| Year |
Citation |
Score |
| 2019 |
Sieng M, Hayes MP, O'Brien JB, Fowler CA, Houtman JC, Roman DL, Lyon AM. High-resolution structure of RGS17 suggests a role for Ca2+ in promoting the GTPase activating protein activity by RZ subfamily members. The Journal of Biological Chemistry. PMID 30940727 DOI: 10.1074/Jbc.Ra118.006059 |
0.382 |
|
| 2017 |
Zhang L, Martini GD, Rube HT, Kribelbauer JF, Rastogi C, FitzPatrick VD, Houtman JC, Bussemaker HJ, Pufall MA. SelexGLM differentiates androgen and glucocorticoid receptor DNA-binding preference over an extended binding site. Genome Research. PMID 29196557 DOI: 10.1101/Gr.222844.117 |
0.356 |
|
| 2017 |
McLinden JH, Bhattarai N, Stapleton JT, Chang Q, Kaufman TM, Cassel SL, Sutterwala FS, Haim H, Houtman J, Xiang J. Yellow fever virus, but not Zika or Dengue virus inhibits T cell receptor-mediated T cell function by an RNA-based mechanism. The Journal of Infectious Diseases. PMID 28968905 DOI: 10.1093/Infdis/Jix462 |
0.318 |
|
| 2016 |
Hastie JL, Williams KB, Bohr LL, Houtman JC, Gakhar L, Ellermeier CD. The Anti-sigma Factor RsiV Is a Bacterial Receptor for Lysozyme: Co-crystal Structure Determination and Demonstration That Binding of Lysozyme to RsiV Is Required for σV Activation. Plos Genetics. 12: e1006287. PMID 27602573 DOI: 10.1371/Journal.Pgen.1006287 |
0.503 |
|
| 2014 |
Hastie JL, Williams KB, Sepúlveda C, Houtman JC, Forest KT, Ellermeier CD. Evidence of a bacterial receptor for lysozyme: binding of lysozyme to the anti-σ factor RsiV controls activation of the ecf σ factor σV. Plos Genetics. 10: e1004643. PMID 25275625 DOI: 10.1371/Journal.Pgen.1004643 |
0.488 |
|
| 2014 |
Streeter J, Schickling BM, Jiang S, Stanic B, Thiel WH, Gakhar L, Houtman JC, Miller FJ. Phosphorylation of Nox1 regulates association with NoxA1 activation domain. Circulation Research. 115: 911-8. PMID 25228390 DOI: 10.1161/Circresaha.115.304267 |
0.488 |
|
| 2014 |
Cruz-Orcutt N, Vacaflores A, Connolly SF, Bunnell SC, Houtman JC. Activated PLC-γ1 is catalytically induced at LAT but activated PLC-γ1 is localized at both LAT- and TCR-containing complexes. Cellular Signalling. 26: 797-805. PMID 24412752 DOI: 10.1016/J.Cellsig.2013.12.022 |
0.334 |
|
| 2013 |
Willett JW, Tiwari N, Müller S, Hummels KR, Houtman JC, Fuentes EJ, Kirby JR. Specificity residues determine binding affinity for two-component signal transduction systems. Mbio. 4: e00420-13. PMID 24194534 DOI: 10.1128/Mbio.00420-13 |
0.31 |
|
| 2013 |
Bartelt RR, Houtman JC. The adaptor protein LAT serves as an integration node for signaling pathways that drive T cell activation. Wiley Interdisciplinary Reviews. Systems Biology and Medicine. 5: 101-10. PMID 23150273 DOI: 10.1002/Wsbm.1194 |
0.313 |
|
| 2009 |
Cruz-Orcutt N, Houtman JC. PI3 kinase function is vital for the function but not formation of LAT-mediated signaling complexes. Molecular Immunology. 46: 2274-83. PMID 19427038 DOI: 10.1016/j.molimm.2009.04.006 |
0.317 |
|
| 2006 |
Houtman JC, Yamaguchi H, Barda-Saad M, Braiman A, Bowden B, Appella E, Schuck P, Samelson LE. Oligomerization of signaling complexes by the multipoint binding of GRB2 to both LAT and SOS1. Nature Structural & Molecular Biology. 13: 798-805. PMID 16906159 DOI: 10.1038/nsmb1133 |
0.364 |
|
| 2004 |
Houtman JC, Higashimoto Y, Dimasi N, Cho S, Yamaguchi H, Bowden B, Regan C, Malchiodi EL, Mariuzza R, Schuck P, Appella E, Samelson LE. Binding specificity of multiprotein signaling complexes is determined by both cooperative interactions and affinity preferences. Biochemistry. 43: 4170-8. PMID 15065860 DOI: 10.1021/bi0357311 |
0.342 |
|
| 2004 |
Cho S, Velikovsky CA, Swaminathan CP, Houtman JC, Samelson LE, Mariuzza RA. Structural basis for differential recognition of tyrosine-phosphorylated sites in the linker for activation of T cells (LAT) by the adaptor Gads. The Embo Journal. 23: 1441-51. PMID 15029250 DOI: 10.1038/Sj.Emboj.7600168 |
0.349 |
|
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