The DOI matches its Crossref record; 182 of the 182 references it cites were found in a registry or an index.
Recent insights of T cell receptor-mediated signaling pathways for T cell activation and development
Abstract
T cell activation requires extracellular stimulatory signals that are mainly mediated by T cell receptor (TCR) complexes. The TCR recognizes antigens on major histocompatibility complex molecules with the cooperation of CD4 or CD8 coreceptors. After recognition, TCR-induced signaling cascades that propagate signals via various molecules and second messengers are induced. Consequently, many features of T cell-mediated immune responses are determined by these intracellular signaling cascades. Furthermore, differences in the magnitude of TCR signaling direct T cells toward distinct effector linages. Therefore, stringent regulation of T cell activation is crucial for T cell homeostasis and proper immune responses. Dysregulation of TCR signaling can result in anergy or autoimmunity. In this review, we summarize current knowledge on the pathways that govern how the TCR complex transmits signals into cells and the roles of effector molecules that are involved in these pathways.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Figures


Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Inactive Lck will then fail to stimulate PI3K signalling [51] and decrease DOCK8-induced Rac1 activation [52].”
From The Role of RhoH in TCR Signalling and Its Involvement in Diseases (2021) · cites this paper as [51]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
1 retracted
Jia, H., Xu, M. Q., Bo, Y., Li, W., & Zhou, R. (2019) · Life Sciences · doi:10.1016/j.lfs.2019.05.060 · Cited by 5
RetractedHershko, A., & Ciechanover, A. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.425 · Cited by 8,840
Mechanisms Underlying Ubiquitination
Pickart, C. M. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.503 · Cited by 3,184
RAG-1-deficient mice have no mature B and T lymphocytes
Mombaerts, P., Iacomini, J., Johnson, R. S., Herrup, K., Tonegawa, S., & Papaioannou, V. E. (1992) · Cell · doi:10.1016/0092-8674(92)90030-g · Cited by 2,972
RING Domain E3 Ubiquitin Ligases
Deshaies, R. J., & Joazeiro, C. A. P. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.101807.093809 · Cited by 2,679
Negative regulation of PKB/Akt-dependent cell survival by the tumor suppressor PTEN
Stambolic, V., Suzuki, A., de la Pompa, J. L., Brothers, G. M., Mirtsos, C., Sasaki, T., Ruland, J., Penninger, J. M., Siderovski, D. P., & Mak, T. W. (1998) · Cell · doi:10.1016/s0092-8674(00)81780-8 · Cited by 2,551
Zheng, W.-P., & Flavell, R. A. (1997) · Cell · doi:10.1016/s0092-8674(00)80240-8 · Cited by 2,384
Identification of Clonogenic Common Lymphoid Progenitors in Mouse Bone Marrow
Kondo, M., Weissman, I. L., & Akashi, K. (1997) · Cell · doi:10.1016/s0092-8674(00)80453-5 · Cited by 2,253
Smith-Garvin, J. E., Koretzky, G. A., & Jordan, M. S. (2009) · Annual Review of Immunology · doi:10.1146/annurev.immunol.021908.132706 · Cited by 2,144
Deng, L., Wang, C., Spencer, E., Yang, L., Braun, A., You, J., Slaughter, C., Pickart, C., & Chen, Z. J. (2000) · Cell · doi:10.1016/s0092-8674(00)00126-4 · Cited by 1,872
Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain
Schroeter, E. H., Kisslinger, J. A., & Kopan, R. (1998) · Nature · doi:10.1038/30756 · Cited by 1,624
Positive and negative selection of T cells
Starr, T. K., Jameson, S. C., & Hogquist, K. A. (2003) · Annual Review of Immunology · doi:10.1146/annurev.immunol.21.120601.141107 · Cited by 1,601
Zhang, S. L., Yu, Y., Roos, J., Kozak, J. A., Deerinck, T. J., Ellisman, M. H., Stauderman, K. A., & Cahalan, M. D. (2005) · Nature · doi:10.1038/nature04147 · Cited by 1,412
Chen, Z., Hagler, J., Palombella, V. J., Melandri, F., Scherer, D., Ballard, D., & Maniatis, T. (1995) · Genes & Development · doi:10.1101/gad.9.13.1586 · Cited by 1,290
Zhang, W., Sloan‐Lancaster, J., Kitchen, J., Trible, R. P., & Samelson, L. E. (1998) · Cell · doi:10.1016/s0092-8674(00)80901-0 · Cited by 1,271
Isolation of cDNA clones encoding T cell-specific membrane-associated proteins
Hedrick, S. M., Cohen, D. I., Nielsen, E. A., & Davis, M. M. (1984) · Nature · doi:10.1038/308149a0 · Cited by 1,244
Rapamycin selectively expands CD4+CD25+FoxP3+ regulatory T cells.
Battaglia, M., Stabilini, A., & Roncarolo, M. (2005) · Blood · doi:10.1182/blood-2004-10-3932 · Cited by 1,203
Peterson, T. R., Laplante, M., Thoreen, C. C., Sancak, Y., Kang, S. A., Kuehl, W. M., Gray, N. S., & Sabatini, D. M. (2009) · Cell · doi:10.1016/j.cell.2009.03.046 · Cited by 1,202
Wharton, K. A., Johansen, K. M., Xu, T., & Artavanis‐Tsakonas, S. (1985) · Cell · doi:10.1016/0092-8674(85)90229-6 · Cited by 1,065
Moran, A. E., Holzapfel, K. L., Xing, Y., Cunningham, N. R., Maltzman, J. S., Punt, J. A., & Hogquist, K. A. (2011) · The Journal of Experimental Medicine · doi:10.1084/jem.20110308 · Cited by 1,060
ZAP-70: A 70 kd protein-tyrosine kinase that associates with the TCR ζ chain
Chan, A. C., Iwashima, M., Turck, C. W., & Weiss, A. (1992) · Cell · doi:10.1016/0092-8674(92)90598-7 · Cited by 1,041
The ikaros gene is required for the development of all lymphoid lineages
Georgopoulos, K., Bigby, M., Wang, J.-H., Molnar, A., Wu, P., Winandy, S., & Sharpe, A. (1994) · Cell · doi:10.1016/0092-8674(94)90407-3 · Cited by 985
RAS isoforms and mutations in cancer at a glance
Hobbs, G. A., Der, C. J., & Rossman, K. L. (2016) · Journal of Cell Science · doi:10.1242/jcs.182873 · Cited by 973
Profound block in thymocyte development in mice lacking p56lck
Molina, T. J., Kishihara, K., Siderovski, D. P., van Ewijk, W., Narendran, A., Timms, E. M., Wakeham, A. C., Paige, C. J., Hartmann, K.-U., Veillette, A., et al. (1992) · Nature · doi:10.1038/357161a0 · Cited by 970
Mebratu, Y., & Tesfaigzi, Y. (2009) · Cell Cycle · doi:10.4161/cc.8.8.8147 · Cited by 957
Notch1 Expression in Early Lymphopoiesis Influences B versus T Lineage Determination
Pui, J. C., Allman, D., Xu, L., DeRocco, S. E., Karnell, F. G., Bakkour, S., Lee, J. Y., Kadesch, T. R., Hardy, R. R., Aster, J. C., et al. (1999) · Immunity · doi:10.1016/s1074-7613(00)80105-3 · Cited by 943
PKC-θ is required for TCR-induced NF-κB activation in mature but not immature T lymphocytes
Sun, Z., Arendt, C. W., Ellmeier, W., Schaeffer, E. M., Sunshine, M. J., Gandhi, L., Annes, J., Petrzilka, D., Kupfer, A., Schwartzberg, P. L., et al. (2000) · Nature · doi:10.1038/35006090 · Cited by 892
T-cell development and the CD4–CD8 lineage decision
Germain, R. N. (2002) · Nature reviews. Immunology · doi:10.1038/nri798 · Cited by 887
Godfrey, D. I., Kennedy, J., Suda, T., & Zlotnik, A. (1993) · The Journal of Immunology · doi:10.4049/jimmunol.150.10.4244 · Cited by 843
Inositol trisphosphate and calcium signalling mechanisms
Berridge, M. J. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.10.005 · Cited by 797
Regulation of inositol phospholipid-specific phospholipase C isozymes.
Rhee, S. G., & Choi, K. D. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42284-3 · Cited by 741
Nuclear Access and Action of Notch In Vivo
Struhl, G., & Adachi, A. (1998) · Cell · doi:10.1016/s0092-8674(00)81193-9 · Cited by 733
Sun, L., Deng, L., Ea, C.-K., Xia, Z.-P., & Chen, Z. J. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00236-9 · Cited by 699
Complete but curtailed T-cell response to very low-affinity antigen
Zehn, D., Lee, S. Y., & Bevan, M. J. (2009) · Nature · doi:10.1038/nature07657 · Cited by 696
Constant, S., Pfeiffer, C., Woodard, A., Pasqualini, T., & Bottomly, K. (1995) · The Journal of experimental medicine · doi:10.1084/jem.182.5.1591 · Cited by 677
DNA-Binding Specificity of GATA Family Transcription Factors
Merika, M., & Orkin, S. H. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.7.3999-4010.1993 · Cited by 670
Zhang, D.-H., Cohn, L., Ray, P., Bottomly, K., & Ray, A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.34.21597 · Cited by 665
Mutual regulation of the transcriptional activator NF-kappa B and its inhibitor, I kappa B-alpha.
Brown, K., Park, S., Kanno, T., Franzoso, G., & Siebenlist, U. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.6.2532 · Cited by 621
Self-citationTranscription factor GATA-3 is required for development of the T-cell lineage
Ting, C.-N., Olson, M. C., Barton, K. P., & Leiden, J. M. (1996) · Nature · doi:10.1038/384474a0 · Cited by 615
Wang, J., Nichogiannopoulou, A., Wu, L. J., Sun, L., Sharpe, A. H., Bigby, M. E., & Georgopoulos, K. (1996) · Immunity · doi:10.1016/s1074-7613(00)80269-1 · Cited by 614
TCR Signaling: Mechanisms of Initiation and Propagation
Courtney, A. H., Lo, W., & Weiss, A. (2017) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2017.11.008 · Cited by 600
DNA-Binding Specificities of the GATA Transcription Factor Family
Ko, L. J., & Engel, J. D. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.7.4011-4022.1993 · Cited by 583
Transfer of specificity by murine α and β T-cell receptor genes
DembiĆ, Z., Haas, W., Weiss, S., McCubrey, J., Kiefer, H., von Boehmer, H., & Steinmetz, M. (1986) · Nature · doi:10.1038/320232a0 · Cited by 579
Signal Transduction Mediated by the T Cell Antigen Receptor: The Role of Adapter Proteins
Samelson, L. E. (2002) · Annual Review of Immunology · doi:10.1146/annurev.immunol.20.092601.111357 · Cited by 573
Interaction between hamartin and tuberin, the TSC1 and TSC2 gene products
van Slegtenhorst, M. (1998) · Human Molecular Genetics · doi:10.1093/hmg/7.6.1053 · Cited by 565
pp59fyn mutant mice display differential signaling in thymocytes and peripheral T cells
Stein, P. L., Lee, H.-M., Rich, S. S., & Soriano, P. M. (1992) · Cell · doi:10.1016/0092-8674(92)90308-y · Cited by 557
Selective modulation of protein kinase C-Θ during T-cell activation
Monks, C. R. F., Kupfer, H., Tamir, I., Barlow, A. K., & Kupfer, A. (1997) · Nature · doi:10.1038/385083a0 · Cited by 553
Bcl10 activates the NF-κB pathway through ubiquitination of NEMO
Zhou, H., Wertz, I., O'Rourke, K., Ultsch, M., Seshagiri, S., Eby, M., Xiao, W., & Dixit, V. M. (2004) · Nature · doi:10.1038/nature02273 · Cited by 527
Facchinetti, V., Ouyang, W., Wei, H., Soto, N., Lazorchak, A. S., Gould, C. M., Lowry, C. J., Newton, A. C., Mao, Y., Miao, Q., et al. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.120 · Cited by 527
Calcineurin imposes T cell unresponsiveness through targeted proteolysis of signaling proteins
Heissmeyer, V., Macián, F., Im, S., Varma, R., Feske, S., Venuprasad, K., Gu, H., Liu, Y., Dustin, M. L., & Rao, A. (2004) · Nature Immunology · doi:10.1038/ni1047 · Cited by 524
Defective T cell receptor signaling in mice lacking the thymic isoform of p59fyn
Appleby, M. W., Gross, J. A., Cooke, M. P., Levin, S. D., Qian, X., & Perlmutter, R. M. (1992) · Cell · doi:10.1016/0092-8674(92)90309-z · Cited by 499
Inhibition of tyrosine phosphorylation prevents T-cell receptor-mediated signal transduction.
June, C. H., Fletcher, M. C., Ledbetter, J. A., Schieven, G. L., Siegel, J. N., Phillips, A. F., & Samelson, L. E. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.19.7722 · Cited by 491
Ubiquitin signaling in immune responses
Hu, H., & Sun, S.-C. (2016) · Cell Research · doi:10.1038/cr.2016.40 · Cited by 485
TCR ligand discrimination is enforced by competing ERK positive and SHP-1 negative feedback pathways
Štefanová, I., Hemmer, B., Vergelli, M., Martin, R., Biddison, W. E., & Germain, R. N. (2003) · Nature Immunology · doi:10.1038/ni895 · Cited by 465
Georgopoulos, K., Moore, D. D., & Derfler, B. (1992) · Science · doi:10.1126/science.1439790 · Cited by 464
T Cell Antigen Receptor-Mediated Activation of Phospholipase C Requires Tyrosine Phosphorylation
Mustelin, T., Coggeshall, K. M., Isakov, N., & Altman, A. (1990) · Science · doi:10.1126/science.2138816 · Cited by 456
Fazilleau, N., McHeyzer‐Williams, L. J., Rosen, H., & McHeyzer‐Williams, M. G. (2009) · Nature Immunology · doi:10.1038/ni.1704 · Cited by 451
The role of Jun, Fos and the AP-1 complex in cell-proliferation and transformation
Angel, P., & Karin, M. (1991) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/0304-419x(91)90011-9 · Cited by 450
Tubo, N. J., Pagán, A. J., Taylor, J. J., Nelson, R. W., Linehan, J. L., Ertelt, J. M., Huseby, E. S., Way, S. S., & Jenkins, M. K. (2013) · Cell · doi:10.1016/j.cell.2013.04.007 · Cited by 444
The Ikaros gene encodes a family of functionally diverse zinc finger DNA-binding proteins.
Molnár, A., & Georgopoulos, K. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.12.8292 · Cited by 434
Diacylglycerol kinases: at the hub of cell signalling
Mérida, I., Ávila‐Flores, A., & Merino, E. (2007) · Biochemical Journal · doi:10.1042/bj20071040 · Cited by 434
Calcium signaling in lymphocytes
Oh‐hora, M., & Rao, A. (2008) · Current Opinion in Immunology · doi:10.1016/j.coi.2008.04.004 · Cited by 428
Activation of T Cells by a Tyrosine Kinase Activation Domain in the Cytoplasmic Tail of CD3 ε
Letourneur, F., & Klausner, R. D. (1992) · Science · doi:10.1126/science.1532456 · Cited by 412
NF‐κB: roles and regulation in different CD 4+ T‐cell subsets
Oh, H., & Ghosh, S. (2013) · Immunological Reviews · doi:10.1111/imr.12033 · Cited by 408
Malissen, M., Minard, K. I., Mjolsness, S., Kronenberg, M., Goverman, J. M., Hunkapiller, T., Prystowsky, M. B., Yoshikai, Y., Fitch, F. W., Mak, T. W., et al. (1984) · Cell · doi:10.1016/0092-8674(84)90444-6 · Cited by 401
Restoration of T Cell Development in RAG-2-Deficient Mice by Functional TCR Transgenes
Shinkai, Y., Koyasu, S., Nakayama, K. I., MURPHY, K. M. M., Loh, D. Y., Reinherz, E. L., & Alt, F. W. (1993) · Science · doi:10.1126/science.8430336 · Cited by 400
Notch 1–Deficient Common Lymphoid Precursors Adopt a B Cell Fate in the Thymus
Wilson, A., MacDonald, H. R., & Radtke, F. (2001) · The Journal of Experimental Medicine · doi:10.1084/jem.194.7.1003 · Cited by 398
Jun Turnover Is Controlled Through JNK-Dependent Phosphorylation of the E3 Ligase Itch
Gao, M., Labuda, T., Xia, Y., Gallagher, E. D., Fang, D., Liu, Y., & Karin, M. (2004) · Science · doi:10.1126/science.1099414 · Cited by 397
SHP‐1 and SHP‐2 in T cells: two phosphatases functioning at many levels
Lorenz, U. M. (2009) · Immunological Reviews · doi:10.1111/j.1600-065x.2008.00760.x · Cited by 394
CARMA1, BCL-10 and MALT1 in lymphocyte development and activation
Thome, M. (2004) · Nature Reviews Immunology · doi:10.1038/nri1352 · Cited by 391
Regulation of T-cell activation by the cytoskeleton
Billadeau, D. D., Nolz, J. C., & Gomez, T. S. (2007) · Nature reviews. Immunology · doi:10.1038/nri2021 · Cited by 389
STRUCTURE AND FUNCTION OF THE PRE-T CELL RECEPTOR
von Boehmer, H., & Fehling, H. J. (1997) · Annual Review of Immunology · doi:10.1146/annurev.immunol.15.1.433 · Cited by 387
Samelson, L. E., Patel, M. D., Weissman, A. M., Harford, J. B., & Klausner, R. D. (1986) · Cell · doi:10.1016/0092-8674(86)90708-7 · Cited by 381
Morgan, B., Sun, L., Avitahl, N., Andrikopoulos, K., Ikeda, T., Gonzales, E., Wu, P., Neben, S., & Georgopoulos, K. (1997) · The EMBO Journal · doi:10.1093/emboj/16.8.2004 · Cited by 367
CARMA1 is a critical lipid raft–associated regulator of TCR-induced NF-κB activation
Gaide, O., Favier, B., Legler, D. F., Bonnet, D., Brissoni, B., Valitutti, S., Bron, C., Tschopp, J., & Thome, M. (2002) · Nature Immunology · doi:10.1038/ni830 · Cited by 343
Ho, I., Vorhees, P., Marín, N., Oakley, B. K., Tsai, S., Orkin, S. H., & Leiden, J. M. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb08059.x · Cited by 338
Groettrup, M., Ungewiss, K., Azogui, O., Palacios, R., Owen, M. J., Hayday, A., & von Boehmer, H. (1993) · Cell · doi:10.1016/0092-8674(93)80070-u · Cited by 331
Protein Kinase C θ Affects Ca2+ Mobilization and NFAT Activation in Primary Mouse T Cells
Pfeifhofer, C., Kofler, K., Gruber, T., Ghaffari Tabrizi, N., Lutz, C., Maly, K., Leitges, M., & Baier, G. (2003) · The Journal of Experimental Medicine · doi:10.1084/jem.20020234 · Cited by 326
NF-κB activation induced by T cell receptor/CD28 costimulation is mediated by protein kinase C-θ
Coudronniere, N., Villalba, M., Englund, N., & Altman, A. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.7.3394 · Cited by 321
Bergman, M., Mustelin, T., Oetken, C., Partanen, J. M., Flint, N. A., Amrein, K. E., Autero, M., Burn, P., & Alitalo, K. K. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05361.x · Cited by 319
Critical Roles for Transcription Factor GATA-3 in Thymocyte Development
Pai, S., Truitt, M., Ting, C.-N., Leiden, J. M., Glimcher, L. H., & Ho, I. (2003) · Immunity · doi:10.1016/s1074-7613(03)00328-5 · Cited by 312
Decision checkpoints in the thymus
Carpenter, A. C., & Bosselut, R. (2010) · Nature Immunology · doi:10.1038/ni.1887 · Cited by 306
Disruption of diacylglycerol metabolism impairs the induction of T cell anergy
Olenchock, B. A., Guo, R., Carpenter, J. H., Jordan, M. S., Topham, M. K., Koretzky, G. A., & Zhong, X.-P. (2006) · Nature Immunology · doi:10.1038/ni1400 · Cited by 302
Phosphorylation of CARMA1 Plays a Critical Role in T Cell Receptor-Mediated NF-κB Activation
Matsumoto, R., Wang, D., Blonska, M., Li, H., Kobayashi, M., Pappu, B., Chen, Y., Wang, D., & Lin, X. (2005) · Immunity · doi:10.1016/j.immuni.2005.10.007 · Cited by 295
Notch as a Mediator of Cell Fate Determination in Hematopoiesis: Evidence and Speculation
Milner, L. A., & Bigas, A. (1999) · Blood · doi:10.1182/blood.v93.8.2431 · Cited by 293
LFA-1 in T Cell Migration and Differentiation
Walling, B. L., & Kim, M. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.00952 · Cited by 287
Anandasabapathy (2003) · doi:10.1016/s1074-7613(03)00084-0 · Cited by 285
Evans, R., Patzak, I., Svensson, L., De Filippo, K., Jones, K., McDowall, A., & Hogg, N. (2009) · Journal of Cell Science · doi:10.1242/jcs.019117 · Cited by 281
TCR ligand density and affinity determine peripheral induction of Foxp3 in vivo
Gottschalk, R. A., Corse, E., & Allison, J. P. (2010) · Journal of Experimental Medicine · doi:10.1084/jem.20091999 · Cited by 278
T cell anergy is reversed by active Ras and is regulated by diacylglycerol kinase-α
Zha, Y., Marks, R., Ho, A. W., Peterson, A. C., Janardhan, S., Brown, I., Praveen, K., Stang, S., Stone, J. C., & Gajewski, T. F. (2006) · Nature Immunology · doi:10.1038/ni1394 · Cited by 267
Lin, X., O'Mahony, A., Mu, Y., Geleziunas, R., & Greene, W. C. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.8.2933-2940.2000 · Cited by 265
Hahm, K., Cobb, B. S., McCarty, A., Brown, K. E., Klug, C. A., Lee, R., Akashi, K., Weissman, I. L., Fisher, A. G., & Smale, S. T. (1998) · Genes & Development · doi:10.1101/gad.12.6.782 · Cited by 257
Baier, G., Überall, F., Bauer, B., Fresser, F., WACHTER, H., Grunicke, H. H., Utermann, G., Altman, A., & Baier, G. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.4.1842 · Cited by 254
PDK1 Nucleates T Cell Receptor-Induced Signaling Complex for NF-κB Activation
Lee, K.-Y., D'Acquisto, F., Hayden, M. S., Shim, J.-H., & Ghosh, S. (2005) · Science · doi:10.1126/science.1107107 · Cited by 253
GATA-3 Promotes Maturation, IFN-γ Production, and Liver-Specific Homing of NK Cells
Samson, S., Richard, O., Tavian, M., Ranson, T., Vosshenrich, C. A. J., Colucci, F., Buer, J., Grosveld, F. G., Godin, I., & Santo, J. P. D. (2003) · Immunity · doi:10.1016/s1074-7613(03)00294-2 · Cited by 243
Deltex1 Redirects Lymphoid Progenitors to the B Cell Lineage by Antagonizing Notch1
Izon, D. J., Aster, J. C., He, Y., Weng, A. P., Karnell, F. G., Patriub, V., Xu, L., Bakkour, S., Rodríguez, C. E., Allman, D., et al. (2002) · Immunity · doi:10.1016/s1074-7613(02)00271-6 · Cited by 243
Buday, L., Egan, S. E., Viciana, P. R., Cantrell, D. A., & Downward, J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37070-9 · Cited by 238
Shui, J., Boomer, J. S., Han, J., Xu, J. Q., Dement, G. A., Zhou, G., & Tan, T. (2006) · Nature Immunology · doi:10.1038/ni1416 · Cited by 234
Zinc transporter ZIP8 (SLC39A8) and zinc influence IFN-γ expression in activated human T cells
Aydemir, T. B., Liuzzi, J. P., McClellan, S., & Cousins, R. J. (2009) · Journal of Leukocyte Biology · doi:10.1189/jlb.1208759 · Cited by 229
E3 ubiquitin ligases as T cell anergy factors
Mueller, D. L. (2004) · Nature Immunology · doi:10.1038/ni1106 · Cited by 224
Enhanced T cell responses due to diacylglycerol kinase ζ deficiency
Zhong, X., Hainey, E. A., Olenchock, B. A., Jordan, M. S., Maltzman, J. S., Nichols, K. E., Shen, H., & Koretzky, G. A. (2003) · Nature Immunology · doi:10.1038/ni958 · Cited by 221
Wang, L., Wildt, K. F., Zhu, J., Zhang, X., Feigenbaum, L., Tessarollo, L., Paul, W. E., Fowlkes, B. J., & Bosselut, R. (2008) · Nature Immunology · doi:10.1038/ni.1647 · Cited by 220
Gómez‐Rodríguez, J., Sahu, N., Handon, R., Davidson, T. S., Anderson, S. M., Kirby, M., August, A., & Schwartzberg, P. L. (2009) · Immunity · doi:10.1016/j.immuni.2009.07.009 · Cited by 218
Lee, H., Bautista, J. L., Scott-Browne, J. P., Mohan, J. F., & Hsieh, C. (2012) · Immunity · doi:10.1016/j.immuni.2012.07.009 · Cited by 215
Regulation of T cells by mTOR: the known knowns and the known unknowns
Pollizzi, K. N., & Powell, J. D. (2014) · Trends in Immunology · doi:10.1016/j.it.2014.11.005 · Cited by 204
Vogel, K. U., Edelmann, S. L., Jeltsch, K. M., Bertossi, A., Heger, K., Heinz, G. A., Zöller, J., Warth, S. C., Hoefig, K. P., Lohs, C., et al. (2013) · Immunity · doi:10.1016/j.immuni.2012.12.004 · Cited by 200
NF-κB signaling pathways regulated by CARMA family of scaffold proteins
Blonska, M., & Lin, X. (2010) · Cell Research · doi:10.1038/cr.2010.182 · Cited by 198
Koch, U., Lacombe, T. A., Holland, D., Bowman, J. L., Cohen, B. L., Egan, S. E., & Guidos, C. J. (2001) · Immunity · doi:10.1016/s1074-7613(01)00189-3 · Cited by 193
McNeill, L., Salmond, R. J., Cooper, J. C., Carret, C., Cassady-Cain, R. L., Roche-Molina, M., Tandon, P., Holmes, N., & Alexander, D. R. (2007) · Immunity · doi:10.1016/j.immuni.2007.07.015 · Cited by 189
The role of apoptosis in the development and function of T lymphocytes
Zhang, N., Hartig, H. M., Dzhagalov, I. L., DRAPER, D., & He, Y. W. (2005) · Cell Research · doi:10.1038/sj.cr.7290345 · Cited by 186
Cutting Edge: Piezo1 Mechanosensors Optimize Human T Cell Activation
Liu, C. S. C., Raychaudhuri, D., Paul, B., Chakrabarty, Y., Ghosh, A. R., Rahaman, O., Talukdar, A., & Ganguly, D. (2018) · The Journal of Immunology · doi:10.4049/jimmunol.1701118 · Cited by 182
T Regulatory Cells Maintain Intestinal Homeostasis by Suppressing γδ T Cells
Park, S., Mathur, R., Long, M., Hosh, N., Hao, L., Hayden, M. S., & Ghosh, S. (2010) · Immunity · doi:10.1016/j.immuni.2010.10.014 · Cited by 176
Self-citationHuang, H., Jeon, M., Liao, L., Yang, C., Elly, C., Yates, J. R., & Liu, Y. (2010) · Immunity · doi:10.1016/j.immuni.2010.07.002 · Cited by 174
Regulation of ZAP-70 Activation and TCR Signaling by Two Related Proteins, Sts-1 and Sts-2
Carpino, N., Turner, S., Mekala, D. J., Takahashi, Y., Zang, H., Geiger, T. L., Doherty, P. C., & Ihle, J. N. (2004) · Immunity · doi:10.1016/s1074-7613(03)00351-0 · Cited by 169
Cbl Promotes Ubiquitination of the T Cell Receptor ζ through an Adaptor Function of Zap-70
Wang, H.-Y., Altman, Y., Fang, D., Elly, C., Dai, Y., Shao, Y., & Liu, Y. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010738200 · Cited by 168
Physiological roles of MKK4 and MKK7: Insights from animal models
Wang, X., Destrument, A., & Tournier, C. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.10.016 · Cited by 168
Pre–T Cell Receptor (Tcr) and Tcr-Controlled Checkpoints in T Cell Differentiation Are Set by Ikaros
Winandy, S., Wu, L., Wang, J., & Georgopoulos, K. (1999) · The Journal of Experimental Medicine · doi:10.1084/jem.190.8.1039 · Cited by 164
A cascade of protein kinase C isozymes promotes cytoskeletal polarization in T cells
Quann, E. J., Liu, X., Altan-Bonnet, G. Y., & Huse, M. (2011) · Nature Immunology · doi:10.1038/ni.2033 · Cited by 162
Bu, J.-Y., Shaw, A. S., & Chan, A. C. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.11.5106 · Cited by 158
Chiang, G. G., & Sefton, B. M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101219200 · Cited by 157
Park, S., Schulze-Luehrman, J., Hayden, M. S., Hashimoto, N., Ogawa, W., Kasuga, M., & Ghosh, S. (2009) · Nature Immunology · doi:10.1038/ni.1687 · Cited by 154
Self-citationRole of Polyamines in Immune Cell Functions
Hesterberg, R. S., Cleveland, J. L., & Epling‐Burnette, P. K. (2018) · Medical Sciences · doi:10.3390/medsci6010022 · Cited by 150
JunB promotes Th17 cell identity and restrains alternative CD4+ T-cell programs during inflammation
Carr, T. M., Wheaton, J. D., Houtz, G. M., & Ciofani, M. (2017) · Nature Communications · doi:10.1038/s41467-017-00380-3 · Cited by 147
SHP1 Phosphatase-Dependent T Cell Inhibition by CEACAM1 Adhesion Molecule Isoforms
Nagaishi, T., Pao, L. I., Lin, S.-H., Iijima, H., Kaser, A., Qiao, S., Chen, Z., Glickman, J. N., Najjar, S. M., Nakajima, A., et al. (2006) · Immunity · doi:10.1016/j.immuni.2006.08.026 · Cited by 143
Joseph, N., Reicher, B., & Barda‐Saad, M. (2013) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2013.07.009 · Cited by 142
Cutting Edge: The CD45 Tyrosine Phosphatase Is an Inhibitor of Lck Activity in Thymocytes
D’Oro, U., & Ashwell, J. D. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.162.4.1879 · Cited by 138
Brogdon, J. L., Leitenberg, D., & Bottomly, K. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.168.8.3825 · Cited by 136
Abatacept alleviates severe autoimmune symptoms in a patient carrying a de novo variant in CTLA-4
Lee, S., Moon, J. S., Lee, C., Kim, H., Baek, S.-M., Hwang, S., Kang, G. H., Seo, J. K., Shin, C. H., Kang, H. J., et al. (2015) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2015.08.036 · Cited by 133
Self-citationLow-strength T-cell activation promotes Th17 responses
Purvis, H. A., Stoop, J. N., Mann, J., Woods Jon, S., Kozijn, A. E., Hambleton, S., Robinson, J. H., Isaacs, J. D., Anderson, A. E., & Hilkens, C. M. U. (2010) · Blood · doi:10.1182/blood-2010-03-272153 · Cited by 128
Liu, Y., Witte, S., Liu, Y., Doyle, M., Elly, C., & Altman, A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.5.3603 · Cited by 125
T-cell-receptor- and B-cell-receptor-mediated activation of NF-κB in lymphocytes
Weil, R., & Israël, A. (2004) · Current Opinion in Immunology · doi:10.1016/j.coi.2004.03.003 · Cited by 125
NF-κB activation induced by TCR/CD28 costimulation is mediated by PKC-θ
Coudronnière, N. (2000) · Medical Entomology and Zoology · Cited by 124
A Phosphatase Activity of Sts-1 Contributes to the Suppression of TCR Signaling
Mikhailik, A., Ford, B. A., Keller, J. C., Chen, Y., Nassar, N. N., & Carpino, N. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.06.015 · Cited by 123
The roles of CARMA1, Bcl10, and MALT1 in antigen receptor signaling
Lin, X., & Wang, D. (2004) · Seminars in Immunology · doi:10.1016/j.smim.2004.08.022 · Cited by 121
The serine kinase phosphoinositide-dependent kinase 1 (PDK1) regulates T cell development
Hinton, H. J., Alessi, D. R., & Cantrell, D. A. (2004) · Nature Immunology · doi:10.1038/ni1062 · Cited by 121
Regulation of T Cell Receptor-induced Activation of the Ras-ERK Pathway by Diacylglycerol Kinase ζ
Zhong, X., Hainey, E. A., Olenchock, B. A., Zhao, H., Topham, M. K., & Koretzky, G. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203818200 · Cited by 119
Round, J. L., Humphries, L. A., Tomassian, T., Mittelstadt, P. R., Zhang, M., & Miceli, M. C. (2006) · Nature Immunology · doi:10.1038/ni1422 · Cited by 117
The δ- and ε-chains of the human T3/T-cell receptor complex are distinct polypeptides
Borst, J. G., Coligan, J. E., Oettgen, H. C., Pessano, S., Malin, R., & Terhorst, C. (1984) · Nature · doi:10.1038/312455a0 · Cited by 115
Diacylglycerol kinases in immune cell function and self‐tolerance
Zhong, X., Guo, R., Zhou, H., Liu, C., & Wan, E. C. K. (2008) · Immunological Reviews · doi:10.1111/j.1600-065x.2008.00647.x · Cited by 113
TCR Signaling in T Cell Memory
Daniëls, M. A., & Teixeiro, E. (2015) · Frontiers in Immunology · doi:10.3389/fimmu.2015.00617 · Cited by 111
Protein kinase C-θ: signaling from the center of the T-cell synapse
Arendt, C., Albrecht, B., Soos, T. J., & Littman, D. R. (2002) · Current Opinion in Immunology · doi:10.1016/s0952-7915(02)00346-1 · Cited by 103
The p38 mitogen-activated protein kinase signaling cascade in CD4 T cells.
Dodeller, F., & Schulze‐Koops, H. (2006) · Arthritis Research & Therapy · doi:10.1186/ar1905 · Cited by 103
Expression of GATA‐3 During Lymphocyte Differentiation and Mouse Embryogenesis
Oosterwegel, M. A., Timmerman, J. J., Leiden, J. M., & Clevers, H. C. (1992) · Journal of Immunology Research · doi:10.1155/1992/27903 · Cited by 102
Ras - a versatile cellular switch
Rommel, C., & Hafen, E. (1998) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(98)80111-1 · Cited by 101
STIM1 and STIM2‐mediated Ca2+ influx regulates antitumour immunity by CD8+ T cells
Weidinger, C., Shaw, P. J., & Feske, S. (2013) · EMBO Molecular Medicine · doi:10.1002/emmm.201302989 · Cited by 100
Synergistic control of T cell development and tumor suppression by diacylglycerol kinase α and ζ
Guo, R., Wan, E. C. K., Carpenter, J. H., Mousallem, T. I., Boustany, R., Kuan, C.-T., Burks, A. W., & Zhong, X.-P. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0711856105 · Cited by 97
Spatiotemporal Regulation of ERK2 by Dual Specificity Phosphatases
Caunt, C. J., Armstrong, S. P., Rivers, C. A., Norman, M. R., & McArdle, C. A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801500200 · Cited by 96
β-Selection-Induced Proliferation Is Required for αβ T Cell Differentiation
Kreslavsky, T., Gleimer, M., Miyazaki, M., Choi, Y. J., Gagnon, É., Murre, C., Siciński, P., & von Boehmer, H. (2012) · Immunity · doi:10.1016/j.immuni.2012.08.020 · Cited by 96
The calcium/NFAT pathway: role in development and function of regulatory T cells
Oh‐hora, M., & Rao, A. (2009) · Microbes and Infection · doi:10.1016/j.micinf.2009.04.008 · Cited by 90
Spatiotemporal Patterning During T Cell Activation Is Highly Diverse
Singleton, K. L., Roybal, K. T., Sun, Y., Fu, G., Gascoigne, N. R. J., van Oers, N. S. C., & Wülfing, C. (2009) · Science Signaling · doi:10.1126/scisignal.2000199 · Cited by 90
Common-Lymphoid-Progenitor-Independent Pathways of Innate and T Lymphocyte Development
Ghaedi, M., Steer, C. A., Martínez-González, I., Halim, T. Y. F., Abraham, N. B., & Takei, F. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.03.039 · Cited by 87
The signaling symphony: T cell receptor tunes cytokine-mediated T cell differentiation
Huang, W., & August, A. (2014) · Journal of Leukocyte Biology · doi:10.1189/jlb.1ri0614-293r · Cited by 85
Kaga, S., Ragg, S. J., Rogers, K. A., & Ochi, A. (1998) · The Journal of Immunology · doi:10.4049/jimmunol.160.9.4182 · Cited by 79
Negative regulation of lymphocyte development and function by the Cbl family of proteins
Huang, F., & Gu, H. (2008) · Immunological Reviews · doi:10.1111/j.1600-065x.2008.00655.x · Cited by 76
The Ubiquitin System in Immune Regulation
Park, Y., Jin, H., Aki, D., Lee, J., & Liu, Y. (2014) · Advances in immunology · doi:10.1016/b978-0-12-800147-9.00002-9 · Cited by 71
Rhee, J., Park, S.-H., Kim, S., Kim, J.-H., Ha, C., Chun, C.-H., & Chun, J.-S. (2016) · Annals of the Rheumatic Diseases · doi:10.1136/annrheumdis-2015-208953 · Cited by 65
Self-citationDiacylglycerol Kinases (DGKs): Novel Targets for Improving T Cell Activity in Cancer
Riese, M. J., Moon, E. K., Johnson, B. D., & Albelda, S. Μ. (2016) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2016.00108 · Cited by 65
Signal transduction pathways involving RAS
Wiesmüller, L., & Wittinghofer, F. (1994) · Cellular Signalling · doi:10.1016/0898-6568(94)90030-2 · Cited by 63
Saito, T., & Germain, R. N. (1987) · Nature · doi:10.1038/329256a0 · Cited by 60
Protein Kinase C η Is Required for T Cell Activation and Homeostatic Proliferation
Fu, G., Hu, J., Niederberger-Magnenat, N., Rybakin, V., Casas, J., Yachi, P. P., Feldstein, S., Ma, B., Hoerter, J. A. H., Ampudia, J., et al. (2011) · Science Signaling · doi:10.1126/scisignal.2002058 · Cited by 58
Diacylglycerol kinase as a possible therapeutic target for neuronal diseases
Shirai, Y., & Saito, N. (2014) · Journal of Biomedical Science · doi:10.1186/1423-0127-21-28 · Cited by 54
Development of T‐leukaemias in CD45 tyrosine phosphatase‐deficient mutant lck mice
Baker, M., Gamble, J., Tooze, R. M., et al. (2000) · The EMBO Journal · doi:10.1093/emboj/19.17.4644 · Cited by 54
Bertin, S., Lozano‐Ruiz, B., Bachiller, V., García‐Martinez, I., Herdman, S., Zapater, P., Francés, R., Such, J. M., Lee, J., Raz, E., et al. (2014) · Mucosal Immunology · doi:10.1038/mi.2014.84 · Cited by 51
Differential Regulation of Primary and Memory CD8 T Cell Immune Responses by Diacylglycerol Kinases
Shin, J., O’Brien, T. F., Grayson, J. M., & Zhong, X. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1102265 · Cited by 46
Maru, S. Y., Jin, G., Schell, T. D., & Lukacher, A. E. (2017) · PLoS Pathogens · doi:10.1371/journal.ppat.1006318 · Cited by 44
Kang, J., Park, S., Jeong, S. P., Han, M., Lee, C., Lee, K. M., Kim, N., Song, M., Choi, M., Ye, M., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1502166113 · Cited by 41
Self-citationKonicek, B. W., Xia, X., Rajavashisth, T. B., & Harrington, M. A. (1998) · DNA and Cell Biology · doi:10.1089/dna.1998.17.799 · Cited by 38
NF-κB Activation in T Helper 17 Cell Differentiation
Park, S., Cho, G., & Park, S. (2014) · Immune Network · doi:10.4110/in.2014.14.1.14 · Cited by 37
Self-citationYao, X. R., Flaswinkel, H., Reth, M. G., & Scott, D. W. (1995) · The Journal of Immunology · doi:10.4049/jimmunol.155.2.652 · Cited by 33
New Insights into the RNA-Binding and E3 Ubiquitin Ligase Activities of Roquins
Zhang, Q., Fan, L., Hou, F., Dong, A., Wang, Y., & Tong, Y. (2015) · Scientific Reports · doi:10.1038/srep15660 · Cited by 30
Iborra, S., Ramos, M., Arana, D. M., Lázaro, S., Aguilar, F., Santos, E., López, D., Fernández-Malavé, E., & Val, M. D. (2013) · The Journal of Experimental Medicine · doi:10.1084/jem.20112495 · Cited by 28
Molecular mechanisms of cancer.
Koeffler, H. P., McCormick, F. P., & Denny, C. T. (1991) · PubMed Central · Cited by 28
TCRA Gene Rearrangement in Immature Thymocytes in Absence of CD3, Pre-TCR, and TCR Signaling
Mancini, S. J. C., Candéias, S. M., Santo, J. P. D., Ferrier, P., Marche, P. N., & Jouvin‐Marche, E. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.167.8.4485 · Cited by 27
So, T., & Croft, M. (2012) · Frontiers in Immunology · doi:10.3389/fimmu.2012.00133 · Cited by 24
BATF regulates collagen-induced arthritis by regulating T helper cell differentiation
Park, S., Rhee, J., Kim, S., Kang, J., Kwak, J.-S., Son, Y., Choi, W.-S., Park, S., & Chun, J. (2018) · Arthritis Research & Therapy · doi:10.1186/s13075-018-1658-0 · Cited by 23
Self-citationThe Kinase PDK1 Is Essential for B-Cell Receptor Mediated Survival Signaling
Park, S., Long, M., Kang, J., Kim, W., Lee, C., Im, S., Strickland, I., Schulze‐Luehrmann, J., Hayden, M. S., & Ghosh, S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0055378 · Cited by 22
Self-citationDeltex1 Promotes Protein Kinase Cθ Degradation and Sustains Casitas B-Lineage Lymphoma Expression
Hsu, T.-S., Hsiao, H.-W., Wu, P.-J., Liu, W., & Lai, M. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1301416 · Cited by 21
Kang, J., Jeong, S. P., Park, D., Hayden, M. S., Ghosh, S., & Park, S. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1202923 · Cited by 17
Self-citationPKCθ-Mediated PDK1 Phosphorylation Enhances T Cell Activation by Increasing PDK1 Stability
Kang, J., Choi, H., Yang, T., Cho, S. K., Park, Z., & Park, S. (2017) · Molecules and Cells · doi:10.14348/molcells.2017.2236 · Cited by 10
Self-citationProtein kinase C theta affects Ca2+ mobilization and NFAT cell activation in primary mouse T cells.
Pfeifhofer, C., Kofler, K., Gruber, T., Tabrizi, N. G., Lutz, C., Maly, K., Leitges, M., & Baier, G. (2003) · Max Planck Institute for Plasma Physics · Cited by 10
The Role of Diacylglycerol Kinases in T Cell Anergy
Zhong, X. P., Olenchock, B. A., & Koretzky, G. A. (2008) · Ernst Schering Research Foundation workshop/Ernst Schering Foundation Symposium proceedings · doi:10.1007/2789_2007_073 · Cited by 9
Short peptides sensitize target cells to CTL specific for the MHC class Ib molecule, H2-M3
Dabhi, V. M., & Fischer Lindahl, K. (1998) · European Journal of Immunology · doi:10.1002/(sici)1521-4141(199811)28:11<3773::aid-immu3773>3.0.co;2-b
Research works printed but not linked: 1
- Kammerer, R., Hahn, S., Singer, B. B., Luo, J. S. & von Kleist, S. Biliary glycoprotein (CD66a), a cell adhesion molecule of the immunoglobulin superfamily, on human lymphocytes: structure, expression and involvement in T cell activation. Eur. J. Immunol. 28, 3664–3674 (1998). · DOI
Cited by
Bazioti, V., La Rose, A. M., Maassen, S., Bianchi, F., de Boer, R., Halmos, B., Dabral, D., Guilbaud, E., Flohr-Svendsen, A., Groenen, A. G., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31135-4 · Cited by 65
Insulin Signaling in Arthritis
Tripolino, C., Ciaffi, J., Pucino, V., Ruscitti, P., van Leeuwen, N., Borghi, C., Giacomelli, R., Meliconi, R., & Ursini, F. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.672519 · Cited by 46
The Role of RhoH in TCR Signalling and Its Involvement in Diseases
Ahmad Mokhtar, A. M., Hashim, I. F., Mohd Zaini Makhtar, M., Salikin, N. H., & Amin-Nordin, S. (2021) · Cells · doi:10.3390/cells10040950 · Cited by 25
PmVAE: learning interpretable single-cell representations with pathway modules
Gut, G., Stark, S. G., Rätsch, G., & Davidson, N. R. (2021) · doi:10.1101/2021.01.28.428664 · Cited by 24
Thioamide Analogues of MHC I Antigen Peptides
Gibadullin, R., Morris, R. K., Niu, J., Sidney, J., Sette, A., & Gellman, S. H. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.3c05300 · Cited by 17
Metadata
- Authors
- Hwang, J.-R., Byeon, Y., Kim, D., & Park, S.-G.
- ORCID
- Park, Sung-Gyoo
- Venue
- Experimental & Molecular Medicine
- Published
- 2020-05
- Volume
- 52
- Issue
- 5
- Pages
- 750-761
- ISSN
- 1226-3613
- 2092-6413
- PMC
- PMC7272404
- Cited by
- 470
- References
- 182
- Language
- en
- Licence
- creativecommons.org/licenses/by/4.0 (tdm)
- creativecommons.org/licenses/by/4.0 (vor, 20 d)
- Funders
- National Research Foundation of Korea (NRF-2016R1A5A1007318, NRF-2017R1E1A1A01074299)
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.