Year |
Citation |
Score |
2021 |
Agarwal NK, Kim CH, Kunkalla K, Vaghefi A, Sanchez S, Manuel S, Bilbao D, Vega F, Landgraf R. Smoothened (SMO) regulates insulin-like growth factor 1 receptor (IGF1R) levels and protein kinase B (AKT) localization and signaling. Laboratory Investigation; a Journal of Technical Methods and Pathology. PMID 34893758 DOI: 10.1038/s41374-021-00702-6 |
0.346 |
|
2019 |
Agarwal N, Kunkalla K, Bilbao D, Landgraf R, Vega F. Novel Role of Raft-Associated Smoothened (SMO) in AKT Signal Regulation in Diffuse Large B Cell Lymphoma Blood. 134: 3972-3972. DOI: 10.1182/Blood-2019-121847 |
0.422 |
|
2018 |
Qu C, Kunkalla K, Vaghefi A, Frederiksen JK, Liu Y, Chapman JR, Blonska M, Bernal-Mizrachi L, Alderuccio JP, Lossos IS, Landgraf R, Vega F. Smoothened Stabilizes and Protects TRAF6 from Degradation: A Novel Non-Canonical Role of Smoothened with Implications in Lymphoma Biology. Cancer Letters. PMID 30165192 DOI: 10.1016/J.Canlet.2018.08.020 |
0.37 |
|
2018 |
Garri C, Howell S, Tiemann K, Tiffany A, Jalali-Yazdi F, Alba MM, Katz JE, Takahashi TT, Landgraf R, Gross ME, Roberts RW, Kani K. Identification, characterization and application of a new peptide against anterior gradient homolog 2 (AGR2). Oncotarget. 9: 27363-27379. PMID 29937991 DOI: 10.18632/Oncotarget.25221 |
0.528 |
|
2017 |
Lee H, Landgraf R, Wilson JN. Synthesis and photophysical properties of a fluorescent cyanoquinoline probe for profiling ERBB2 kinase inhibitor response. Bioorganic & Medicinal Chemistry. PMID 28974323 DOI: 10.1016/J.Bmc.2017.09.034 |
0.414 |
|
2016 |
Lee H, Liu W, Brown AS, Landgraf R, Wilson JN. Fluorescent Kinase Probes Enabling Identification and Dynamic Imaging of HER2(+) Cells. Analytical Chemistry. 88: 11310-11313. PMID 27934102 DOI: 10.1021/Acs.Analchem.6B03836 |
0.511 |
|
2016 |
Liu W, Barnette AR, Adreansky S, Landgraf R. ERBB2 overexpression establishes ERBB3 dependent hypersensitivity of breast cancer cells to Withaferin A. Molecular Cancer Therapeutics. PMID 27474152 DOI: 10.1158/1535-7163.Mct-15-0932 |
0.462 |
|
2016 |
Astudillo L, da Silva TG, Wang Z, Han X, Jin K, VanWye J, Zhu X, Weaver KL, Oashi T, Lopes PE, Orton D, Neitzel LR, Lee E, Landgraf R, Robbins DJ, et al. The small molecule IMR-1 inhibits the Notch transcriptional activation complex to suppress tumorigenesis. Cancer Research. PMID 27197169 DOI: 10.1158/0008-5472.Can-16-0061 |
0.362 |
|
2016 |
Keramisanou D, Aboalroub A, Zhang Z, Liu W, Marshall D, Diviney A, Larsen RW, Landgraf R, Gelis I. Molecular Mechanism of Protein Kinase Recognition and Sorting by the Hsp90 Kinome-Specific Cochaperone Cdc37. Molecular Cell. 62: 260-271. PMID 27105117 DOI: 10.1016/J.Molcel.2016.04.005 |
0.43 |
|
2016 |
Braley A, Kwak T, Jules J, Harja E, Landgraf R, Hudson BI. Regulation of RAGE ectodomain shedding and its role in cell function. The Journal of Biological Chemistry. PMID 27022018 DOI: 10.1074/Jbc.M115.702399 |
0.433 |
|
2015 |
Wilson JN, Liu W, Brown AS, Landgraf R. Binding-induced, turn-on fluorescence of the EGFR/ERBB kinase inhibitor, lapatinib. Organic & Biomolecular Chemistry. 13: 5006-11. PMID 25820099 DOI: 10.1039/C5Ob00239G |
0.423 |
|
2015 |
Liu W, Landgraf R. Phosphorylated and unphosphorylated serine 13 of CDC37 stabilize distinct interactions between its client and HSP90 binding domains. Biochemistry. 54: 1493-504. PMID 25619116 DOI: 10.1021/Bi501129G |
0.44 |
|
2015 |
Lu X, Sicard R, Jiang X, Stockus JN, McNamara G, Abdulreda M, Moy VT, Landgraf R, Lossos IS. HGAL localization to cell membrane regulates B-cell receptor signaling. Blood. 125: 649-57. PMID 25381061 DOI: 10.1182/Blood-2014-04-571331 |
0.414 |
|
2014 |
Dhuguru J, Liu W, Gonzalez WG, Babinchak WM, Miksovska J, Landgraf R, Wilson JN. Emission tuning of fluorescent kinase inhibitors: conjugation length and substituent effects. The Journal of Organic Chemistry. 79: 4940-7. PMID 24784897 DOI: 10.1021/Jo500520X |
0.39 |
|
2013 |
Patel N, Barrientos A, Landgraf R. The growth factor receptor ERBB2 regulates mitochondrial activity on a signaling time scale. The Journal of Biological Chemistry. 288: 35253-65. PMID 24142693 DOI: 10.1074/Jbc.M113.478271 |
0.397 |
|
2013 |
Macdonald-Obermann JL, Adak S, Landgraf R, Piwnica-Worms D, Pike LJ. Dynamic analysis of the epidermal growth factor (EGF) receptor-ErbB2-ErbB3 protein network by luciferase fragment complementation imaging. The Journal of Biological Chemistry. 288: 30773-84. PMID 24014028 DOI: 10.1074/Jbc.M113.489534 |
0.514 |
|
2013 |
Ward TM, Iorns E, Liu X, Hoe N, Kim P, Singh S, Dean S, Jegg AM, Gallas M, Rodriguez C, Lippman M, Landgraf R, Pegram MD. Truncated p110 ERBB2 induces mammary epithelial cell migration, invasion and orthotopic xenograft formation, and is associated with loss of phosphorylated STAT5. Oncogene. 32: 2463-74. PMID 22751112 DOI: 10.1038/Onc.2012.256 |
0.382 |
|
2012 |
Jegg AM, Ward TM, Iorns E, Hoe N, Zhou J, Liu X, Singh S, Landgraf R, Pegram MD. PI3K independent activation of mTORC1 as a target in lapatinib-resistant ERBB2+ breast cancer cells. Breast Cancer Research and Treatment. 136: 683-92. PMID 23089982 DOI: 10.1007/S10549-012-2252-9 |
0.388 |
|
2012 |
Sicard R, Dhuguru J, Liu W, Patel N, Landgraf R, Wilson JN. A fluorescent reporter of ATP binding-competent receptor kinases. Bioorganic & Medicinal Chemistry Letters. 22: 5532-5. PMID 22868229 DOI: 10.1016/J.Bmcl.2012.07.034 |
0.507 |
|
2012 |
Zhang Q, Park E, Kani K, Landgraf R. Functional isolation of activated and unilaterally phosphorylated heterodimers of ERBB2 and ERBB3 as scaffolds in ligand-dependent signaling. Proceedings of the National Academy of Sciences of the United States of America. 109: 13237-42. PMID 22733765 DOI: 10.1073/Pnas.1200105109 |
0.752 |
|
2011 |
Zhang Q, Park E, Kani K, Landgraf R. Abstract C58: Heterotetramers of ERBB2 and ERBB3 generate qualitatively distinct signals from heterodimers and provide most of the neuregulin-induced phosphorylation of ERBB2 Cancer Research. 71. DOI: 10.1158/1538-7445.Fbcr11-C58 |
0.672 |
|
2011 |
Ward TM, Iorns E, Liu X, Singh S, Kim P, Jegg A, Dean S, Gallas M, Villasboas-Bisneto J, Lippman M, Landgraf R, Pegram M. Abstract 1211: Novel detection and characterization of truncated ERBB2 demonstrates potent oncogenicity of the p110 isoform in human mammary epithelial cells Cancer Research. 71: 1211-1211. DOI: 10.1158/1538-7445.Am2011-1211 |
0.351 |
|
2011 |
Patel NM, Xiang J, Warren C, Avliyakulov N, Haykinson M, Landgraf R. Abstract 1210: Activation of heterogeneous nuclear ribonucleoprotein K (HNRNPK) by ERBB2/ERBB3 Cancer Research. 71: 1210-1210. DOI: 10.1158/1538-7445.Am2011-1210 |
0.645 |
|
2010 |
Gerbin CS, Landgraf R. Geldanamycin selectively targets the nascent form of ERBB3 for degradation. Cell Stress & Chaperones. 15: 529-44. PMID 20084478 DOI: 10.1007/S12192-009-0166-1 |
0.679 |
|
2010 |
Ward T, Iorns E, Singh S, Jegg A, Gallas M, Lippman M, Landgraf R, Pegram M. Abstract P5-06-03: Truncated ERBB2 Receptors: Diagnostic and Therapeutic Targets Cancer Research. 70. DOI: 10.1158/0008-5472.Sabcs10-P5-06-03 |
0.324 |
|
2009 |
Ward T, Iorns E, Gallas M, Lippman M, Landgraf R, Pegram M. Truncated p95erbB2Isoforms Are Capable of Transforming Human Mammary Epithelial Cells. Cancer Research. 69: 3136-3136. DOI: 10.1158/0008-5472.Sabcs-09-3136 |
0.312 |
|
2008 |
Park E, Baron R, Landgraf R. Higher-order association states of cellular ERBB3 probed with photo-cross-linkable aptamers. Biochemistry. 47: 11992-2005. PMID 18942860 DOI: 10.1021/Bi8004208 |
0.674 |
|
2007 |
Landgraf R. HER2 therapy. HER2 (ERBB2): functional diversity from structurally conserved building blocks. Breast Cancer Research : Bcr. 9: 202. PMID 17274834 DOI: 10.1186/Bcr1633 |
0.453 |
|
2006 |
Warren CM, Kani K, Landgraf R. The N-terminal domains of neuregulin 1 confer signal attenuation. The Journal of Biological Chemistry. 281: 27306-16. PMID 16825199 DOI: 10.1074/Jbc.M512887200 |
0.721 |
|
2006 |
Warren CM, Landgraf R. Signaling through ERBB receptors: multiple layers of diversity and control. Cellular Signalling. 18: 923-33. PMID 16460914 DOI: 10.1016/J.Cellsig.2005.12.007 |
0.689 |
|
2005 |
Kani K, Park E, Landgraf R. The extracellular domains of ErbB3 retain high ligand binding affinity at endosome pH and in the locked conformation. Biochemistry. 44: 15842-57. PMID 16313187 DOI: 10.1021/Bi0515220 |
0.704 |
|
2005 |
Kani K, Warren CM, Kaddis CS, Loo JA, Landgraf R. Oligomers of ERBB3 have two distinct interfaces that differ in their sensitivity to disruption by heregulin. The Journal of Biological Chemistry. 280: 8238-47. PMID 15611073 DOI: 10.1074/Jbc.M410944200 |
0.73 |
|
2003 |
Chen CH, Chernis GA, Hoang VQ, Landgraf R. Inhibition of heregulin signaling by an aptamer that preferentially binds to the oligomeric form of human epidermal growth factor receptor-3. Proceedings of the National Academy of Sciences of the United States of America. 100: 9226-31. PMID 12874383 DOI: 10.1073/Pnas.1332660100 |
0.51 |
|
2001 |
Singer E, Landgraf R, Horan T, Slamon D, Eisenberg D. Identification of a heregulin binding site in HER3 extracellular domain. The Journal of Biological Chemistry. 276: 44266-74. PMID 11555649 DOI: 10.1074/Jbc.M105428200 |
0.436 |
|
2000 |
Landgraf R, Eisenberg D. Heregulin reverses the oligomerization of HER3. Biochemistry. 39: 8503-11. PMID 10913256 DOI: 10.1021/Bi000953+ |
0.407 |
|
2000 |
Atienza JM, Suh M, Xenarios I, Landgraf R, Colicelli J. Human ERK1 induces filamentous growth and cell wall remodeling pathways in Saccharomyces cerevisiae. The Journal of Biological Chemistry. 275: 20638-46. PMID 10787425 DOI: 10.1074/Jbc.M910024199 |
0.382 |
|
2000 |
Landgraf R, Fischer D, Eisenberg D. Analysis of heregulin symmetry by weighted evolutionary tracing. Protein Engineering. 12: 943-51. PMID 10585499 DOI: 10.1093/Protein/12.11.943 |
0.378 |
|
1998 |
Landgraf R, Pegram M, Slamon DJ, Eisenberg D. Cytotoxicity and specificity of directed toxins composed of diphtheria toxin and the EGF-like domain of heregulin beta1. Biochemistry. 37: 3220-8. PMID 9485477 DOI: 10.1021/Bi972326Z |
0.499 |
|
1994 |
Landgraf R, Chen CH, Sigman DS. Oligonucleotide-directed nucleic acid scission by micrococcal nuclease. Biochemistry. 33: 10607-15. PMID 8075060 DOI: 10.1021/Bi00201A006 |
0.308 |
|
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