Year |
Citation |
Score |
2016 |
Volpon L, Culjkovic-Kraljacic B, Osborne MJ, Ramteke A, Sun Q, Niesman A, Chook YM, Borden KL. Importin 8 mediates m7G cap-sensitive nuclear import of the eukaryotic translation initiation factor eIF4E. Proceedings of the National Academy of Sciences of the United States of America. PMID 27114554 DOI: 10.1073/pnas.1524291113 |
0.302 |
|
2013 |
Culjkovic B, Fernando T, Yang S, Melnick AM, Borden KL, Cerchietti L. The Eukaryotic Translation Initiation Factor 4E (eIF4E) Has Oncogenic Functions and May Represent a New Therapeutic Target In Diffuse Large B Cell Lymphoma (DLBCL) Blood. 122: 3785-3785. DOI: 10.1182/blood.V122.21.3785.3785 |
0.317 |
|
2010 |
Volpon L, Osborne MJ, Capul AA, de la Torre JC, Borden KL. Structural characterization of the Z RING-eIF4E complex reveals a distinct mode of control for eIF4E. Proceedings of the National Academy of Sciences of the United States of America. 107: 5441-6. PMID 20212144 DOI: 10.1073/Pnas.0909877107 |
0.46 |
|
2009 |
Ploski JE, Topisirovic I, Park KW, Borden KL, Radu A. A mechanism of nucleocytoplasmic trafficking for the homeodomain protein PRH. Molecular and Cellular Biochemistry. 332: 173-81. PMID 19588232 DOI: 10.1007/S11010-009-0188-0 |
0.332 |
|
2007 |
Peng H, Gibson LC, Capili AD, Borden KL, Osborne MJ, Harper SL, Speicher DW, Zhao K, Marmorstein R, Rock TA, Rauscher FJ. The structurally disordered KRAB repression domain is incorporated into a protease resistant core upon binding to KAP-1-RBCC domain. Journal of Molecular Biology. 370: 269-89. PMID 17512541 DOI: 10.1016/j.jmb.2007.03.047 |
0.687 |
|
2005 |
Djavani M, Topisirovic I, Zapata JC, Sadowska M, Yang Y, Rodas J, Lukashevich IS, Bogue CW, Pauza CD, Borden KL, Salvato MS. The proline-rich homeodomain (PRH/HEX) protein is down-regulated in liver during infection with lymphocytic choriomeningitis virus. Journal of Virology. 79: 2461-73. PMID 15681447 DOI: 10.1128/Jvi.79.4.2461-2473.2005 |
0.366 |
|
2005 |
Topisirovic I, Kentsis A, Perez JM, Guzman ML, Jordan CT, Borden KL. Eukaryotic translation initiation factor 4E activity is modulated by HOXA9 at multiple levels. Molecular and Cellular Biology. 25: 1100-12. PMID 15657436 DOI: 10.1128/Mcb.25.3.1100-1112.2005 |
0.63 |
|
2003 |
Topisirovic I, Guzman ML, McConnell MJ, Licht JD, Culjkovic B, Neering SJ, Jordan CT, Borden KL. Aberrant eukaryotic translation initiation factor 4E-dependent mRNA transport impedes hematopoietic differentiation and contributes to leukemogenesis. Molecular and Cellular Biology. 23: 8992-9002. PMID 14645512 DOI: 10.1128/Mcb.23.24.8992-9002.2003 |
0.416 |
|
2003 |
Seker H, Rubbi C, Linke SP, Bowman ED, Garfield S, Hansen L, Borden KL, Milner J, Harris CC. UV-C-induced DNA damage leads to p53-dependent nuclear trafficking of PML. Oncogene. 22: 1620-8. PMID 12642865 DOI: 10.1038/Sj.Onc.1206140 |
0.31 |
|
2003 |
Topisirovic I, Culjkovic B, Cohen N, Perez JM, Skrabanek L, Borden KL. The proline-rich homeodomain protein, PRH, is a tissue-specific inhibitor of eIF4E-dependent cyclin D1 mRNA transport and growth. The Embo Journal. 22: 689-703. PMID 12554669 DOI: 10.1093/Emboj/Cdg069 |
0.464 |
|
2002 |
Topisirovic I, Capili AD, Borden KL. Gamma interferon and cadmium treatments modulate eukaryotic initiation factor 4E-dependent mRNA transport of cyclin D1 in a PML-dependent manner. Molecular and Cellular Biology. 22: 6183-98. PMID 12167712 DOI: 10.1128/Mcb.22.17.6183-6198.2002 |
0.66 |
|
2002 |
Borden KL. Pondering the promyelocytic leukemia protein (PML) puzzle: possible functions for PML nuclear bodies. Molecular and Cellular Biology. 22: 5259-69. PMID 12101223 DOI: 10.1128/Mcb.22.15.5259-5269.2002 |
0.455 |
|
2002 |
Strudwick S, Borden KL. The emerging roles of translation factor eIF4E in the nucleus. Differentiation; Research in Biological Diversity. 70: 10-22. PMID 11963652 DOI: 10.1046/J.1432-0436.2002.700102.X |
0.459 |
|
2001 |
Capili AD, Schultz DC, RauscherIII FJ, Borden KL. Solution structure of the PHD domain from the KAP-1 corepressor: structural determinants for PHD, RING and LIM zinc-binding domains. The Embo Journal. 20: 165-77. PMID 11226167 DOI: 10.1093/Emboj/20.1.165 |
0.675 |
|
2000 |
Topcu Z, Borden KL. The yeast two-hybrid system and its pharmaceutical significance. Pharmaceutical Research. 17: 1049-55. PMID 11087035 DOI: 10.1023/A:1026493310144 |
0.351 |
|
2000 |
Melnick A, Ahmad KF, Arai S, Polinger A, Ball H, Borden KL, Carlile GW, Prive GG, Licht JD. In-depth mutational analysis of the promyelocytic leukemia zinc finger BTB/POZ domain reveals motifs and residues required for biological and transcriptional functions. Molecular and Cellular Biology. 20: 6550-67. PMID 10938130 DOI: 10.1128/Mcb.20.17.6550-6567.2000 |
0.391 |
|
2000 |
Lai HK, Borden KL. The promyelocytic leukemia (PML) protein suppresses cyclin D1 protein production by altering the nuclear cytoplasmic distribution of cyclin D1 mRNA. Oncogene. 19: 1623-34. PMID 10763819 DOI: 10.1038/Sj.Onc.1203473 |
0.43 |
|
2000 |
Campbell Dwyer EJ, Lai H, MacDonald RC, Salvato MS, Borden KL. The lymphocytic choriomeningitis virus RING protein Z associates with eukaryotic initiation factor 4E and selectively represses translation in a RING-dependent manner. Journal of Virology. 74: 3293-300. PMID 10708446 DOI: 10.1128/Jvi.74.7.3293-3300.2000 |
0.447 |
|
2000 |
Borden KL. RING domains: master builders of molecular scaffolds? Journal of Molecular Biology. 295: 1103-12. PMID 10653689 DOI: 10.1006/Jmbi.1999.3429 |
0.471 |
|
1999 |
Topcu Z, Mack DL, Hromas RA, Borden KL. The promyelocytic leukemia protein PML interacts with the proline-rich homeodomain protein PRH: a RING may link hematopoiesis and growth control. Oncogene. 18: 7091-100. PMID 10597310 DOI: 10.1038/Sj.Onc.1203201 |
0.498 |
|
1998 |
Borden KL. RING fingers and B-boxes: zinc-binding protein-protein interaction domains. Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire. 76: 351-8. PMID 9923704 DOI: 10.1139/Bcb-76-2-3-351 |
0.514 |
|
1998 |
Carlile GW, Tatton WG, Borden KL. Demonstration of a RNA-dependent nuclear interaction between the promyelocytic leukaemia protein and glyceraldehyde-3-phosphate dehydrogenase. The Biochemical Journal. 335: 691-6. PMID 9794812 DOI: 10.1042/Bj3350691 |
0.375 |
|
1998 |
Borden KL. Structure/function in neuroprotection and apoptosis. Annals of Neurology. 44: S65-71. PMID 9749576 DOI: 10.1002/Ana.410440711 |
0.407 |
|
1998 |
Cao T, Duprez E, Borden KL, Freemont PS, Etkin LD. Ret finger protein is a normal component of PML nuclear bodies and interacts directly with PML. Journal of Cell Science. 111: 1319-29. PMID 9570750 |
0.419 |
|
1998 |
Borden KL, Campbelldwyer EJ, Carlile GW, Djavani M, Salvato MS. Two RING finger proteins, the oncoprotein PML and the arenavirus Z protein, colocalize with the nuclear fraction of the ribosomal P proteins. Journal of Virology. 72: 3819-26. PMID 9557665 DOI: 10.1128/Jvi.72.5.3819-3826.1998 |
0.376 |
|
1998 |
Borden KL, Campbell Dwyer EJ, Salvato MS. An arenavirus RING (zinc-binding) protein binds the oncoprotein promyelocyte leukemia protein (PML) and relocates PML nuclear bodies to the cytoplasm. Journal of Virology. 72: 758-66. PMID 9420283 DOI: 10.1128/Jvi.72.1.758-766.1998 |
0.467 |
|
1997 |
Borden KL, CampbellDwyer EJ, Salvato MS. The promyelocytic leukemia protein PML has a pro-apoptotic activity mediated through its RING domain. Febs Letters. 418: 30-4. PMID 9414089 DOI: 10.1016/S0014-5793(97)01344-6 |
0.399 |
|
1997 |
Boddy MN, Duprez E, Borden KL, Freemont PS. Surface residue mutations of the PML RING finger domain alter the formation of nuclear matrix-associated PML bodies. Journal of Cell Science. 110: 2197-205. PMID 9378769 |
0.404 |
|
1997 |
Cao T, Borden KL, Freemont PS, Etkin LD. Involvement of the rfp tripartite motif in protein-protein interactions and subcellular distribution. Journal of Cell Science. 110: 1563-71. PMID 9247190 |
0.421 |
|
1996 |
Borden KL, Freemont PS. The RING finger domain: a recent example of a sequence-structure family. Current Opinion in Structural Biology. 6: 395-401. PMID 8804826 DOI: 10.1016/S0959-440X(96)80060-1 |
0.37 |
|
1996 |
Saurin AJ, Borden KL, Boddy MN, Freemont PS. Does this have a familiar RING? Trends in Biochemical Sciences. 21: 208-14. PMID 8744354 DOI: 10.1016/S0968-0004(96)80017-X |
0.525 |
|
1996 |
Borden KL, Lally JM, Martin SR, O'Reilly NJ, Solomon E, Freemont PS. In vivo and in vitro characterization of the B1 and B2 zinc-binding domains from the acute promyelocytic leukemia protooncoprotein PML. Proceedings of the National Academy of Sciences of the United States of America. 93: 1601-6. PMID 8643677 DOI: 10.1073/Pnas.93.4.1601 |
0.422 |
|
1995 |
Borden KL, Boddy MN, Lally J, O'Reilly NJ, Martin S, Howe K, Solomon E, Freemont PS. The solution structure of the RING finger domain from the acute promyelocytic leukaemia proto-oncoprotein PML. The Embo Journal. 14: 1532-41. PMID 7729428 DOI: 10.1002/J.1460-2075.1995.Tb07139.X |
0.427 |
|
1994 |
Boddy MN, Freemont PS, Borden KL. The p53-associated protein MDM2 contains a newly characterized zinc-binding domain called the RING finger. Trends in Biochemical Sciences. 19: 198-9. PMID 8048160 DOI: 10.1016/0968-0004(94)90020-5 |
0.478 |
|
1990 |
Borden KL, Richards FM. Folding of the reduced form of the thioredoxin from bacteriophage T4. Biochemistry. 29: 8207-10. PMID 2252882 DOI: 10.1021/Bi00488A002 |
0.464 |
|
1990 |
Borden KL, Richards FM. Folding kinetics of phage T4 thioredoxin. Biochemistry. 29: 3071-7. PMID 2186806 DOI: 10.1021/Bi00464A025 |
0.435 |
|
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