Design of DNA-Binding Peptides Based on the Leucine Zipper Motif
A class of transcriptional regulator proteins bind to DNA at dyad-symmetric sites through a motif consisting of (i) a "leucine zipper" sequence that associates into noncovalent, parallel, α-helical dimers and (ii) a covalently connected basic region necessary for binding DNA. The basic reg...
Gespeichert in:
| Veröffentlicht in: | Science (American Association for the Advancement of Science) 1990-08, Vol.249 (4970), p.774-778 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 778 |
|---|---|
| container_issue | 4970 |
| container_start_page | 774 |
| container_title | Science (American Association for the Advancement of Science) |
| container_volume | 249 |
| creator | O'Neil, Karyn T. Hoess, Ronald H. DeGrado, William F. |
| description | A class of transcriptional regulator proteins bind to DNA at dyad-symmetric sites through a motif consisting of (i) a "leucine zipper" sequence that associates into noncovalent, parallel, α-helical dimers and (ii) a covalently connected basic region necessary for binding DNA. The basic regions are predicted to be disordered in the absence of DNA and to form α helices when bound to DNA. These helices bind in the major groove forming multiple hydrogen-bonded and van der Waals contacts with the nucleotide bases. To test this model, two peptides were designed that were identical to natural leucine zipper proteins only at positions hypothesized to be critical for dimerization and DNA recognition. The peptides form dimers that bind specifically to DNA with their basic regions in α-helical conformations. |
| doi_str_mv | 10.1126/science.2389143 |
| format | Article |
| fullrecord | <record><control><sourceid>gale_proqu</sourceid><recordid>TN_cdi_proquest_miscellaneous_79957717</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A8872166</galeid><jstor_id>2878082</jstor_id><sourcerecordid>A8872166</sourcerecordid><originalsourceid>FETCH-LOGICAL-c499t-6398975820d122115f7ec3deb2fef08305137ddb9f119fce8cdbb9289c192d553</originalsourceid><addsrcrecordid>eNqFkU2P0zAQhi0EWroLZy4gRUjAAWXXY9exfaPb5UsqLAe4cLESe1xcpXaIE2n596RqRCUOcPLhfebReF5CngC9BGDVVbYBo8VLxpWGJb9HFkC1KDWj_D5ZUMqrUlEpHpLznHeUTpnmZ-RsxhfkzQ3msI1F8sXN51V5HaILcVt8wW4IDnNxXWd0RYrF8AOLDY42RCy-h67DvviUhuAfkQe-bjM-nt8L8u3d26_rD-Xm9v3H9WpT2qXWQ1lxrbQUilEHjAEIL9Fyhw3z6KniVACXzjXaA2hvUVnXNJopbUEzJwS_IC-P3q5PP0fMg9mHbLFt64hpzEZqLaQEOYGv_g0uOUglK_5fJQitQdOD8vlf4C6NfZy-axhwMQn1YcHXR2hbt2hCtCkOeDfY1La4RTMdY31rVkpJBlU10VdH2vYp5x696fqwr_tfBqg5NGvmZs1c1TTxbF5ibPbo_vCn_MWc19nWre_raEM-aafzMFrBxD09crs8pP6kUVJRxfhv3WmyKA</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>213543195</pqid></control><display><type>article</type><title>Design of DNA-Binding Peptides Based on the Leucine Zipper Motif</title><source>American Association for the Advancement of Science</source><source>Jstor Complete Legacy</source><source>MEDLINE</source><creator>O'Neil, Karyn T. ; Hoess, Ronald H. ; DeGrado, William F.</creator><creatorcontrib>O'Neil, Karyn T. ; Hoess, Ronald H. ; DeGrado, William F.</creatorcontrib><description>A class of transcriptional regulator proteins bind to DNA at dyad-symmetric sites through a motif consisting of (i) a "leucine zipper" sequence that associates into noncovalent, parallel, α-helical dimers and (ii) a covalently connected basic region necessary for binding DNA. The basic regions are predicted to be disordered in the absence of DNA and to form α helices when bound to DNA. These helices bind in the major groove forming multiple hydrogen-bonded and van der Waals contacts with the nucleotide bases. To test this model, two peptides were designed that were identical to natural leucine zipper proteins only at positions hypothesized to be critical for dimerization and DNA recognition. The peptides form dimers that bind specifically to DNA with their basic regions in α-helical conformations.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.2389143</identifier><identifier>PMID: 2389143</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>Washington, DC: American Society for the Advancement of Science</publisher><subject>Amino Acid Sequence ; Amino acids ; Base Sequence ; Binding Sites ; Biological and medical sciences ; Chemical Phenomena ; Chemistry, Physical ; Circular Dichroism ; Computer Simulation ; Deoxyribonucleic acid ; Dimers ; DNA ; DNA - metabolism ; DNA binding proteins ; DNA-Binding Proteins - metabolism ; Enzymes ; Fundamental and applied biological sciences. Psychology ; Gels ; Genetic regulation ; Hydrogen Bonding ; Hydrogen bonds ; Leucine ; Macromolecular Substances ; Modeling ; Models, Molecular ; Molecular and cellular biology ; Molecular genetics ; Molecular Sequence Data ; Nucleotide sequence ; Nucleotide sequences ; Oligonucleotides ; Physiological aspects ; Protein Conformation ; Proteins ; Scissors ; Transcription. Transcription factor. Splicing. Rna processing</subject><ispartof>Science (American Association for the Advancement of Science), 1990-08, Vol.249 (4970), p.774-778</ispartof><rights>Copyright 1990 American Association for the Advancement of Science</rights><rights>1991 INIST-CNRS</rights><rights>Copyright American Association for the Advancement of Science Aug 17, 1990</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c499t-6398975820d122115f7ec3deb2fef08305137ddb9f119fce8cdbb9289c192d553</citedby><cites>FETCH-LOGICAL-c499t-6398975820d122115f7ec3deb2fef08305137ddb9f119fce8cdbb9289c192d553</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2878082$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2878082$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,776,780,799,2871,2872,27901,27902,57992,58225</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19572061$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2389143$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>O'Neil, Karyn T.</creatorcontrib><creatorcontrib>Hoess, Ronald H.</creatorcontrib><creatorcontrib>DeGrado, William F.</creatorcontrib><title>Design of DNA-Binding Peptides Based on the Leucine Zipper Motif</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>A class of transcriptional regulator proteins bind to DNA at dyad-symmetric sites through a motif consisting of (i) a "leucine zipper" sequence that associates into noncovalent, parallel, α-helical dimers and (ii) a covalently connected basic region necessary for binding DNA. The basic regions are predicted to be disordered in the absence of DNA and to form α helices when bound to DNA. These helices bind in the major groove forming multiple hydrogen-bonded and van der Waals contacts with the nucleotide bases. To test this model, two peptides were designed that were identical to natural leucine zipper proteins only at positions hypothesized to be critical for dimerization and DNA recognition. The peptides form dimers that bind specifically to DNA with their basic regions in α-helical conformations.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Base Sequence</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>Chemical Phenomena</subject><subject>Chemistry, Physical</subject><subject>Circular Dichroism</subject><subject>Computer Simulation</subject><subject>Deoxyribonucleic acid</subject><subject>Dimers</subject><subject>DNA</subject><subject>DNA - metabolism</subject><subject>DNA binding proteins</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Enzymes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gels</subject><subject>Genetic regulation</subject><subject>Hydrogen Bonding</subject><subject>Hydrogen bonds</subject><subject>Leucine</subject><subject>Macromolecular Substances</subject><subject>Modeling</subject><subject>Models, Molecular</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>Molecular Sequence Data</subject><subject>Nucleotide sequence</subject><subject>Nucleotide sequences</subject><subject>Oligonucleotides</subject><subject>Physiological aspects</subject><subject>Protein Conformation</subject><subject>Proteins</subject><subject>Scissors</subject><subject>Transcription. Transcription factor. Splicing. Rna processing</subject><issn>0036-8075</issn><issn>1095-9203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BEC</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqFkU2P0zAQhi0EWroLZy4gRUjAAWXXY9exfaPb5UsqLAe4cLESe1xcpXaIE2n596RqRCUOcPLhfebReF5CngC9BGDVVbYBo8VLxpWGJb9HFkC1KDWj_D5ZUMqrUlEpHpLznHeUTpnmZ-RsxhfkzQ3msI1F8sXN51V5HaILcVt8wW4IDnNxXWd0RYrF8AOLDY42RCy-h67DvviUhuAfkQe-bjM-nt8L8u3d26_rD-Xm9v3H9WpT2qXWQ1lxrbQUilEHjAEIL9Fyhw3z6KniVACXzjXaA2hvUVnXNJopbUEzJwS_IC-P3q5PP0fMg9mHbLFt64hpzEZqLaQEOYGv_g0uOUglK_5fJQitQdOD8vlf4C6NfZy-axhwMQn1YcHXR2hbt2hCtCkOeDfY1La4RTMdY31rVkpJBlU10VdH2vYp5x696fqwr_tfBqg5NGvmZs1c1TTxbF5ibPbo_vCn_MWc19nWre_raEM-aafzMFrBxD09crs8pP6kUVJRxfhv3WmyKA</recordid><startdate>19900817</startdate><enddate>19900817</enddate><creator>O'Neil, Karyn T.</creator><creator>Hoess, Ronald H.</creator><creator>DeGrado, William F.</creator><general>American Society for the Advancement of Science</general><general>American Association for the Advancement of Science</general><general>The American Association for the Advancement of Science</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>0-V</scope><scope>3V.</scope><scope>7QF</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QQ</scope><scope>7QR</scope><scope>7SC</scope><scope>7SE</scope><scope>7SN</scope><scope>7SP</scope><scope>7SR</scope><scope>7SS</scope><scope>7T7</scope><scope>7TA</scope><scope>7TB</scope><scope>7TK</scope><scope>7TM</scope><scope>7U5</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88B</scope><scope>88E</scope><scope>88I</scope><scope>8AF</scope><scope>8BQ</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ALSLI</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>CJNVE</scope><scope>D1I</scope><scope>DWQXO</scope><scope>F28</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H8D</scope><scope>H8G</scope><scope>H94</scope><scope>HCIFZ</scope><scope>JG9</scope><scope>JQ2</scope><scope>K9-</scope><scope>K9.</scope><scope>KB.</scope><scope>KR7</scope><scope>L6V</scope><scope>L7M</scope><scope>LK8</scope><scope>L~C</scope><scope>L~D</scope><scope>M0K</scope><scope>M0P</scope><scope>M0R</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>MBDVC</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PCBAR</scope><scope>PDBOC</scope><scope>PQEDU</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>Q9U</scope><scope>R05</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19900817</creationdate><title>Design of DNA-Binding Peptides Based on the Leucine Zipper Motif</title><author>O'Neil, Karyn T. ; Hoess, Ronald H. ; DeGrado, William F.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c499t-6398975820d122115f7ec3deb2fef08305137ddb9f119fce8cdbb9289c192d553</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Base Sequence</topic><topic>Binding Sites</topic><topic>Biological and medical sciences</topic><topic>Chemical Phenomena</topic><topic>Chemistry, Physical</topic><topic>Circular Dichroism</topic><topic>Computer Simulation</topic><topic>Deoxyribonucleic acid</topic><topic>Dimers</topic><topic>DNA</topic><topic>DNA - metabolism</topic><topic>DNA binding proteins</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Enzymes</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gels</topic><topic>Genetic regulation</topic><topic>Hydrogen Bonding</topic><topic>Hydrogen bonds</topic><topic>Leucine</topic><topic>Macromolecular Substances</topic><topic>Modeling</topic><topic>Models, Molecular</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>Molecular Sequence Data</topic><topic>Nucleotide sequence</topic><topic>Nucleotide sequences</topic><topic>Oligonucleotides</topic><topic>Physiological aspects</topic><topic>Protein Conformation</topic><topic>Proteins</topic><topic>Scissors</topic><topic>Transcription. Transcription factor. Splicing. Rna processing</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>O'Neil, Karyn T.</creatorcontrib><creatorcontrib>Hoess, Ronald H.</creatorcontrib><creatorcontrib>DeGrado, William F.</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 Social Sciences Premium Collection</collection><collection>ProQuest Central (Corporate)</collection><collection>Aluminium Industry Abstracts</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Ceramic Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Computer and Information Systems Abstracts</collection><collection>Corrosion Abstracts</collection><collection>Ecology Abstracts</collection><collection>Electronics & Communications Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Materials Business File</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Education Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>STEM Database</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</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>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Social Science Premium Collection</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>eLibrary</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Earth, Atmospheric & Aquatic Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>Education Collection</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Engineering Research Database</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>Aerospace Database</collection><collection>Copper Technical Reference Library</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>Materials Research Database</collection><collection>ProQuest Computer Science Collection</collection><collection>Consumer Health Database (Alumni Edition)</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>Civil Engineering Abstracts</collection><collection>ProQuest Engineering Collection</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>ProQuest Biological Science Collection</collection><collection>Computer and Information Systems Abstracts Academic</collection><collection>Computer and Information Systems Abstracts Professional</collection><collection>Agricultural Science Database</collection><collection>Education Database</collection><collection>Consumer Health Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Engineering Database</collection><collection>Research Library (Corporate)</collection><collection>Advanced Technologies & Aerospace Database</collection><collection>ProQuest Advanced Technologies & Aerospace Collection</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environmental Science Database</collection><collection>Earth, Atmospheric & Aquatic Science Database</collection><collection>Materials Science Collection</collection><collection>ProQuest One Education</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>Engineering Collection</collection><collection>Environmental Science Collection</collection><collection>ProQuest Central Basic</collection><collection>University of Michigan</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Science (American Association for the Advancement of Science)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>O'Neil, Karyn T.</au><au>Hoess, Ronald H.</au><au>DeGrado, William F.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Design of DNA-Binding Peptides Based on the Leucine Zipper Motif</atitle><jtitle>Science (American Association for the Advancement of Science)</jtitle><addtitle>Science</addtitle><date>1990-08-17</date><risdate>1990</risdate><volume>249</volume><issue>4970</issue><spage>774</spage><epage>778</epage><pages>774-778</pages><issn>0036-8075</issn><eissn>1095-9203</eissn><coden>SCIEAS</coden><abstract>A class of transcriptional regulator proteins bind to DNA at dyad-symmetric sites through a motif consisting of (i) a "leucine zipper" sequence that associates into noncovalent, parallel, α-helical dimers and (ii) a covalently connected basic region necessary for binding DNA. The basic regions are predicted to be disordered in the absence of DNA and to form α helices when bound to DNA. These helices bind in the major groove forming multiple hydrogen-bonded and van der Waals contacts with the nucleotide bases. To test this model, two peptides were designed that were identical to natural leucine zipper proteins only at positions hypothesized to be critical for dimerization and DNA recognition. The peptides form dimers that bind specifically to DNA with their basic regions in α-helical conformations.</abstract><cop>Washington, DC</cop><pub>American Society for the Advancement of Science</pub><pmid>2389143</pmid><doi>10.1126/science.2389143</doi><tpages>5</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0036-8075 |
| ispartof | Science (American Association for the Advancement of Science), 1990-08, Vol.249 (4970), p.774-778 |
| issn | 0036-8075 1095-9203 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_79957717 |
| source | American Association for the Advancement of Science; Jstor Complete Legacy; MEDLINE |
| subjects | Amino Acid Sequence Amino acids Base Sequence Binding Sites Biological and medical sciences Chemical Phenomena Chemistry, Physical Circular Dichroism Computer Simulation Deoxyribonucleic acid Dimers DNA DNA - metabolism DNA binding proteins DNA-Binding Proteins - metabolism Enzymes Fundamental and applied biological sciences. Psychology Gels Genetic regulation Hydrogen Bonding Hydrogen bonds Leucine Macromolecular Substances Modeling Models, Molecular Molecular and cellular biology Molecular genetics Molecular Sequence Data Nucleotide sequence Nucleotide sequences Oligonucleotides Physiological aspects Protein Conformation Proteins Scissors Transcription. Transcription factor. Splicing. Rna processing |
| title | Design of DNA-Binding Peptides Based on the Leucine Zipper Motif |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-30T19%3A46%3A59IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_proqu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Design%20of%20DNA-Binding%20Peptides%20Based%20on%20the%20Leucine%20Zipper%20Motif&rft.jtitle=Science%20(American%20Association%20for%20the%20Advancement%20of%20Science)&rft.au=O'Neil,%20Karyn%20T.&rft.date=1990-08-17&rft.volume=249&rft.issue=4970&rft.spage=774&rft.epage=778&rft.pages=774-778&rft.issn=0036-8075&rft.eissn=1095-9203&rft.coden=SCIEAS&rft_id=info:doi/10.1126/science.2389143&rft_dat=%3Cgale_proqu%3EA8872166%3C/gale_proqu%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=213543195&rft_id=info:pmid/2389143&rft_galeid=A8872166&rft_jstor_id=2878082&rfr_iscdi=true |