Year |
Citation |
Score |
2024 |
Bagchi A, Stayrook SE, Xenaki KT, Starbird CA, Doulkeridou S, El Khoulati R, Roovers RC, Schmitz KR, van Bergen En Henegouwen PMP, Ferguson KM. Structural insights into the role and targeting of EGFRvIII. Structure (London, England : 1993). PMID 38908376 DOI: 10.1016/j.str.2024.05.018 |
0.777 |
|
2022 |
Hu C, Leche CA, Kiyatkin A, Yu Z, Stayrook SE, Ferguson KM, Lemmon MA. Glioblastoma mutations alter EGFR dimer structure to prevent ligand bias. Nature. 602: 518-522. PMID 35140400 DOI: 10.1038/s41586-021-04393-3 |
0.42 |
|
2020 |
Ferguson KM, Hu C, Lemmon MA. Insulin and EGF receptor family members share parallel activation mechanisms. Protein Science : a Publication of the Protein Society. PMID 32297376 DOI: 10.1002/Pro.3871 |
0.554 |
|
2018 |
Emptage RP, Lemmon MA, Ferguson KM, Marmorstein R. Structural Basis for MARK1 Kinase Autoinhibition by Its KA1 Domain. Structure (London, England : 1993). 26: 1137-1143.e3. PMID 30099988 DOI: 10.1016/J.Str.2018.05.008 |
0.687 |
|
2017 |
Bagchi A, Haidar JN, Eastman SW, Vieth M, Topper M, Iacolina MD, Walker JM, Forest A, Shen Y, Novosiadly RD, Ferguson KM. Molecular basis for necitumumab inhibition of EGFR variants associated with acquired cetuximab resistance. Molecular Cancer Therapeutics. PMID 29158469 DOI: 10.1158/1535-7163.Mct-17-0575 |
0.784 |
|
2017 |
Freed DM, Bessman NJ, Kiyatkin A, Salazar-Cavazos E, Byrne PO, Moore JO, Valley CC, Ferguson KM, Leahy DJ, Lidke DS, Lemmon MA. EGFR Ligands Differentially Stabilize Receptor Dimers to Specify Signaling Kinetics. Cell. PMID 28988771 DOI: 10.1016/J.Cell.2017.09.017 |
0.506 |
|
2017 |
Emptage RP, Schoenberger MJ, Ferguson KM, Marmorstein R. Intramolecular autoinhibition of Checkpoint Kinase 1 is mediated by conserved basic motifs of the C-terminal Kinase Associated-1 domain. The Journal of Biological Chemistry. PMID 28972186 DOI: 10.1074/Jbc.M117.811265 |
0.652 |
|
2017 |
Moore JO, Lemmon MA, Ferguson KM. Dimerization of Tie2 mediated by its membrane-proximal FNIII domains. Proceedings of the National Academy of Sciences of the United States of America. PMID 28396397 DOI: 10.1073/Pnas.1617800114 |
0.563 |
|
2016 |
Emptage RP, Lemmon MA, Ferguson KM. Molecular determinants of KA1 domain-mediated autoinhibition and phospholipid activation of MARK1 kinase. The Biochemical Journal. PMID 27879374 DOI: 10.1042/Bcj20160792 |
0.538 |
|
2015 |
Moravcevic K, Alvarado D, Schmitz KR, Kenniston JA, Mendrola JM, Ferguson KM, Lemmon MA. Comparison of Saccharomyces cerevisiae F-BAR domain structures reveals a conserved inositol phosphate binding site. Structure (London, England : 1993). 23: 352-63. PMID 25620000 DOI: 10.1016/J.Str.2014.12.009 |
0.734 |
|
2014 |
Bessman NJ, Bagchi A, Ferguson KM, Lemmon MA. Complex relationship between ligand binding and dimerization in the epidermal growth factor receptor. Cell Reports. 9: 1306-17. PMID 25453753 DOI: 10.1016/J.Celrep.2014.10.010 |
0.799 |
|
2014 |
Huoh YS, Ferguson KM. The pellino e3 ubiquitin ligases recognize specific phosphothreonine motifs and have distinct substrate specificities. Biochemistry. 53: 4946-55. PMID 25027698 DOI: 10.1021/Bi5005156 |
0.799 |
|
2014 |
Lemmon MA, Schlessinger J, Ferguson KM. The EGFR family: not so prototypical receptor tyrosine kinases. Cold Spring Harbor Perspectives in Biology. 6: a020768. PMID 24691965 DOI: 10.1101/Cshperspect.A020768 |
0.536 |
|
2014 |
Bagchi A, Bessman NJ, Wu NZ, Raines L, Kan Z, Hu W, Englander SW, Leahy DJ, Lemmon MA, Ferguson KM. Allosteric Regulation of the Epidermal Growth Factor Receptor Biophysical Journal. 106: 105a. DOI: 10.1016/J.Bpj.2013.11.650 |
0.797 |
|
2013 |
Schmitz KR, Bagchi A, Roovers RC, van Bergen en Henegouwen PM, Ferguson KM. Structural evaluation of EGFR inhibition mechanisms for nanobodies/VHH domains. Structure (London, England : 1993). 21: 1214-24. PMID 23791944 DOI: 10.1016/J.Str.2013.05.008 |
0.796 |
|
2013 |
Huoh Y, Ferguson KM. The Molecular Basis of Substrate Recognition by the E3 Ubiquitin Ligase Pellino Biophysical Journal. 104. DOI: 10.1016/J.Bpj.2012.11.3384 |
0.804 |
|
2012 |
Wood CS, Hung CS, Huoh YS, Mousley CJ, Stefan CJ, Bankaitis V, Ferguson KM, Burd CG. Local control of phosphatidylinositol 4-phosphate signaling in the Golgi apparatus by Vps74 and Sac1 phosphoinositide phosphatase. Molecular Biology of the Cell. 23: 2527-36. PMID 22553352 DOI: 10.1091/Mbc.E12-01-0077 |
0.761 |
|
2012 |
Ferguson KM. Discoidin discoveries. Structure (London, England : 1993). 20: 568-70. PMID 22483103 DOI: 10.1016/j.str.2012.03.003 |
0.352 |
|
2011 |
Roovers RC, Vosjan MJ, Laeremans T, el Khoulati R, de Bruin RC, Ferguson KM, Verkleij AJ, van Dongen GA, van Bergen en Henegouwen PM. A biparatopic anti-EGFR nanobody efficiently inhibits solid tumour growth. International Journal of Cancer. 129: 2013-24. PMID 21520037 DOI: 10.1002/Ijc.26145 |
0.481 |
|
2009 |
Wood CS, Schmitz KR, Bessman NJ, Setty TG, Ferguson KM, Burd CG. PtdIns4P recognition by Vps74/GOLPH3 links PtdIns 4-kinase signaling to retrograde Golgi trafficking. The Journal of Cell Biology. 187: 967-75. PMID 20026658 DOI: 10.1083/Jcb.200909063 |
0.75 |
|
2009 |
Schmitz KR, Ferguson KM. Interaction of antibodies with ErbB receptor extracellular regions. Experimental Cell Research. 315: 659-70. PMID 18992239 DOI: 10.1016/J.Yexcr.2008.10.008 |
0.746 |
|
2008 |
Lin CC, Huoh YS, Schmitz KR, Jensen LE, Ferguson KM. Pellino proteins contain a cryptic FHA domain that mediates interaction with phosphorylated IRAK1. Structure (London, England : 1993). 16: 1806-16. PMID 19081057 DOI: 10.1016/J.Str.2008.09.011 |
0.774 |
|
2008 |
Ferguson KM. Structure-based view of epidermal growth factor receptor regulation. Annual Review of Biophysics. 37: 353-73. PMID 18573086 DOI: 10.1146/Annurev.Biophys.37.032807.125829 |
0.562 |
|
2008 |
Schmitz KR, Liu J, Li S, Setty TG, Wood CS, Burd CG, Ferguson KM. Golgi localization of glycosyltransferases requires a Vps74p oligomer. Developmental Cell. 14: 523-34. PMID 18410729 DOI: 10.1016/J.Devcel.2008.02.016 |
0.721 |
|
2008 |
Schmiedel J, Blaukat A, Li S, Knöchel T, Ferguson KM. Matuzumab binding to EGFR prevents the conformational rearrangement required for dimerization. Cancer Cell. 13: 365-73. PMID 18394559 DOI: 10.1016/J.Ccr.2008.02.019 |
0.617 |
|
2008 |
Li S, Kussie P, Ferguson KM. Structural basis for EGF receptor inhibition by the therapeutic antibody IMC-11F8. Structure (London, England : 1993). 16: 216-27. PMID 18275813 DOI: 10.1016/J.Str.2007.11.009 |
0.492 |
|
2007 |
Lemmon MA, Ferguson KM. A new twist in the transmembrane signaling tool-kit. Cell. 130: 213-5. PMID 17662934 DOI: 10.1016/J.Cell.2007.07.006 |
0.469 |
|
2005 |
Bouyain S, Longo PA, Li S, Ferguson KM, Leahy DJ. The extracellular region of ErbB4 adopts a tethered conformation in the absence of ligand. Proceedings of the National Academy of Sciences of the United States of America. 102: 15024-9. PMID 16203964 DOI: 10.1073/Pnas.0507591102 |
0.542 |
|
2005 |
Dawson JP, Berger MB, Lin CC, Schlessinger J, Lemmon MA, Ferguson KM. Epidermal growth factor receptor dimerization and activation require ligand-induced conformational changes in the dimer interface. Molecular and Cellular Biology. 25: 7734-42. PMID 16107719 DOI: 10.1128/Mcb.25.17.7734-7742.2005 |
0.537 |
|
2005 |
Li S, Schmitz KR, Jeffrey PD, Wiltzius JJ, Kussie P, Ferguson KM. Structural basis for inhibition of the epidermal growth factor receptor by cetuximab. Cancer Cell. 7: 301-11. PMID 15837620 DOI: 10.1016/J.Ccr.2005.03.003 |
0.8 |
|
2004 |
Ferguson KM. Active and inactive conformations of the epidermal growth factor receptor Biochemical Society Transactions. 32: 742-745. PMID 15494003 DOI: 10.1042/Bst0320742 |
0.542 |
|
2003 |
Burgess AW, Cho HS, Eigenbrot C, Ferguson KM, Garrett TP, Leahy DJ, Lemmon MA, Sliwkowski MX, Ward CW, Yokoyama S. An open-and-shut case? Recent insights into the activation of EGF/ErbB receptors. Molecular Cell. 12: 541-52. PMID 14527402 DOI: 10.1016/S1097-2765(03)00350-2 |
0.511 |
|
2003 |
Ferguson KM, Berger MB, Mendrola JM, Cho HS, Leahy DJ, Lemmon MA. EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization. Molecular Cell. 11: 507-17. PMID 12620237 DOI: 10.1016/S1097-2765(03)00047-9 |
0.511 |
|
2002 |
Lemmon MA, Ferguson KM, Abrams CS. Pleckstrin homology domains and the cytoskeleton. Febs Letters. 513: 71-6. PMID 11911883 DOI: 10.1016/S0014-5793(01)03243-4 |
0.51 |
|
2001 |
Lemmon MA, Ferguson KM. Molecular determinants in pleckstrin homology domains that allow specific recognition of phosphoinositides Biochemical Society Transactions. 29: 377-384. PMID 11497993 DOI: 10.1042/Bst0290377 |
0.498 |
|
2000 |
Ferguson KM, Kavran JM, Sankaran VG, Fournier E, Isakoff SJ, Skolnik EY, Lemmon MA. Structural basis for discrimination of 3-phosphoinositides by pleckstrin homology domains. Molecular Cell. 6: 373-84. PMID 10983984 DOI: 10.1016/S1097-2765(00)00037-X |
0.473 |
|
2000 |
Ferguson KM, Darling PJ, Mohan MJ, Macatee TL, Lemmon MA. Extracellular domains drive homo- but not hetero-dimerization of erbB receptors. The Embo Journal. 19: 4632-43. PMID 10970856 DOI: 10.1093/Emboj/19.17.4632 |
0.529 |
|
2000 |
Lemmon MA, Ferguson KM. Signal-dependent membrane targeting by pleckstrin homology (PH) domains Biochemical Journal. 350: 1-18. PMID 10926821 DOI: 10.1042/0264-6021:3500001 |
0.379 |
|
2000 |
LEMMON MA, FERGUSON KM. Signal-dependent membrane targeting by pleckstrin homology (PH) domains Biochemical Journal. 350: 1-18. DOI: 10.1042/Bj3500001 |
0.479 |
|
1998 |
Isakoff SJ, Cardozo T, Andreev J, Li Z, Ferguson KM, Abagyan R, Lemmon MA, Aronheim A, Skolnik EY. Identification and analysis of PH domain-containing targets of phosphatidylinositol 3-kinase using a novel in vivo assay in yeast. The Embo Journal. 17: 5374-87. PMID 9736615 DOI: 10.1093/Emboj/17.18.5374 |
0.473 |
|
1998 |
Lemmon MA, Ferguson KM. Pleckstrin homology domains. Current Topics in Microbiology and Immunology. 228: 39-74. PMID 9401202 DOI: 10.1007/978-3-642-80481-6_3 |
0.478 |
|
1996 |
Lemmon MA, Ferguson KM, Schlessinger J. PH domains: diverse sequences with a common fold recruit signaling molecules to the cell surface. Cell. 85: 621-4. PMID 8646770 DOI: 10.1016/S0092-8674(00)81022-3 |
0.499 |
|
1995 |
Ferguson KM, Lemmon MA, Schlessinger J, Sigler PB. Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain. Cell. 83: 1037-46. PMID 8521504 DOI: 10.1016/0092-8674(95)90219-8 |
0.662 |
|
1995 |
Ferguson KM, Lemmon MA, Sigler PB, Schlessinger J. Scratching the surface with the PH domain. Nature Structural Biology. 2: 715-8. PMID 7552736 DOI: 10.1038/Nsb0995-715 |
0.611 |
|
1995 |
Lemmon MA, Ferguson KM, O'Brien R, Sigler PB, Schlessinger J. Specific and high-affinity binding of inositol phosphates to an isolated pleckstrin homology domain. Proceedings of the National Academy of Sciences of the United States of America. 92: 10472-6. PMID 7479822 DOI: 10.1073/Pnas.92.23.10472 |
0.665 |
|
1994 |
Ferguson KM, Lemmon MA, Schlessinger J, Sigler PB. Crystal structure at 2.2 A resolution of the pleckstrin homology domain from human dynamin. Cell. 79: 199-209. PMID 7954789 DOI: 10.1016/0092-8674(94)90190-2 |
0.612 |
|
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