dawley ; Sarcoma - metabolism ; Sarcoma - mortality ; Survival Analysis ; Tumors</subject><ispartof>Journal of cancer research and clinical oncology, 2011-09, Vol.137 (9), p.1349-1361</ispartof><rights>Springer-Verlag 2011</rights><rights>2015 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c514t-2dd2c37bb9912f4b65e037349384d2175c235610c151849160bcdd9789d360433</citedby><cites>FETCH-LOGICAL-c514t-2dd2c37bb9912f4b65e037349384d2175c235610c151849160bcdd9789d360433</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00432-011-1005-1$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00432-011-1005-1$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>315,782,786,27931,27932,41495,42564,51326</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=24433000$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21833720$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Heinrich, Jörg-Christian</creatorcontrib><creatorcontrib>Tuukkanen, Anne</creatorcontrib><creatorcontrib>Schroeder, Michael</creatorcontrib><creatorcontrib>Fahrig, Torsten</creatorcontrib><creatorcontrib>Fahrig, Rudolf</creatorcontrib><title>RP101 (brivudine) binds to heat shock protein HSP27 (HSPB1) and enhances survival in animals and pancreatic cancer patients</title><title>Journal of cancer research and clinical oncology</title><addtitle>J Cancer Res Clin Oncol</addtitle><addtitle>J Cancer Res Clin Oncol</addtitle><description>Background
Several reports describe the importance of the chaperone HSP27 (HSPB1) in cancer progression, and the demand for drugs that modulate HSPB1-activity is increasing rapidly. We reported earlier that RP101 (Bromovinyldeoxyuridine, BVDU, Brivudine) improves the efficacy of chemotherapy in pancreatic cancer.
Methods
Chemistry
: Binding of RP101 and HSPB1 was discovered by affinity chromatography.
Molecular and cell biology
: HSPB1 in vitro transcription/translation (TNT), Pull down using RP101-coupled magnetic beads, Immuno Co-precipitations, Structural modeling of HSP27 (HSPB1), Introduction of point mutations into linear expression templates by PCR, Heat shock, Tumor Invasion.
Animal experiments:
Treatment of AH13r Sarcomas in SD-rats.
Clinical Studies with late-stage pancreatic cancer patients:
Pilot study, Dose finding study, Phase II study (NCT00550004).
Results
Here, we report that RP101 binds in vitro to the heat shock protein HSPB1 and inhibits interaction with its binding partners. As a result, more activated CASP9 was detected in RP101-treated cancer cells. We modeled HSPB1-structure and identified the RP101 binding site. When we tested RP101 as an anti-cancer drug in a rat model, we found that it improved chemotherapy. In clinical studies with late-stage pancreatic cancer patients, the dose of 500 mg/day was safe and efficient, but 760 mg/day turned out to be too high for lightweight patients.
Conclusions
The development of RP101 as a cancer drug represents a truly novel approach for prevention of chemoresistance and enhancement of chemosensitivity.</description><subject>Adenocarcinoma - drug therapy</subject><subject>Adenocarcinoma - metabolism</subject><subject>Adenocarcinoma - mortality</subject><subject>Animals</subject><subject>Antineoplastic agents</subject><subject>Antineoplastic Agents - administration & dosage</subject><subject>Antineoplastic Agents - metabolism</subject><subject>Antineoplastic Agents - pharmacology</subject><subject>Biological and medical sciences</subject><subject>Bromodeoxyuridine - administration & dosage</subject><subject>Bromodeoxyuridine - analogs & derivatives</subject><subject>Bromodeoxyuridine - metabolism</subject><subject>Bromodeoxyuridine - pharmacology</subject><subject>Cancer Research</subject><subject>Chemotherapy</subject><subject>Disease Models, Animal</subject><subject>Dose-Response Relationship, Drug</subject><subject>Double-Blind Method</subject><subject>Drug Evaluation, Preclinical</subject><subject>Female</subject><subject>Gastroenterology. Liver. Pancreas. Abdomen</subject><subject>Heat shock proteins</subject><subject>Hematology</subject><subject>HSP27 Heat-Shock Proteins - metabolism</subject><subject>Humans</subject><subject>Internal Medicine</subject><subject>Liver. Biliary tract. Portal circulation. Exocrine pancreas</subject><subject>Male</subject><subject>Medical sciences</subject><subject>Medicine</subject><subject>Medicine & Public Health</subject><subject>Middle Aged</subject><subject>Models, Molecular</subject><subject>Oncology</subject><subject>Original Paper</subject><subject>Pancreatic cancer</subject><subject>Pancreatic Neoplasms - drug therapy</subject><subject>Pancreatic Neoplasms - metabolism</subject><subject>Pancreatic Neoplasms - mortality</subject><subject>Pharmacology. Drug treatments</subject><subject>Pilot Projects</subject><subject>Placebos</subject><subject>Rats</subject><subject>Rats, Sprague-Dawley</subject><subject>Sarcoma - metabolism</subject><subject>Sarcoma - mortality</subject><subject>Survival Analysis</subject><subject>Tumors</subject><issn>0171-5216</issn><issn>1432-1335</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNp1kE1rGzEQhkVoiJ00P6CXIgqB-LDtjLTaj2Ni8gWGmrY5L7uSXMu1tY60ayj585mN3eTU0_DOPPP1MvYJ4SsC5N8iQCpFAogJaZXgERvjkEEp1Qc2BswxUQKzETuNcQWkVS5O2EhgIWUuYMyef8wRkF82we1647yd8MZ5E3nX8qWtOx6Xrf7Dt6HtrPP8_udc5PySwjVOeO0Nt35Ze20jj33YuV295oTV3m3qdXwFtlQONMlprgcyUKZz1nfxIzteEGXPD_GMPd7e_JreJ7Pvdw_Tq1miFaZdIowRWuZNU5YoFmmTKQsyl2kpi9QIekkLqTIEjQqLtMQMGm1MmRelkRkZJM_Yl_1c-uKpt7GrVm0fPK2sikKCkrIcINxDOrQxBruotoGeCH8rhGpwu9q7XZHbg1YVUs_nw-C-2Vjz1vHPXgIuDkAddb1eBDLAxXcupesABk7suUgl_9uG9wv_v_0FM_aTfg</recordid><startdate>20110901</startdate><enddate>20110901</enddate><creator>Heinrich, Jörg-Christian</creator><creator>Tuukkanen, Anne</creator><creator>Schroeder, Michael</creator><creator>Fahrig, Torsten</creator><creator>Fahrig, Rudolf</creator><general>Springer-Verlag</general><general>Springer</general><general>Springer Nature B.V</general><scope>IQODW</scope><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>3V.</scope><scope>7TO</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>MBDVC</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope></search><sort><creationdate>20110901</creationdate><title>RP101 (brivudine) binds to heat shock protein HSP27 (HSPB1) and enhances survival in animals and pancreatic cancer patients</title><author>Heinrich, Jörg-Christian ; Tuukkanen, Anne ; Schroeder, Michael ; Fahrig, Torsten ; Fahrig, Rudolf</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c514t-2dd2c37bb9912f4b65e037349384d2175c235610c151849160bcdd9789d360433</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Adenocarcinoma - drug therapy</topic><topic>Adenocarcinoma - metabolism</topic><topic>Adenocarcinoma - mortality</topic><topic>Animals</topic><topic>Antineoplastic agents</topic><topic>Antineoplastic Agents - administration & dosage</topic><topic>Antineoplastic Agents - metabolism</topic><topic>Antineoplastic Agents - pharmacology</topic><topic>Biological and medical sciences</topic><topic>Bromodeoxyuridine - administration & dosage</topic><topic>Bromodeoxyuridine - analogs & derivatives</topic><topic>Bromodeoxyuridine - metabolism</topic><topic>Bromodeoxyuridine - pharmacology</topic><topic>Cancer Research</topic><topic>Chemotherapy</topic><topic>Disease Models, Animal</topic><topic>Dose-Response Relationship, Drug</topic><topic>Double-Blind Method</topic><topic>Drug Evaluation, Preclinical</topic><topic>Female</topic><topic>Gastroenterology. Liver. Pancreas. Abdomen</topic><topic>Heat shock proteins</topic><topic>Hematology</topic><topic>HSP27 Heat-Shock Proteins - metabolism</topic><topic>Humans</topic><topic>Internal Medicine</topic><topic>Liver. Biliary tract. Portal circulation. Exocrine pancreas</topic><topic>Male</topic><topic>Medical sciences</topic><topic>Medicine</topic><topic>Medicine & Public Health</topic><topic>Middle Aged</topic><topic>Models, Molecular</topic><topic>Oncology</topic><topic>Original Paper</topic><topic>Pancreatic cancer</topic><topic>Pancreatic Neoplasms - drug therapy</topic><topic>Pancreatic Neoplasms - metabolism</topic><topic>Pancreatic Neoplasms - mortality</topic><topic>Pharmacology. Drug treatments</topic><topic>Pilot Projects</topic><topic>Placebos</topic><topic>Rats</topic><topic>Rats, Sprague-Dawley</topic><topic>Sarcoma - metabolism</topic><topic>Sarcoma - mortality</topic><topic>Survival Analysis</topic><topic>Tumors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Heinrich, Jörg-Christian</creatorcontrib><creatorcontrib>Tuukkanen, Anne</creatorcontrib><creatorcontrib>Schroeder, Michael</creatorcontrib><creatorcontrib>Fahrig, Torsten</creatorcontrib><creatorcontrib>Fahrig, Rudolf</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Health & Medical Complete (ProQuest Database)</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>ProQuest Public Health Database</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>ProQuest Research Library</collection><collection>Research Library (Corporate)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><jtitle>Journal of cancer research and clinical oncology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Heinrich, Jörg-Christian</au><au>Tuukkanen, Anne</au><au>Schroeder, Michael</au><au>Fahrig, Torsten</au><au>Fahrig, Rudolf</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>RP101 (brivudine) binds to heat shock protein HSP27 (HSPB1) and enhances survival in animals and pancreatic cancer patients</atitle><jtitle>Journal of cancer research and clinical oncology</jtitle><stitle>J Cancer Res Clin Oncol</stitle><addtitle>J Cancer Res Clin Oncol</addtitle><date>2011-09-01</date><risdate>2011</risdate><volume>137</volume><issue>9</issue><spage>1349</spage><epage>1361</epage><pages>1349-1361</pages><issn>0171-5216</issn><eissn>1432-1335</eissn><coden>JCROD7</coden><abstract>Background
Several reports describe the importance of the chaperone HSP27 (HSPB1) in cancer progression, and the demand for drugs that modulate HSPB1-activity is increasing rapidly. We reported earlier that RP101 (Bromovinyldeoxyuridine, BVDU, Brivudine) improves the efficacy of chemotherapy in pancreatic cancer.
Methods
Chemistry
: Binding of RP101 and HSPB1 was discovered by affinity chromatography.
Molecular and cell biology
: HSPB1 in vitro transcription/translation (TNT), Pull down using RP101-coupled magnetic beads, Immuno Co-precipitations, Structural modeling of HSP27 (HSPB1), Introduction of point mutations into linear expression templates by PCR, Heat shock, Tumor Invasion.
Animal experiments:
Treatment of AH13r Sarcomas in SD-rats.
Clinical Studies with late-stage pancreatic cancer patients:
Pilot study, Dose finding study, Phase II study (NCT00550004).
Results
Here, we report that RP101 binds in vitro to the heat shock protein HSPB1 and inhibits interaction with its binding partners. As a result, more activated CASP9 was detected in RP101-treated cancer cells. We modeled HSPB1-structure and identified the RP101 binding site. When we tested RP101 as an anti-cancer drug in a rat model, we found that it improved chemotherapy. In clinical studies with late-stage pancreatic cancer patients, the dose of 500 mg/day was safe and efficient, but 760 mg/day turned out to be too high for lightweight patients.
Conclusions
The development of RP101 as a cancer drug represents a truly novel approach for prevention of chemoresistance and enhancement of chemosensitivity.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer-Verlag</pub><pmid>21833720</pmid><doi>10.1007/s00432-011-1005-1</doi><tpages>13</tpages></addata></record> |
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| identifier | ISSN: 0171-5216 |
| ispartof | Journal of cancer research and clinical oncology, 2011-09, Vol.137 (9), p.1349-1361 |
| issn | 0171-5216 1432-1335 |
| language | eng |
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| subjects | Adenocarcinoma - drug therapy Adenocarcinoma - metabolism Adenocarcinoma - mortality Animals Antineoplastic agents Antineoplastic Agents - administration & dosage Antineoplastic Agents - metabolism Antineoplastic Agents - pharmacology Biological and medical sciences Bromodeoxyuridine - administration & dosage Bromodeoxyuridine - analogs & derivatives Bromodeoxyuridine - metabolism Bromodeoxyuridine - pharmacology Cancer Research Chemotherapy Disease Models, Animal Dose-Response Relationship, Drug Double-Blind Method Drug Evaluation, Preclinical Female Gastroenterology. Liver. Pancreas. Abdomen Heat shock proteins Hematology HSP27 Heat-Shock Proteins - metabolism Humans Internal Medicine Liver. Biliary tract. Portal circulation. Exocrine pancreas Male Medical sciences Medicine Medicine & Public Health Middle Aged Models, Molecular Oncology Original Paper Pancreatic cancer Pancreatic Neoplasms - drug therapy Pancreatic Neoplasms - metabolism Pancreatic Neoplasms - mortality Pharmacology. Drug treatments Pilot Projects Placebos Rats Rats, Sprague-Dawley Sarcoma - metabolism Sarcoma - mortality Survival Analysis Tumors |
| title | RP101 (brivudine) binds to heat shock protein HSP27 (HSPB1) and enhances survival in animals and pancreatic cancer patients |
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