Publications

Lipper CH, Gabriel K, Seegar TC, Dürr KL, Tomlinson MG, Blacklow SC. Crystal structure of the Tspan15 LEL domain reveals a conserved ADAM10 binding site. Structure 2022 Feb 3;30(2):206-214. doi: 10.1016/j.str.2021.10.007

Vemulapalli V, Donovan KA, Seegar TC, Rogers JM, Bae M, Lumpkin RJ, Cao R, Henke MT, Ray SS, Fischer ES, Cuny GD, Blacklow SC. Targeted Degradation of the Oncogenic Phosphatase SHP2. ACS Chem Bio. 2021 Aug 19;60(34):2593-2609. doi: 10.1021/acs.biochem.1c00377.

Vemulapalli V, Chylek LA, Erickson A, Pfeiffer A, Gabriel K, LaRochelle J, Subramanian K, Cao R, Stegmaier K, Mohseni M, LaMarche MJ, Acker MG, Sorger PK, Gygi SP, Blacklow SC. Time-resolved phosphoproteomics reveals scaffolding and catalysis-responsive patterns of SHP2-dependent signaling. eLife 2021 Mar 23;10. pii: e64251 doi: 10.7554/eLife.64251.

Susa KJ, Rawson S, Kruse AC, Blacklow SC. Cryo-EM structure of the B cell co-receptor CD19 bound to the tetraspanin CD81. Science. 2021 Jan 15;371(6526):300-305. doi: 10.1126/science.abd9836.

Susa KJ, Seegar TCM, Blacklow SC, Kruse AC. A dynamic interaction between CD19 and the tetraspanin CD81 controls B cell co-receptor trafficking. Elife. 2020 Apr 27;9. pii: e52337. doi: 10.7554/eLife.52337.

Rogers JM, Guo B, Egan ED, Aster JC, Adelman K, Blacklow SC. MAML1-dependent Notch responsive genes exhibit differing co-factor requirements for transcriptional activation. Mol Cell Biol. 2020 Mar 16. pii: MCB.00014-20. doi: 10.1128/MCB.00014-20.

Rome KS, Stein SJ, Kurachi M, Petrovic J, Schwartz GW, Mack EA, Uljon S, Wu WW, DeHart AG, McClory SE, Xu L, Gimotty PA, Blacklow SC, Faryabi RB, Wherry EJ, Jordan MS, Pear WS.Trib1 regulates T cell differentiation during chronic infection by restraining the effector program. J Exp Med. 2020 May 4;217(5). pii: e20190888. doi: 10.1084/jem.20190888.

Adhikari AA, Seegar TCM, Ficarro SB, McCurry MD, Ramachandran D, Yao L, Chaudhari SN, Ndousse-Fetter S, Banks AS, Marto JA, Blacklow SC, Devlin AS. Development of a covalent inhibitor of gut bacterial bile salt hydrolases. Nat Chem Biol. 2020 Mar;16(3):318-326. doi: 10.1038/s41589-020-0467-3.

Jarrett SM, Seegar TCM, Andrews M, Adelmant G, Marto JA, Aster JC, Blacklow SC. Extension of the Notch intracellular domain ankyrin repeat stack by NRARP promotes feedback inhibition of Notch signaling. Sci Signal. 2019 Nov 5;12(606). pii: eaay2369. doi: 10.1126/scisignal.aay2369.

Seegar TC, Blacklow SC. Domain integration of ADAM family proteins: Emerging themes from structural studies. Exp Biol Med (Maywood). 2019 Dec;244(17):1510-1519. doi: 10.1177/1535370219865901.

Drabek AA, Loparo JJ, Blacklow SC. A Flow-Extension Tethered Particle Motion Assay for Single-Molecule Proteolysis. Biochemistry. 2019 May 21;58(20):2509-2518. doi: 10.1021/acs.biochem.9b00106.

Rogers JM, Waters CT, Seegar TCM, Jarrett SM, Hallworth AN, Blacklow SC, Bulyk ML. Bispecific Forkhead Transcription Factor FoxN3 Recognizes Two Distinct Motifs with Different DNA Shapes. Mol Cell. 2019 Apr 18;74(2):245-253.e6. doi: 10.1016/j.molcel.2019.01.019.

Petrovic J, Zhou Y, Fasolino M, Goldman N, Schwartz GW, Mumbach MR, Nguyen SC, Rome KS, Sela Y, Zapataro Z, Blacklow SC, Kruhlak MJ, Shi J, Aster JC, Joyce EF, Little SC, Vahedi G, Pear WS, Faryabi RB. Oncogenic Notch Promotes Long-Range Regulatory Interactions within Hyperconnected 3D Cliques. Mol Cell. 2019 Mar 21;73(6):1174-1190.e12. doi: 10.1016/j.molcel.2019.01.006.

LaRochelle JR, Fodor M, Vemulapalli V, Mohseni M, Wang P, Stams T, LaMarche MJ, Chopra R, Acker MG, Blacklow SC. Structural reorganization of SHP2 by oncogenic mutations and implications for oncoprotein resistance to allosteric inhibition. Nat Commun. 2018 Oct 30;9(1):4508. doi: 10.1038/s41467-018-06823-9.

Tveriakhina L, Schuster-Gossler K, Jarrett SM, Andrawes MB, Rohrbach M, Blacklow SC, Gossler A. The ectodomains determine ligand function in vivo and selectivity of DLL1 and DLL4 toward NOTCH1 and NOTCH2 in vitro. Elife. 2018 Oct 5;7. pii: e40045. doi: 10.7554/eLife.40045.

Wang J, Erazo T, Ferguson FM, Buckley DL, Gomez N, Muñoz-Guardiola P, Diéguez-Martínez N, Deng X, Hao M, Massefski W, Fedorov O, Offei-Addo NK, Park PM, Dai L, DiBona A, Becht K, Kim ND, McKeown MR, Roberts JM, Zhang J, Sim T, Alessi DR, Bradner JE, Lizcano JM, Blacklow SC, Qi J, Xu X, Gray NS. Structural and Atropisomeric Factors Governing the Selectivity of Pyrimido-benzodiazipinones as Inhibitors of Kinases and Bromodomains. ACS Chem Biol. 2018 Sep 21;13(9):2438-2448. doi: 10.1021/acschembio.7b00638.

Lovendahl KN, Blacklow SC, Gordon WR. The Molecular Mechanism of Notch Activation. Adv Exp Med Biol. 2018;1066:47-58. doi: 10.1007/978-3-319-89512-3_3.

Fodor M, Price E, Wang P, Lu H, Argintaru A, Chen Z, Glick M, Hao HX, Kato M, Koenig R, LaRochelle JR, Liu G, McNeill E, Majumdar D, Nishiguchi GA, Perez LB, Paris G, Quinn CM, Ramsey T, Sendzik M, Shultz MD, Williams SL, Stams T, Blacklow SC, Acker MG, LaMarche MJ. Dual Allosteric Inhibition of SHP2 Phosphatase. ACS Chem Biol. 2018;13(3):647-656. doi: 10.1021/acschembio.7b00980. PMID: 29304282.

LaRochelle JR, Fodor M, Ellegast JM, Liu X, Vemulapalli V, Mohseni M, Stams T, Buhrlage SJ, Stegmaier K, LaMarche MJ, Acker MG, Blacklow SC. Identification of an allosteric benzothiazolopyrimidone inhibitor of the oncogenic protein tyrosine phosphatase SHP2. Bioorg Med Chem. 2017;25(24):6479-6485. doi: 10.1016/j.bmc.2017.10.025. PMID: 29089257.

Seegar, TCM, Killingsworth, LB, Saha, N, Meyer, PA, Patra, D, Zimmerman, B, Janes, PW, Rubinstein, E, Nikolov, DB, Skiniotis, G, Kruse, AC, and Blacklow SC. Structural Basis for Regulated Proteolysis by the α-Secretase ADAM10. Cell 2017;171:1638-1648.e7. PMID: 29224781. PMCID: PMC5773094.

Pajcini KV, Xu L, Shao L, Petrovic J, Palasiewicz K, Ohtani Y, Bailis W, Lee C, Wertheim GB, Mani R, Musuthamy N, Li Y, Meijerink JPP, Blacklow SC, Faryabi RB, Cherry S, Pear WS. MAFB enhances oncogenic Notch signaling in T cell acute lymphoblastic leukemia. Sci Signal. 2017;10(505). pii: eaam6846. doi: 10.1126/scisignal.aam6846. PMID: 29138297. PMCID: PMC5885022.

Sajed DP, Faquin WC, Carey C, Severson EA, Afrogheh AH, Johnson CA, Blacklow SC, Chau NG, Lin DT, Krane JF, Jo VY, Garcia JJ, Sholl LM, Aster JC. Diffuse Staining for Activated NOTCH1 Correlates With NOTCH1 Mutation Status and Is Associated With Worse Outcome in Adenoid Cystic Carcinoma. Am J Surg Pathol. 2017 Nov;41(11):1473-1482. doi: 10.1097/PAS.0000000000000945. PMID: 28914715. PMCID: PMC5657508.

Ryan RJH, Petrovic J, Rausch DM, Zhou Y, Lareau CA, Kluk MJ, Christie AL, Lee WY, Tarjan DR, Guo B, Donohue LKH, Gillespie SM, Nardi V, Hochberg EP, Blacklow SC, Weinstock DM, Faryabi RB, Bernstein BE, Aster JC, Pear WS. A B Cell Regulome Links Notch to Downstream Oncogenic Pathways in Small B Cell Lymphomas. Cell Rep. 2017;21(3):784-797. doi: 10.1016/j.celrep.2017.09.066. PMID: 29045844. PMCID: PMC5687286.

Severson E, Arnett K, Wang H, Zang C, Liu H, Pear WS, Liu X, Blacklow SC*, and Aster JC*. Genome-wide identification and characterization of Notch transcription complex-binding sequence paired sites in leukemia cells. Science Signaling 2017;10:477. doi: 10.1126/scisignal.aag1598. PMID: 28465412.

*Co-corresponding authors.

McMillan BJ, Tibbe C, Drabek AA, Seegar TCM, Blacklow SC*, and Klein T*. Structural Basis for Regulation of ESCRT-III Complexes by Lgd. Cell Rep. 2017 May 30;19(9):1750-1757. doi: 10.1016/j.celrep.2017.05.026. PMID: 28564595. PMCID: PMC5528166.

*Co-corresponding authors.

Choi SH, Severson E, Pear WS, Liu XS, Aster JC*, Blacklow SC*. The common oncogenomic program of NOTCH1 and NOTCH3 signaling in T-cell acute lymphoblastic leukemia. PLoS One 2017;12(10):e0185762. doi: 10.1371/journal.pone.0185762. PMID: 29023469. PMC5638296.

McMillan BJ, Zimmerman B, Egan ED, Lofgren, M, Xu X, Hesser A, and Blacklow SC. Structure of human POFUT1, its requirement in ligand-independent oncogenic notch signaling, and functional effects of Dowling-Degos mutations. Glycobiology, 2017, 27(8):777-786. doi: 10.1093/glycob/cwx020. PMID: 28334865. PMC5881682.

Durzynska I, Xu X, Adelmant G, Ficarro SB, Marto JA, Sliz P, Uljon S, and Blacklow SC. STK40 Is a Pseudokinase that Binds the E3 Ubiquitin Ligase COP1. Structure 2017:25, 287-294. doi: 10.1016/j.str.2016.12.008. PMID: 28089446. PMCID: PMC5299031.

Zimmerman B, Kelly B, McMillan, BJ, Seegar, TCM, Dror, RO, Kruse, AC, and Blacklow SC. Crystal Structure of a Full-Length Human Tetraspanin Reveals a Cholesterol-Binding Pocket. Cell 2016;167:1041-1051. doi: 10.1016/j.cell.2016.09.056. PMCID: PMC5127602.

McMillan BJ, Tibbe C, Jeon H, Drabek AA, Klein T and Blacklow SC. Electrostatic Interactions between Elongated Monomers Drive Filamentation of Drosophila Shrub, a Metazoan ESCRT-III Protein. Cell Reports 2016;16(5):1211-1217. doi: 10.1016/j.celrep.2016.06.093. PMCID: PMC4985235.

Bernasconi-Elias P, Hu T, Jenkins D, Firestone B, Gans S, Kurth E, Capodieci P, Deplazes-Lauber J, Petropoulos K, Thiel P, Ponsel D, Hee Choi S, LeMotte P, London A, Goetcshkes M, Nolin E, Jones MD, Slocum K, Kluk MJ, Weinstock DM, Christodoulou A, Weinberg O, Jaehrling J, Ettenberg SA, Buckler A, Blacklow SC, Aster JC, Fryer CJ. Characterization of activating mutations of NOTCH3 in T-cell acute lymphoblastic leukemia and anti-leukemic activity of NOTCH3 inhibitory antibodies. Oncogene. 2016 May 9. doi: 10.1038/onc.2016.133. PMID: 27157619. PMCID: PMC5102827.

LaRochelle JR, Fodor M, Xu X, Durzynska I, Fan L, Stams T, Chan HM, LaMarche MJ, Chopra R, Wang P, Fortin PD, Acker MG, Blacklow SC. Structural and Functional Consequences of Three Cancer-Associated Mutations of the Oncogenic Phosphatase SHP2. Biochemistry 2016;55(15):2269-2277. doi: 10.1021/acs.biochem.5b01287. PMID: 27030275. PMCID: PMC4900891.

Uljon S, Xu X, Durzynska I, Stein S, Adelmant G, Marto JA, Pear WS, Blacklow SC. Structural Basis for Substrate Selectivity of the E3 Ligase COP1. Structure. 2016;24(5):687-96. doi: 10.1016/j.str.2016.03.002. PMID: 27041596. PMCID: PMC4856590

Meyer PA, Socias S, Key J, Ransey E, Tjon EC, Buschiazzo A, Lei M, Botka C, Withrow J, Neau D, Rajashankar K, Anderson KS, Baxter RH, Blacklow SC, Boggon TJ, Bonvin AM, Borek D, Brett TJ, Caflisch A, Chang CI, Chazin WJ, Corbett KD, Cosgrove MS, Crosson S, Dhe-Paganon S, Di Cera E, Drennan CL, Eck MJ, Eichman BF, Fan QR, Ferré-D'Amaré AR, Christopher Fromme J, Garcia KC, Gaudet R, Gong P, Harrison SC, Heldwein EE, Jia Z, Keenan RJ, Kruse AC, Kvansakul M, McLellan JS, Modis Y, Nam Y, Otwinowski Z, Pai EF, Pereira PJ, Petosa C, Raman CS, Rapoport TA, Roll-Mecak A, Rosen MK, Rudenko G, Schlessinger J, Schwartz TU, Shamoo Y, Sondermann H, Tao YJ, Tolia NH, Tsodikov OV, Westover KD, Wu H, Foster I, Fraser JS, Maia FR, Gonen T, Kirchhausen T, Diederichs K, Crosas M, Sliz P. Data publication with the structural biology data grid supports live analysis. Nat Commun. 2016;7:10882. doi: 10.1038/ncomms10882. PMID: 26947396. PMCID: PMC4786681.

Knoechel B, Bhatt A, Pan L, Pedamallu CS, Severson E, Gutierrez A, Dorfman DM, Kuo FC, Kluk M, Kung AL, Zweidler-McKay P, Meyerson M, Blacklow SC, DeAngelo DJ, Aster JC. Complete hematologic response of early T-cell progenitor acute lymphoblastic leukemia to the γ-secretase inhibitor BMS-906024: genetic and epigenetic findings in an outlier case. Cold Spring Harb Mol Case Stud. 2015;1(1):a000539. doi: 10.1101/mcs.a000539. PMID: 27148573. PMCID: PMC4850884.

X. Xu, S. H. Choi, T. Hu, K. Tiyanont, R. Habets, A. J. Groot, M. Vooijs, J. C. Aster, R. Chopra, C. Fryer, and S. C. Blacklow, “Insights into Autoregulation of Notch3 from Structural and Functional Studies of Its Negative Regulatory Region.,” Structure (London, England : 1993), vol. 23, no. 7, pp. 1227–1235, Jul. 2015.

W. R. Gordon, B. Zimmerman, L. He, L. J. Miles, J. Huang, K. Tiyanont, D. G. McArthur, J. C. Aster, N. Perrimon, J. J. Loparo, and S. C. Blacklow, “Mechanical Allostery: Evidence for a Force Requirement in the Proteolytic Activation of Notch.,” Dev Cell, vol. 33, no. 6, pp. 729–736, Jun. 2015.

R. A. J. Habets, A. J. Groot, S. Yahyanejad, K. Tiyanont, S. C. Blacklow, and M. Vooijs, “Human NOTCH2 Is Resistant to Ligand-independent Activation by Metalloprotease Adam17.,” J Biol Chem, vol. 290, no. 23, pp. 14705–14716, Jun. 2015.

B. J. McMillan, B. Schnute, N. Ohlenhard, B. Zimmerman, L. Miles, N. Beglova, T. Klein, and S. C. Blacklow, “A tail of two sites: a bipartite mechanism for recognition of notch ligands by mind bomb e3 ligases.,” Mol Cell, vol. 57, no. 5, pp. 912–924, Mar. 2015.

Y. Yashiro-Ohtani, H. Wang, C. Zang, K. L. Arnett, W. Bailis, Y. Ho, B. Knoechel, C. Lanauze, L. Louis, K. S. Forsyth, S. Chen, Y. Chung, J. Schug, G. A. Blobel, S. A. Liebhaber, B. E. Bernstein, S. C. Blacklow, X. S. Liu, J. C. Aster, and W. S. Pear, “Long-range enhancer activity determines Myc sensitivity to Notch inhibitors in T cell leukemia.,” Proceedings of the National Academy of Sciences, vol. 111, no. 46, pp. E4946–53, Nov. 2014.

M. R. McKeown, D. L. Shaw, H. Fu, S. Liu, X. Xu, J. J. Marineau, Y. Huang, X. Zhang, D. L. Buckley, A. Kadam, Z. Zhang, S. C. Blacklow, J. Qi, W. Zhang, and J. E. Bradner, “Biased multicomponent reactions to develop novel bromodomain inhibitors.,” J Med Chem, vol. 57, no. 21, pp. 9019–9027, Nov. 2014.

K. L. Arnett and S. C. Blacklow, “Analyzing the nuclear complexes of Notch signaling by electrophoretic mobility shift assay.,” Methods Mol Biol, vol. 1187, pp. 231–245, 2014.

H. Wang, C. Zang, L. Taing, K. L. Arnett, Y. J. Wong, W. S. Pear, S. C. Blacklow, X. S. Liu, and J. C. Aster, “NOTCH1-RBPJ complexes drive target gene expression through dynamic interactions with superenhancers.,” Proceedings of the National Academy of Sciences, vol. 111, no. 2, pp. 705–710, Jan. 2014.

S. C. Blacklow, “Refining a Jagged edge.,” Structure (London, England : 1993), vol. 21, no. 12, pp. 2100–2101, Dec. 2013.

K. Tiyanont, T. E. Wales, C. W. Siebel, J. R. Engen, and S. C. Blacklow, “Insights into Notch3 Activation and Inhibition Mediated by Antibodies Directed against Its Negative Regulatory Region.,” J Mol Biol, vol. 425, no. 17, pp. 3192–3204, Sep. 2013.

M. B. Andrawes, X. Xu, H. Liu, S. B. Ficarro, J. A. Marto, J. C. Aster, and S. C. Blacklow, “Intrinsic Selectivity of Notch 1 for Delta-like 4 Over Delta-like 1.,” J Biol Chem, vol. 288, no. 35, pp. 25477–25489, Aug. 2013.

G. Roti, A. Carlton, K. N. Ross, M. Markstein, K. Pajcini, A. H. Su, N. Perrimon, W. S. Pear, A. L. Kung, S. C. Blacklow, J. C. Aster, and K. Stegmaier, “Complementary genomic screens identify SERCA as a therapeutic target in NOTCH1 mutated cancer.,” Cancer Cell, vol. 23, no. 3, pp. 390–405, Mar. 2013.

J. C. Aster and S. C. Blacklow, “Targeting the Notch pathway: twists and turns on the road to rational therapeutics.,” J Clin Oncol, vol. 30, no. 19, pp. 2418–2420, Jul. 2012.

D. J. O'Donovan, I. Stokes-Rees, Y. Nam, S. C. Blacklow, G. F. Schröder, A. T. Brunger, and P. Sliz, “A grid-enabled web service for low-resolution crystal structure refinement.,” Acta Crystallogr D Biol Crystallogr, vol. 68, no. 3, pp. 261–267, Mar. 2012.

S. H. Choi, T. E. Wales, Y. Nam, D. J. O'Donovan, P. Sliz, J. R. Engen, and S. C. Blacklow, “Conformational locking upon cooperative assembly of notch transcription complexes.,” Structure (London, England : 1993), vol. 20, no. 2, pp. 340–349, Feb. 2012.

K. Germar, M. Dose, T. Konstantinou, J. Zhang, H. Wang, C. Lobry, K. L. Arnett, S. C. Blacklow, I. Aifantis, J. C. Aster, and F. Gounari, “T-cell factor 1 is a gatekeeper for T-cell specification in response to Notch signaling.,” Proceedings of the National Academy of Sciences, Nov. 2011.

N. J. Wang, Z. Sanborn, K. L. Arnett, L. J. Bayston, W. Liao, C. M. Proby, I. M. Leigh, E. A. Collisson, P. B. Gordon, L. Jakkula, S. Pennypacker, Y. Zou, M. Sharma, J. P. North, S. S. Vemula, T. M. Mauro, I. M. Neuhaus, P. E. Leboit, J. S. Hur, K. Park, N. Huh, P.-Y. Kwok, S. T. Arron, P. P. Massion, A. E. Bale, D. Haussler, J. E. Cleaver, J. W. Gray, P. T. Spellman, A. P. South, J. C. Aster, S. C. Blacklow, and R. J. Cho, “Loss-of-function mutations in Notch receptors in cutaneous and lung squamous cell carcinoma.,” Proceedings of the National Academy of Sciences, vol. 108, no. 43, pp. 17761–17766, Oct. 2011.

B. Zhao, J. Zou, H. Wang, E. Johannsen, C.-W. Peng, J. Quackenbush, J. C. Mar, C. C. Morton, M. L. Freedman, S. C. Blacklow, J. C. Aster, B. E. Bernstein, and E. Kieff, “Epstein-Barr virus exploits intrinsic B-lymphocyte transcription programs to achieve immortal cell growth.,” Proceedings of the National Academy of Sciences, vol. 108, no. 36, pp. 14902–14907, Sep. 2011.

H. Wang, J. Zou, B. Zhao, E. Johannsen, T. Ashworth, H. Wong, W. S. Pear, J. Schug, S. C. Blacklow, K. L. Arnett, B. E. Bernstein, E. Kieff, and J. C. Aster, “Genome-wide analysis reveals conserved and divergent features of Notch1/RBPJ binding in human and murine T-lymphoblastic leukemia cells.,” Proceedings of the National Academy of Sciences, Jul. 2011.

M. A. Calderwood, S. Lee, A. M. Holthaus, S. C. Blacklow, E. Kieff, and E. Johannsen, “Epstein-Barr virus nuclear protein 3C binds to the N-terminal (NTD) and beta trefoil domains (BTD) of RBP/CSL; only the NTD interaction is essential for lymphoblastoid cell growth.,” Virology, vol. 414, no. 1, pp. 19–25, May 2011.

K. Tiyanont, T. E. Wales, M. Aste-Amezaga, J. C. Aster, J. R. Engen, and S. C. Blacklow, “Evidence for increased exposure of the Notch1 metalloprotease cleavage site upon conversion to an activated conformation.,” Structure (London, England : 1993), vol. 19, no. 4, pp. 546–554, Apr. 2011.

J. C. Aster, S. C. Blacklow, and W. S. Pear, “Notch signalling in T-cell lymphoblastic leukaemia/lymphoma and other haematological malignancies.,” J. Pathol., vol. 223, no. 2, pp. 262–273, Jan. 2011.

J. C. Aster, N. Bodnar, L. Xu, F. Karnell, J. M. Milholland, I. Maillard, G. Histen, Y. Nam, S. C. Blacklow, and W. S. Pear, “Notch ankyrin repeat domain variation influences leukemogenesis and myc transactivation.,” PLoS ONE, vol. 6, no. 10, p. e25645, 2011.

T. D. Ashworth, W. S. Pear, M. Y. Chiang, S. C. Blacklow, J. Mastio, L. Xu, M. Kelliher, P. Kastner, S. Chan, and J. C. Aster, “Deletion-based mechanisms of Notch1 activation in T-ALL: key roles for RAG recombinase and a conserved internal translational start site in Notch1.,” Blood, vol. 116, no. 25, pp. 5455–5464, Dec. 2010.

K. Keeshan, W. Bailis, P. H. Dedhia, M. E. Vega, O. Shestova, L. Xu, K. Toscano, S. N. Uljon, S. C. Blacklow, and W. S. Pear, “Transformation by Tribbles homolog 2 (Trib2) requires both the Trib2 kinase domain and COP1 binding.,” Blood, vol. 116, no. 23, pp. 4948–4957, Dec. 2010.

H. Liu, A. W. S. Chi, K. L. Arnett, M. Y. Chiang, L. Xu, O. Shestova, H. Wang, Y.-M. Li, A. Bhandoola, J. C. Aster, S. C. Blacklow, and W. S. Pear, “Notch dimerization is required for leukemogenesis and T-cell development.,” Genes Dev, vol. 24, no. 21, pp. 2395–2407, Nov. 2010.

K. L. Arnett, M. Hass, D. G. McArthur, M. X. G. Ilagan, J. C. Aster, R. Kopan, and S. C. Blacklow, “Structural and mechanistic insights into cooperative assembly of dimeric Notch transcription complexes.,” Nat Struct Mol Biol, vol. 17, no. 11, pp. 1312–1317, Nov. 2010.

P. H. Dedhia, K. Keeshan, S. Uljon, L. Xu, M. E. Vega, O. Shestova, M. Zaks-Zilberman, C. Romany, S. C. Blacklow, and W. S. Pear, “Differential ability of Tribbles family members to promote degradation of C/EBPalpha and induce acute myelogenous leukemia.,” Blood, vol. 116, no. 8, pp. 1321–1328, Aug. 2010.

R. A. Kovall and S. C. Blacklow, “Mechanistic insights into Notch receptor signaling from structural and biochemical studies.,” Curr Top Dev Biol, vol. 92, pp. 31–71, 2010.

M. Aste-Amezaga, N. Zhang, J. E. Lineberger, B. A. Arnold, T. J. Toner, M. Gu, L. Huang, S. Vitelli, K. T. Vo, P. Haytko, J. Z. Zhao, F. Baleydier, S. L'Heureux, H. Wang, W. R. Gordon, E. Thoryk, M. B. Andrawes, K. Tiyanont, K. Stegmaier, G. Roti, K. N. Ross, L. L. Franlin, H. Wang, F. Wang, M. Chastain, A. J. Bett, L. P. Audoly, J. C. Aster, S. C. Blacklow, and H. E. Huber, “Characterization of Notch1 antibodies that inhibit signaling of both normal and mutated Notch1 receptors.,” PLoS ONE, vol. 5, no. 2, p. e9094, 2010.

C. Del Bianco, A. Vedenko, S. H. Choi, M. F. Berger, L. Shokri, M. L. Bulyk, and S. C. Blacklow, “Notch and MAML-1 complexation do not detectably alter the DNA binding specificity of the transcription factor CSL.,” PLoS ONE, vol. 5, no. 11, p. e15034, 2010

R. E. Moellering, M. Cornejo, T. N. Davis, C. Del Bianco, J. C. Aster, S. C. Blacklow, A. L. Kung, D. G. Gilliland, G. L. Verdine, and J. E. Bradner, “Direct inhibition of the NOTCH transcription factor complex.,” Nature, vol. 462, no. 7270, pp. 182–188, Nov. 2009.

Y. Yashiro-Ohtani, Y. He, T. Ohtani, M. E. Jones, O. Shestova, L. Xu, T. C. Fang, M. Y. Chiang, A. M. Intlekofer, S. C. Blacklow, Y. Zhuang, and W. S. Pear, “Pre-TCR signaling inactivates Notch1 transcription by antagonizing E2A.,” Genes Dev, vol. 23, no. 14, pp. 1665–1676, Jul. 2009.

W. R. Gordon, M. Roy, D. Vardar-Ulu, M. Garfinkel, M. R. Mansour, J. C. Aster, and S. C. Blacklow, “Structure of the Notch1-negative regulatory region: implications for normal activation and pathogenic signaling in T-ALL.,” Blood, vol. 113, no. 18, pp. 4381–4390, Apr. 2009.

W. R. Gordon, D. Vardar-Ulu, S. L'Heureux, T. Ashworth, M. J. Malecki, C. Sanchez-Irizarry, D. G. McArthur, G. Histen, J. L. Mitchell, J. C. Aster, and S. C. Blacklow, “Effects of S1 cleavage on the structure, surface export, and signaling activity of human Notch1 and Notch2.,” PLoS ONE, vol. 4, no. 8, p. e6613, 2009.

W. R. Gordon, K. L. Arnett, and S. C. Blacklow, “The molecular logic of Notch signaling--a structural and biochemical perspective.,” J Cell Sci, vol. 121, no. 19, pp. 3109–3119, Oct. 2008.

K. Li, Y. Li, W. Wu, W. R. Gordon, D. W. Chang, M. Lu, S. Scoggin, T. Fu, L. Vien, G. Histen, J. Zheng, R. Martin-Hollister, T. Duensing, S. Singh, S. C. Blacklow, Z. Yao, J. C. Aster, and B.-B. S. Zhou, “Modulation of Notch signaling by antibodies specific for the extracellular negative regulatory region of NOTCH3.,” J Biol Chem, vol. 283, no. 12, pp. 8046–8054, Mar. 2008.

K. Estrada, C. Fisher, and S. C. Blacklow, “Unfolding of the RAP-D3 helical bundle facilitates dissociation of RAP-receptor complexes.,” Biochemistry, vol. 47, no. 6, pp. 1532–1539, Feb. 2008.

C. Del Bianco, J. C. Aster, and S. C. Blacklow, “Mutational and energetic studies of Notch 1 transcription complexes.,” J Mol Biol, vol. 376, no. 1, pp. 131–140, Feb. 2008.

J. C. Aster, W. S. Pear, and S. C. Blacklow, “Notch signaling in leukemia.,” Annu Rev Pathol, vol. 3, pp. 587–613, 2008.

S. C. Blacklow, “Versatility in ligand recognition by LDL receptor family proteins: advances and frontiers.,” Curr Opin Struct Biol, vol. 17, no. 4, pp. 419–426, Aug. 2007.

T. C. Fang, Y. Yashiro-Ohtani, C. Del Bianco, D. M. Knoblock, S. C. Blacklow, and W. S. Pear, “Notch directly regulates Gata3 expression during T helper 2 cell differentiation.,” Immunity, vol. 27, no. 1, pp. 100–110, Jul. 2007

V. Koduri and S. C. Blacklow, “Requirement for natively unstructured regions of mesoderm development candidate 2 in promoting low-density lipoprotein receptor-related protein 6 maturation.,” Biochemistry, vol. 46, no. 22, pp. 6570–6577, Jun. 2007.

W. R. Gordon, D. Vardar-Ulu, G. Histen, C. Sanchez-Irizarry, J. C. Aster, and S. C. Blacklow, “Structural basis for autoinhibition of Notch.,” Nat Struct Mol Biol, vol. 14, no. 4, pp. 295–300, Apr. 2007.

Y. Nam, P. Sliz, W. S. Pear, J. C. Aster, and S. C. Blacklow, “Cooperative assembly of higher-order Notch complexes functions as a switch to induce transcription.,” Proc Natl Acad Sci USA, vol. 104, no. 7, pp. 2103–2108, Feb. 2007.

A. P. Weng, J. M. Millholland, Y. Yashiro-Ohtani, M. L. Arcangeli, A. Lau, C. Wai, C. Del Bianco, C. G. Rodriguez, H. Sai, J. Tobias, Y. Li, M. S. Wolfe, C. Shachaf, D. Felsher, S. C. Blacklow, W. S. Pear, and J. C. Aster, “c-Myc is an important direct target of Notch1 in T-cell acute lymphoblastic leukemia/lymphoma.,” Genes Dev, vol. 20, no. 15, pp. 2096–2109, Aug. 2006.

M. Y. Chiang, M. L. Xu, G. Histen, O. Shestova, M. Roy, Y. Nam, S. C. Blacklow, D. B. Sacks, W. S. Pear, and J. C. Aster, “Identification of a conserved negative regulatory sequence that influences the leukemogenic activity of NOTCH1.,” Mol Cell Biol, vol. 26, no. 16, pp. 6261–6271, Aug. 2006.

D. Lee, J. D. Walsh, I. Mikhailenko, P. Yu, M. Migliorini, Y. Wu, S. Krueger, J. E. Curtis, B. Harris, S. Lockett, S. C. Blacklow, D. K. Strickland, and Y.-X. Wang, “RAP uses a histidine switch to regulate its interaction with LRP in the ER and Golgi.,” Mol Cell, vol. 22, no. 3, pp. 423–430, May 2006.

C. Fisher, N. Beglova, and S. C. Blacklow, “Structure of an LDLR-RAP complex reveals a general mode for ligand recognition by lipoprotein receptors.,” Mol Cell, vol. 22, no. 2, pp. 277–283, Apr. 2006.

Y. Nam, P. Sliz, L. Song, J. C. Aster, and S. C. Blacklow, “Structural basis for cooperativity in recruitment of MAML coactivators to Notch transcription complexes.,” Cell, vol. 124, no. 5, pp. 973–983, Mar. 2006.

M. J. Malecki, C. Sanchez-Irizarry, J. L. Mitchell, G. Histen, M. L. Xu, J. C. Aster, and S. C. Blacklow, “Leukemia-associated mutations within the NOTCH1 heterodimerization domain fall into at least two distinct mechanistic classes.,” Mol Cell Biol, vol. 26, no. 12, pp. 4642–4651, Jun. 2006.

C. Sanchez-Irizarry, A. C. Carpenter, A. P. Weng, W. S. Pear, J. C. Aster, and S. C. Blacklow, “Notch Subunit Heterodimerization and Prevention of Ligand-Independent Proteolytic Activation Depend, Respectively, on a Novel Domain and the LNR Repeats,” Mol Cell Biol, vol. 24, no. 21, pp. 9265–9273, Oct. 2004.

Activating mutations of NOTCH1 in human T cell acute lymphoblastic leukemia.
Weng AP, Ferrando AA, Lee W, Morris JP, Silverman LB, Sanchez-Irizarry C, Blacklow SC, Look T, and Aster JC. Science. 2004 Oct 8;306(5694):269-71.

NMR Structure of a Prototype LNR Module from Human Notch1.
Vardar D, North CL, Sanchez-Irizarry C, Aster JC, and Blacklow SC. Biochemistry 2003; 42:7061-7067.

S.C. Structural Requirements for Assembly of the CSL/Intracellular Notch1/Mastermind-like 1 Transcriptional Activation Complex.
Nam Y, Weng AP, Aster JC and Blacklow, J. Biol. Chem. 2003, 278:21232-21239.

Growth Suppression of Pre-T Acute Lymphoblastic Leukemia Cells by Inhibition of Notch Signaling.
Weng AP, Nam Y, Wolfe MS, Pear WS, Griffin JD, Blacklow SC, and Aster JC. Mol Cell Biol 2003; 23:655-664.

Notch signaling as a therapeutic target.
Nam Y, Aster JC, Blacklow SC. Curr Opin Chem Biol. 2002 Aug;6(4):501-9. Review.

MAM1, a human homologue of Drosophila Mastermind, is a transcriptional co-activator for notch receptors.
Wu L, Aster JC, Blacklow SC, Lake R, Artavanis-Tsakonas S, and Griffin JD. Nature Genetics 2000;26:484-489.

Calcium depletion dissociates and activates heterodimeric notch receptors.
Rand MD, Grimm LM, Artavanis-Tsakonas S, Patriub V, Blacklow SC, Sklar J, Aster JC. Mol Cell Biol. 2000 Mar;20(5):1825-35

Folding and structural integrity of the first LIN12 module of human Notch1 are calcium dependent.
Aster JC, Simms WB, Zavala-Ruiz Z, Patriub V, North CL, and Blacklow SC. Biochemistry 1999;38:4736-42.

Amino Acid Backbone Specificity of the Escherichia coli Translation Machinery.
Tan Z, Forster AC, Blacklow SC, Cornish VW.J Am Chem Soc. 2004;126:12752-12753.

Pure Translation Display.
Forster, AC, Cornish, V, Blacklow, SC. Analytical Biochemistry 2004; 333(2):358-64.

Programming peptidomimetic syntheses by translating genetic codes designed de novo.
Forster, A., Tan, Z., Nalam, M.N., Lin, H., Qu, H., Cornish, V.W., and Blacklow, S.C. Proc Natl Acad Sci U S A. 2003; 100(11):6353-6357.

A Simplified Reconstitution of mRNA-Directed Peptide Synthesis: Activity of the Epsilon Enhancer Sequence and an Unnatural Amino Acid.
Forster, A, Weissbach, H, and Blacklow, SC. Analytical Biochemistry 2001; 297: 60-70.

Cysteine-Rich Module Structure Reveals a Fulcrum for Integrin Rearrangement Upon Activation.
Beglova, N, Blacklow, SC, Takagi, J, Springer, TA. Nature Structure Biology 2002; 9:282-287.

Definition of EGF-like, closely interacting modules that bear activation epitopes in integrin beta subunits.
Takagi, J, Beglova, N, Yalamanchili, P, Blacklow, SC, and Springer, TA. PNAS 2001; 98:11175-11180.

The SCAN domain of ZNF174 is a dimer.
Stone JR, Maki JL, Blacklow SC, and Collins T. J Biol Chem 2002;277:5448-5452.

The role of water in the catalytic efficiency of triosephosphate isomerase.
Zhang Z, Komives EA, Sugio S, Blacklow SC, Narayana N, Xuong NH, Stock AM, Petsko GA, and Ringe D. Biochemistry 1999;38:4389-97.

The zinc finger-associated SCAN box is an oligomerization domain.
Williams, AJ, Blacklow, SC, and Collins, T. Mol Cell Biol 1999;19:8526-8535.