| Year |
Citation |
Score |
| 2004 |
Nguyen-Hackley DH, Ramm E, Taylor CM, Joung JK, Dervan PB, Pabo CO. Allosteric inhibition of zinc-finger binding in the major groove of DNA by minor-groove binding ligands. Biochemistry. 43: 3880-90. PMID 15049695 DOI: 10.1021/Bi030223C |
0.416 |
|
| 2003 |
Wolfe SA, Grant RA, Pabo CO. Structure of a designed dimeric zinc finger protein bound to DNA. Biochemistry. 42: 13401-9. PMID 14621985 DOI: 10.1021/bi034830b |
0.493 |
|
| 2003 |
Hurt JA, Thibodeau SA, Hirsh AS, Pabo CO, Joung JK. Highly specific zinc finger proteins obtained by directed domain shuffling and cell-based selection. Proceedings of the National Academy of Sciences of the United States of America. 100: 12271-6. PMID 14527993 DOI: 10.1073/Pnas.2135381100 |
0.335 |
|
| 2003 |
Peisach E, Pabo CO. Constraints for zinc finger linker design as inferred from X-ray crystal structure of tandem Zif268-DNA complexes. Journal of Molecular Biology. 330: 1-7. PMID 12818197 DOI: 10.1016/S0022-2836(03)00572-2 |
0.429 |
|
| 2003 |
Jamieson AC, Miller JC, Pabo CO. Drug discovery with engineered zinc-finger proteins. Nature Reviews. Drug Discovery. 2: 361-8. PMID 12750739 DOI: 10.1038/nrd1087 |
0.342 |
|
| 2001 |
Miller JC, Pabo CO. Rearrangement of side-chains in a Zif268 mutant highlights the complexities of zinc finger-DNA recognition. Journal of Molecular Biology. 313: 309-15. PMID 11800559 DOI: 10.1006/jmbi.2001.4975 |
0.476 |
|
| 2001 |
Wolfe SA, Grant RA, Elrod-Erickson M, Pabo CO. Beyond the "recognition code": structures of two Cys2His2 zinc finger/TATA box complexes. Structure (London, England : 1993). 9: 717-23. PMID 11587646 DOI: 10.1016/S0969-2126(01)00632-3 |
0.409 |
|
| 2001 |
Wang BS, Grant RA, Pabo CO. Selected peptide extension contacts hydrophobic patch on neighboring zinc finger and mediates dimerization on DNA. Nature Structural Biology. 8: 589-93. PMID 11427887 DOI: 10.1038/89617 |
0.421 |
|
| 2001 |
Pabo CO, Peisach E, Grant RA. Design and selection of novel Cys2His2 zinc finger proteins. Annual Review of Biochemistry. 70: 313-40. PMID 11395410 DOI: 10.1146/annurev.biochem.70.1.313 |
0.419 |
|
| 2000 |
Pabo CO, Nekludova L. Geometric analysis and comparison of protein-DNA interfaces: why is there no simple code for recognition? Journal of Molecular Biology. 301: 597-624. PMID 10966773 DOI: 10.1006/jmbi.2000.3918 |
0.442 |
|
| 2000 |
Wolfe SA, Nekludova L, Pabo CO. DNA recognition by Cys2His2 zinc finger proteins. Annual Review of Biophysics and Biomolecular Structure. 29: 183-212. PMID 10940247 DOI: 10.1146/annurev.biophys.29.1.183 |
0.458 |
|
| 2000 |
Wolfe SA, Ramm EI, Pabo CO. Combining structure-based design with phage display to create new Cys(2)His(2) zinc finger dimers. Structure (London, England : 1993). 8: 739-50. PMID 10903945 DOI: 10.1016/S0969-2126(00)00161-1 |
0.401 |
|
| 2000 |
Grant RA, Rould MA, Klemm JD, Pabo CO. Exploring the role of glutamine 50 in the homeodomain-DNA interface: crystal structure of engrailed (Gln50 --> ala) complex at 2.0 A. Biochemistry. 39: 8187-92. PMID 10889025 DOI: 10.1021/bi000071a |
0.404 |
|
| 2000 |
Joung JK, Ramm EI, Pabo CO. A bacterial two-hybrid selection system for studying protein-DNA and protein-protein interactions. Proceedings of the National Academy of Sciences of the United States of America. 97: 7382-7. PMID 10852947 DOI: 10.1073/pnas.110149297 |
0.344 |
|
| 1999 |
Chasman D, Cepek K, Sharp PA, Pabo CO. Crystal structure of an OCA-B peptide bound to an Oct-1 POU domain/octamer DNA complex: specific recognition of a protein-DNA interface. Genes & Development. 13: 2650-7. PMID 10541551 DOI: 10.1101/gad.13.20.2650 |
0.419 |
|
| 1999 |
Wang BS, Pabo CO. Dimerization of zinc fingers mediated by peptides evolved in vitro from random sequences. Proceedings of the National Academy of Sciences of the United States of America. 96: 9568-73. PMID 10449733 DOI: 10.1073/pnas.96.17.9568 |
0.303 |
|
| 1999 |
Ohndorf UM, Rould MA, He Q, Pabo CO, Lippard SJ. Basis for recognition of cisplatin-modified DNA by high-mobility-group proteins. Nature. 399: 708-12. PMID 10385126 DOI: 10.1038/21460 |
0.472 |
|
| 1999 |
Elrod-Erickson M, Pabo CO. Binding studies with mutants of Zif268. Contribution of individual side chains to binding affinity and specificity in the Zif268 zinc finger-DNA complex. The Journal of Biological Chemistry. 274: 19281-5. PMID 10383437 DOI: 10.1074/jbc.274.27.19281 |
0.42 |
|
| 1999 |
Xu HE, Rould MA, Xu W, Epstein JA, Maas RL, Pabo CO. Crystal structure of the human Pax6 paired domain-DNA complex reveals specific roles for the linker region and carboxy-terminal subdomain in DNA binding. Genes & Development. 13: 1263-75. PMID 10346815 DOI: 10.1101/Gad.13.10.1263 |
0.519 |
|
| 1999 |
Zheng N, Fraenkel E, Pabo CO, Pavletich NP. Structural basis of DNA recognition by the heterodimeric cell cycle transcription factor E2F-DP. Genes & Development. 13: 666-74. PMID 10090723 DOI: 10.1101/Gad.13.6.666 |
0.805 |
|
| 1999 |
Wolfe SA, Greisman HA, Ramm EI, Pabo CO. Analysis of zinc fingers optimized via phage display: evaluating the utility of a recognition code. Journal of Molecular Biology. 285: 1917-34. PMID 9925775 DOI: 10.1006/jmbi.1998.2421 |
0.415 |
|
| 1998 |
Fraenkel E, Rould MA, Chambers KA, Pabo CO. Engrailed homeodomain-DNA complex at 2.2 A resolution: a detailed view of the interface and comparison with other engrailed structures. Journal of Molecular Biology. 284: 351-61. PMID 9813123 DOI: 10.1006/Jmbi.1998.2147 |
0.675 |
|
| 1998 |
Fraenkel E, Pabo CO. Comparison of X-ray and NMR structures for the Antennapedia homeodomain-DNA complex. Nature Structural Biology. 5: 692-7. PMID 9699632 DOI: 10.1038/1382 |
0.676 |
|
| 1998 |
Elrod-Erickson M, Benson TE, Pabo CO. High-resolution structures of variant Zif268-DNA complexes: implications for understanding zinc finger-DNA recognition. Structure (London, England : 1993). 6: 451-64. PMID 9562555 |
0.485 |
|
| 1998 |
Kim JS, Pabo CO. Getting a handhold on DNA: design of poly-zinc finger proteins with femtomolar dissociation constants. Proceedings of the National Academy of Sciences of the United States of America. 95: 2812-7. PMID 9501172 DOI: 10.1073/Pnas.95.6.2812 |
0.504 |
|
| 1998 |
Pomerantz JL, Wolfe SA, Pabo CO. Structure-based design of a dimeric zinc finger protein. Biochemistry. 37: 965-70. PMID 9467467 DOI: 10.1021/bi972464o |
0.42 |
|
| 1997 |
Kim JS, Pabo CO. Transcriptional repression by zinc finger peptides. Exploring the potential for applications in gene therapy. The Journal of Biological Chemistry. 272: 29795-800. PMID 9368051 DOI: 10.1074/Jbc.272.47.29795 |
0.403 |
|
| 1997 |
Tucker-Kellogg L, Rould MA, Chambers KA, Ades SE, Sauer RT, Pabo CO. Engrailed (Gln50-->Lys) homeodomain-DNA complex at 1.9 A resolution: structural basis for enhanced affinity and altered specificity. Structure (London, England : 1993). 5: 1047-54. PMID 9309220 DOI: 10.1016/S0969-2126(97)00256-6 |
0.765 |
|
| 1997 |
Kim JS, Kim J, Cepek KL, Sharp PA, Pabo CO. Design of TATA box-binding protein/zinc finger fusions for targeted regulation of gene expression. Proceedings of the National Academy of Sciences of the United States of America. 94: 3616-20. PMID 9108026 DOI: 10.1073/Pnas.94.8.3616 |
0.552 |
|
| 1997 |
Greisman HA, Pabo CO. A general strategy for selecting high-affinity zinc finger proteins for diverse DNA target sites. Science (New York, N.Y.). 275: 657-61. PMID 9005850 DOI: 10.1126/science.275.5300.657 |
0.406 |
|
| 1996 |
Elrod-Erickson M, Rould MA, Nekludova L, Pabo CO. Zif268 protein-DNA complex refined at 1.6 A: a model system for understanding zinc finger-DNA interactions. Structure (London, England : 1993). 4: 1171-80. PMID 8939742 |
0.456 |
|
| 1996 |
Rebar EJ, Greisman HA, Pabo CO. Phage display methods for selecting zinc finger proteins with novel DNA-binding specificities. Methods in Enzymology. 267: 129-49. PMID 8743314 |
0.397 |
|
| 1996 |
Klemm JD, Pabo CO. Oct-1 POU domain-DNA interactions: cooperative binding of isolated subdomains and effects of covalent linkage. Genes & Development. 10: 27-36. PMID 8557192 |
0.417 |
|
| 1995 |
Xu W, Rould MA, Jun S, Desplan C, Pabo CO. Crystal structure of a paired domain-DNA complex at 2.5 A resolution reveals structural basis for Pax developmental mutations. Cell. 80: 639-50. PMID 7867071 DOI: 10.1016/0092-8674(95)90518-9 |
0.438 |
|
| 1995 |
Pomerantz JL, Sharp PA, Pabo CO. Structure-based design of transcription factors. Science (New York, N.Y.). 267: 93-6. PMID 7809612 DOI: 10.1126/science.7809612 |
0.435 |
|
| 1995 |
Pomerantz JL, Pabo CO, Sharp PA. Analysis of homeodomain function by structure-based design of a transcription factor. Proceedings of the National Academy of Sciences of the United States of America. 92: 9752-6. PMID 7568211 DOI: 10.1073/pnas.92.21.9752 |
0.334 |
|
| 1994 |
Rebar EJ, Pabo CO. Zinc finger phage: affinity selection of fingers with new DNA-binding specificities. Science (New York, N.Y.). 263: 671-3. PMID 8303274 |
0.432 |
|
| 1994 |
Ma PC, Rould MA, Weintraub H, Pabo CO. Crystal structure of MyoD bHLH domain-DNA complex: perspectives on DNA recognition and implications for transcriptional activation. Cell. 77: 451-9. PMID 8181063 DOI: 10.1016/0092-8674(94)90159-7 |
0.482 |
|
| 1994 |
Klemm JD, Rould MA, Aurora R, Herr W, Pabo CO. Crystal structure of the Oct-1 POU domain bound to an octamer site: DNA recognition with tethered DNA-binding modules. Cell. 77: 21-32. PMID 8156594 DOI: 10.1016/0092-8674(94)90231-3 |
0.472 |
|
| 1994 |
Raumann BE, Rould MA, Pabo CO, Sauer RT. DNA recognition by beta-sheets in the Arc repressor-operator crystal structure. Nature. 367: 754-7. PMID 8107872 DOI: 10.1038/367754A0 |
0.577 |
|
| 1994 |
Nekludova L, Pabo CO. Distinctive DNA conformation with enlarged major groove is found in Zn-finger-DNA and other protein-DNA complexes. Proceedings of the National Academy of Sciences of the United States of America. 91: 6948-52. PMID 8041727 DOI: 10.1073/pnas.91.15.6948 |
0.432 |
|
| 1994 |
Clarke ND, Kissinger CR, Desjarlais J, Gilliland GL, Pabo CO. Structural studies of the engrailed homeodomain. Protein Science : a Publication of the Protein Society. 3: 1779-87. PMID 7849596 DOI: 10.1002/Pro.5560031018 |
0.406 |
|
| 1993 |
Pavletich NP, Pabo CO. Crystal structure of a five-finger GLI-DNA complex: new perspectives on zinc fingers. Science (New York, N.Y.). 261: 1701-7. PMID 8378770 |
0.788 |
|
| 1993 |
Pavletich NP, Chambers KA, Pabo CO. The DNA-binding domain of p53 contains the four conserved regions and the major mutation hot spots. Genes & Development. 7: 2556-64. PMID 8276238 |
0.758 |
|
| 1992 |
Godley L, Pfeifer J, Steinhauer D, Ely B, Shaw G, Kaufmann R, Suchanek E, Pabo C, Skehel JJ, Wiley DC. Introduction of intersubunit disulfide bonds in the membrane-distal region of the influenza hemagglutinin abolishes membrane fusion activity. Cell. 68: 635-45. PMID 1739972 DOI: 10.1016/0092-8674(92)90140-8 |
0.436 |
|
| 1992 |
Pabo CO, Sauer RT. Transcription factors: structural families and principles of DNA recognition. Annual Review of Biochemistry. 61: 1053-95. PMID 1497306 DOI: 10.1146/Annurev.Bi.61.070192.005201 |
0.513 |
|
| 1992 |
Beamer LJ, Pabo CO. Refined 1.8 A crystal structure of the lambda repressor-operator complex. Journal of Molecular Biology. 227: 177-96. PMID 1387915 DOI: 10.1016/0022-2836(92)90690-L |
0.447 |
|
| 1991 |
Pavletich NP, Pabo CO. Zinc finger-DNA recognition: crystal structure of a Zif268-DNA complex at 2.1 A. Science (New York, N.Y.). 252: 809-17. PMID 2028256 DOI: 10.1126/Science.2028256 |
0.804 |
|
| 1991 |
Wolberger C, Pabo CO, Vershon AK, Johnson AD. Crystallization and preliminary X-ray diffraction studies of a MAT alpha 2-DNA complex. Journal of Molecular Biology. 217: 11-3. PMID 1988673 DOI: 10.1016/0022-2836(91)90605-6 |
0.777 |
|
| 1991 |
Clarke ND, Beamer LJ, Goldberg HR, Berkower C, Pabo CO. The DNA binding arm of lambda repressor: critical contacts from a flexible region. Science (New York, N.Y.). 254: 267-70. PMID 1833818 DOI: 10.1126/Science.1833818 |
0.391 |
|
| 1991 |
Wolberger C, Vershon AK, Liu B, Johnson AD, Pabo CO. Crystal structure of a MAT alpha 2 homeodomain-operator complex suggests a general model for homeodomain-DNA interactions. Cell. 67: 517-28. PMID 1682054 DOI: 10.1016/0092-8674(91)90526-5 |
0.773 |
|
| 1990 |
Pabo CO, Aggarwal AK, Jordan SR, Beamer LJ, Obeysekare UR, Harrison SC. Conserved residues make similar contacts in two repressor-operator complexes. Science (New York, N.Y.). 247: 1210-3. PMID 2315694 DOI: 10.1126/Science.2315694 |
0.634 |
|
| 1990 |
Sauer RT, Jordan SR, Pabo CO. Lambda repressor: a model system for understanding protein-DNA interactions and protein stability. Advances in Protein Chemistry. 40: 1-61. PMID 2195849 DOI: 10.1016/S0065-3233(08)60286-7 |
0.68 |
|
| 1990 |
Bowie JU, Clarke ND, Pabo CO, Sauer RT. Identification of protein folds: matching hydrophobicity patterns of sequence sets with solvent accessibility patterns of known structures. Proteins. 7: 257-64. PMID 2163535 DOI: 10.1002/Prot.340070307 |
0.526 |
|
| 1990 |
Kissinger CR, Liu BS, Martin-Blanco E, Kornberg TB, Pabo CO. Crystal structure of an engrailed homeodomain-DNA complex at 2.8 A resolution: a framework for understanding homeodomain-DNA interactions. Cell. 63: 579-90. PMID 1977522 DOI: 10.1016/0092-8674(90)90453-L |
0.545 |
|
| 1990 |
Liu B, Kissinger CR, Pabo CO. Crystallization and preliminary X-ray diffraction studies of the engrailed homeodomain and of an engrailed homeodomain/DNA complex. Biochemical and Biophysical Research Communications. 171: 257-9. PMID 1975495 DOI: 10.1016/0006-291X(90)91385-6 |
0.373 |
|
| 1988 |
Frankel AD, Pabo CO. Fingering too many proteins. Cell. 53: 675. PMID 3370671 DOI: 10.1016/0092-8674(88)90083-9 |
0.55 |
|
| 1988 |
Jordan SR, Pabo CO. Structure of the lambda complex at 2.5 A resolution: details of the repressor-operator interactions. Science (New York, N.Y.). 242: 893-9. PMID 3187530 DOI: 10.1126/Science.3187530 |
0.496 |
|
| 1988 |
Stearman RS, Frankel AD, Freire E, Liu BS, Pabo CO. Combining thermostable mutations increases the stability of lambda repressor. Biochemistry. 27: 7571-4. PMID 3061460 DOI: 10.1021/Bi00419A059 |
0.564 |
|
| 1988 |
Frankel AD, Pabo CO. Cellular uptake of the tat protein from human immunodeficiency virus. Cell. 55: 1189-93. PMID 2849510 DOI: 10.1016/0092-8674(88)90263-2 |
0.568 |
|
| 1988 |
Frankel AD, Chen L, Cotter RJ, Pabo CO. Dimerization of the tat protein from human immunodeficiency virus: a cysteine-rich peptide mimics the normal metal-linked dimer interface. Proceedings of the National Academy of Sciences of the United States of America. 85: 6297-300. PMID 2842763 DOI: 10.1073/Pnas.85.17.6297 |
0.592 |
|
| 1988 |
Frankel AD, Bredt DS, Pabo CO. Tat protein from human immunodeficiency virus forms a metal-linked dimer. Science (New York, N.Y.). 240: 70-3. PMID 2832944 DOI: 10.1126/Science.2832944 |
0.571 |
|
| 1987 |
Frankel AD, Berg JM, Pabo CO. Metal-dependent folding of a single zinc finger from transcription factor IIIA. Proceedings of the National Academy of Sciences of the United States of America. 84: 4841-5. PMID 3474629 DOI: 10.1073/Pnas.84.14.4841 |
0.597 |
|
| 1987 |
Weiss MA, Pabo CO, Karplus M, Sauer RT. Dimerization of the operator binding domain of phage lambda repressor. Biochemistry. 26: 897-904. PMID 2952164 DOI: 10.1021/Bi00377A034 |
0.615 |
|
| 1986 |
Sauer RT, Hehir K, Stearman RS, Weiss MA, Jeitler-Nilsson A, Suchanek EG, Pabo CO. An engineered intersubunit disulfide enhances the stability and DNA binding of the N-terminal domain of lambda repressor. Biochemistry. 25: 5992-8. PMID 3539184 DOI: 10.1021/Bi00368A024 |
0.648 |
|
| 1985 |
Jordan SR, Pabo CO, Vershon AK, Sauer RT. Crystallization of the Arc repressor. Journal of Molecular Biology. 185: 445-6. PMID 4057251 DOI: 10.1016/0022-2836(85)90415-2 |
0.479 |
|
| 1985 |
Jordan SR, Whitcombe TV, Berg JM, Pabo CO. Systematic variation in DNA length yields highly ordered repressor-operator cocrystals. Science (New York, N.Y.). 230: 1383-5. PMID 3906896 DOI: 10.1126/Science.3906896 |
0.438 |
|
| 1984 |
Pabo CO, Sauer RT. Protein-DNA recognition. Annual Review of Biochemistry. 53: 293-321. PMID 6236744 DOI: 10.1146/Annurev.Bi.53.070184.001453 |
0.653 |
|
| 1983 |
Pabo CO, Jordan SR, Frankel AD. Systematic analysis of possible hydrogen bonds between amino acid side chains and B-form DNA. Journal of Biomolecular Structure & Dynamics. 1: 1039-49. PMID 6400903 DOI: 10.1080/07391102.1983.10507501 |
0.591 |
|
| 1983 |
Lewis M, Jeffrey A, Wang J, Ladner R, Ptashne M, Pabo CO. Structure of the operator-binding domain of bacteriophage lambda repressor: implications for DNA recognition and gene regulation. Cold Spring Harbor Symposia On Quantitative Biology. 47: 435-40. PMID 6305562 DOI: 10.1101/Sqb.1983.047.01.051 |
0.72 |
|
| 1983 |
Ohlendorf DH, Anderson WF, Lewis M, Pabo CO, Matthews BW. Comparison of the structures of cro and lambda repressor proteins from bacteriophage lambda. Journal of Molecular Biology. 169: 757-69. PMID 6226802 DOI: 10.1016/S0022-2836(83)80169-7 |
0.341 |
|
| 1982 |
Pabo CO, Lewis M. The operator-binding domain of lambda repressor: structure and DNA recognition. Nature. 298: 443-7. PMID 7088190 DOI: 10.1038/298443a0 |
0.41 |
|
| 1982 |
Pabo CO, Krovatin W, Jeffrey A, Sauer RT. The N-terminal arms of lambda repressor wrap around the operator DNA. Nature. 298: 441-3. PMID 7088189 DOI: 10.1038/298441A0 |
0.566 |
|
| 1982 |
Sauer RT, Yocum RR, Doolittle RF, Lewis M, Pabo CO. Homology among DNA-binding proteins suggests use of a conserved super-secondary structure. Nature. 298: 447-51. PMID 6896364 DOI: 10.1038/298447A0 |
0.629 |
|
| 1982 |
Ptashne M, Johnson AD, Pabo CO. A genetic switch in a bacterial virus. Scientific American. 247: 128-30, 132, 134-40. PMID 6216590 DOI: 10.1038/Scientificamerican1182-128 |
0.636 |
|
| 1980 |
Johnson AD, Pabo CO, Sauer RT. Bacteriophage lambda repressor and cro protein: interactions with operator DNA. Methods in Enzymology. 65: 839-56. PMID 6445470 DOI: 10.1016/S0076-6879(80)65078-2 |
0.67 |
|
| 1980 |
Ptashne M, Jeffrey A, Johnson AD, Maurer R, Meyer BJ, Pabo CO, Roberts TM, Sauer RT. How the lambda repressor and cro work. Cell. 19: 1-11. PMID 6444544 DOI: 10.1016/0092-8674(80)90383-9 |
0.71 |
|
| 1979 |
Sauer RT, Pabo CO, Meyer BJ, Ptashne M, Backman KC. Regulatory functions of the lambda repressor reside in the amino-terminal domain. Nature. 279: 396-400. PMID 16068162 DOI: 10.1038/279396A0 |
0.766 |
|
| 1979 |
Pabo CO, Sauer RT, Sturtevant JM, Ptashne M. The lambda repressor contains two domains. Proceedings of the National Academy of Sciences of the United States of America. 76: 1608-12. PMID 287002 DOI: 10.1073/Pnas.76.4.1608 |
0.724 |
|
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