The DOI matches its Crossref record; 37 of the 38 references it cites were found in a registry or an index.
SHP2 inhibition triggers anti-tumor immunity and synergizes with PD-1 blockade
Open accessAbstract
Tyrosine phosphatase SHP2 is a promising drug target in cancer immunotherapy due to its bidirectional role in both tumor growth promotion and T-cell inactivation. Its allosteric inhibitor SHP099 is known to inhibit cancer cell growth both in vitro and in vivo. However, whether SHP099-mediated SHP2 inhibition retards tumor growth in vivo via anti-tumor immunity remains elusive. To address this, a CT-26 colon cancer xenograft model was established in mice since this cell line is insensitive to SHP099. Consequently, SHP099 minimally affected CT-26 tumor growth in immuno-deficient nude mice, but significantly decreased the tumor burden in CT-26 tumor-bearing mice with intact immune system. SHP099 augmented anti-tumor immunity, as shown by the elevated proportion of CD8+IFN-γ+ T cells and the upregulation of cytotoxic T-cell related genes including Granzyme B andPerforin, which decreased the tumor load. In addition, tumor growth in mice with SHP2-deficient T-cells was markedly slowed down because of enhanced anti-tumor responses. Finally, the combination of SHP099 and anti-PD-1 antibody showed a higher therapeutic efficacy than either monotherapy in controlling tumor growth in two colon cancer xenograft models, indicating that these agents complement each other. Our study suggests that SHP2 inhibitor SHP099 is a promising candidate drug for cancer immunotherapy.
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
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
“SHP2 inhibitor enhanced the efficacy of α-PD-1 in murine tumor models [252–254].”
From Combination strategies with PD-1/PD-L1 blockade: current advances and future directions (2022) · cites this paper as [254]
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
PD-1 and PD-L1 Immune Checkpoint Blockade to Treat Breast Cancer
Hartkopf, A. D., Taran, F., Wallwiener, M., Walter, C. B., Krämer, B., Grischke, E., & Brucker, S. Y. (2016) · Breast Care · doi:10.1159/000453569 · Cited by 30,989
The blockade of immune checkpoints in cancer immunotherapy
Pardoll, D. M. (2012) · Nature Reviews Cancer · doi:10.1038/nrc3239 · Cited by 13,838
Molecular mechanisms of T cell co-stimulation and co-inhibition
Chen, L., & Flies, D. B. (2013) · Nature Reviews Immunology · doi:10.1038/nri3405 · Cited by 3,114
CTLA-4 and PD-1 Receptors Inhibit T-Cell Activation by Distinct Mechanisms
Parry, R. V., Chemnitz, J. M., Frauwirth, K. A., Lanfranco, A. R., Braunstein, I., Kobayashi, S. V., Linsley, P. S., Thompson, C. B., & Riley, J. L. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.21.9543-9553.2005 · Cited by 1,931
T cell costimulatory receptor CD28 is a primary target for PD-1–mediated inhibition
Hui, E., Cheung, J., Zhu, J., Su, X., Taylor, M. J., Wallweber, H. A., Sasmal, D. K., Huang, J., Kim, J. M., Mellman, I., et al. (2017) · Science · doi:10.1126/science.aaf1292 · Cited by 1,689
Yokosuka, T., Takamatsu, M., Kobayashi-Imanishi, W., Hashimoto-Tane, A., Azuma, M., & Saito, T. (2012) · Journal of Experimental Medicine · doi:10.1084/jem.20112741 · Cited by 1,161
Crystal Structure of the Tyrosine Phosphatase SHP-2
Hof, P., Pluskey, S., Dhe‐Paganon, S., Eck, M. J., & Shoelson, S. E. (1998) · Cell · doi:10.1016/s0092-8674(00)80938-1 · Cited by 997
LAG 3 ( CD 223) as a cancer immunotherapy target
Andrews, L. P., Marciscano, A. E. E., Drake, C. G., & Vignali, D. A. A. (2017) · Immunological Reviews · doi:10.1111/imr.12519 · Cited by 980
Allosteric inhibition of SHP2 phosphatase inhibits cancers driven by receptor tyrosine kinases
Chen, Y.-N. P., LaMarche, M. J., Chan, H. M., Fekkes, P., Garcia-Fortanet, J., Acker, M. G., Antonakos, B., Chen, C. H.-T., Chen, Z., Cooke, V. G., et al. (2016) · Nature · doi:10.1038/nature18621 · Cited by 925
Melanoma Cell-Intrinsic PD-1 Receptor Functions Promote Tumor Growth
Kleffel, S., Posch, C., Barthel, S. R., Mueller, H., Schlapbach, C., Guenova, E., Elco, C. P., Lee, N., Juneja, V. R., Zhan, Q., et al. (2015) · Cell · doi:10.1016/j.cell.2015.08.052 · Cited by 672
Flagged first, then by citations
1 of the 38 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Items 101–195 of 195
Oncogenic Tyrosine Phosphatases: Novel Therapeutic Targets for Melanoma Treatment
Pardella, E., Pranzini, E., Leo, A., Taddei, M. L., Paoli, P., & Raugei, G. (2020) · Cancers · doi:10.3390/cancers12102799 · Cited by 14
Enhancing Adoptive Cell Therapy by T Cell Loading of SHP2 Inhibitor Nanocrystals before Infusion
Li, X., Halldórsdóttir, H. R., Weller, S., Colliander, A., Bak, M., Kempen, P. J., Clergeaud, G., & Andresen, T. L. (2022) · ACS Nano · doi:10.1021/acsnano.2c03311 · Cited by 13
Sui, Y., Shen, Z., Li, X., Lu, Y., Feng, S., Ma, R., Wu, J., Jing, C., Wang, Z., Feng, J., et al. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-06941-x · Cited by 13
Self-citationTargeting SHP2 Signaling in Lung Cancer
Imbody, D. J., Arce-Ruiz, K. M., Solanki, H. S., Haura, E. B., & Pellini, B. (2023) · Journal of Thoracic Oncology · doi:10.1016/j.jtho.2023.08.009 · Cited by 12
Protein tyrosine phosphatases as emerging targets for cancer immunotherapy
Qu, Z., Dong, J., & Zhang, Z. (2023) · British Journal of Pharmacology · doi:10.1111/bph.16304 · Cited by 12
Zhu, J., Li, X., Chen, W., Zuo, Z., Gong, Q., Hu, J., Huang, K., Liu, W., Gu, Y., Xu, Q., et al. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103796 · Cited by 12
Self-citationDesign of novel SHP2 inhibitors using Topomer CoMFA, HQSAR analysis, and molecular docking
Tong, J., Luo, D., Zhang, X., & Bian, S. (2020) · Structural Chemistry · doi:10.1007/s11224-020-01677-8 · Cited by 12
A small molecule inhibitor targeting SHP2 mutations for the lung carcinoma
Nian, Q., Zeng, J., Li, H., Chen, Y., Zhang, Z., Rodrigues‐Lima, F., Zhao, L., Feng, X., & Shi, J. (2021) · Chinese Chemical Letters · doi:10.1016/j.cclet.2021.01.002 · Cited by 12
Feng, H., Chen, Y., Xie, Z., Jiang, J., Zhong, Y., Guo, W., Yan, W., Lv, Z., Lu, D., Liang, H., et al. (2021) · Thoracic Cancer · doi:10.1111/1759-7714.14137 · Cited by 11
Self-citationAllosteric modulation of SHP2: Quest from known to unknown
Wang, N., Zhu, S., Lv, D., Wang, Y., Khawar, M. B., & Sun, H. (2023) · Drug Development Research · doi:10.1002/ddr.22100 · Cited by 11
Lam, W., Hu, R., Liu, S.-H., Cheng, P., & Cheng, Y. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.1095186 · Cited by 11
Emerging immunological strategies: recent advances and future directions
Zhao, H., Luo, F., Xue, J., Li, S., & Xu, R. (2021) · Frontiers of Medicine · doi:10.1007/s11684-021-0886-x · Cited by 12
Purine metabolites promote ectopic new bone formation in ankylosing spondylitis
Zhang, S., Fan, Z., Ouyang, Z., Sun, H., Song, Y., Yu, H., Xu, Q., Liu, S., Sun, Y., & Shao, F. (2023) · International Immunopharmacology · doi:10.1016/j.intimp.2023.109810 · Cited by 9
Self-citationResearch progress in bifunctional small molecules for cancer immunotherapy
Cheng, B., Li, H., Hong, Y., Zhou, Y., Chen, J., Shao, C., & Kong, Z. (2025) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2025.117289 · Cited by 9
Zhong, Y., Lu, Y., Li, J., Ren, Q., Fan, Y., Meng, X., Shao, J., & Qian, H. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c02682 · Cited by 10
Self-citationLiu, P., & Chen, J. (2025) · World Journal of Gastrointestinal Oncology · doi:10.4251/wjgo.v17.i7.107380 · Cited by 10
Current advances and future directions of combined ICIs and TILs in solid tumors
Wang, Y., Ding, Q., & Wei, J. (2025) · Cancer Letters · doi:10.1016/j.canlet.2025.218145 · Cited by 9
Protein Tyrosine Phosphatase SHP2 Controls Interleukin-8 Expression in Breast Cancer Cells
Amante, R. J., der Maur, P. A., Richina, V., Sethi, A., Iešmantavičius, V., Bonenfant, D., Aceto, N., & Bentires‐Alj, M. (2022) · Journal of Mammary Gland Biology and Neoplasia · doi:10.1007/s10911-022-09521-x · Cited by 9
Tumor Cell–Autonomous SHP2 Contributes to Immune Suppression in Metastatic Breast Cancer
Chen, H., Cresswell, G. M., Libring, S., Ayers, M. G., Miao, J., Zhang, Z., Solorio, L., Ratliff, T. L., & Wendt, M. K. (2022) · Cancer Research Communications · doi:10.1158/2767-9764.crc-22-0117 · Cited by 9
Combination of apatinib with apo-IDO1 inhibitor for the treatment of colorectal cancer
Yu, L., Wang, Y., He, Y., Zhong, H., Ge, S., Zou, Y., Lai, Y., Xu, Q., Gao, J., Liu, W., et al. (2022) · International Immunopharmacology · doi:10.1016/j.intimp.2022.109233 · Cited by 9
Self-citationYu, L., Xu, L., Chen, Y., Rong, Y., Zou, Y., Ge, S., Wu, T., Lai, Y., Xu, Q., Guo, W., et al. (2024) · The Journal of Immunology · doi:10.4049/jimmunol.2300545 · Cited by 8
Self-citationSetting sail: Maneuvering SHP2 activity and its effects in cancer
Welsh, C. L., Allen, S., & Madan, L. K. (2023) · Advances in cancer research · doi:10.1016/bs.acr.2023.03.003 · Cited by 9
Exploration of T cell immune responses by expression of a dominant-negative SHP1 and SHP2
Taylor, J., Bulek, A. M., Gannon, I., Robson, M. P., Kokalaki, E., Grothier, T., McKenzie, C., El-Kholy, M., Stavrou, M., Traynor-White, C., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1119350 · Cited by 8
Wang, S., Battigelli, A., Alkekhia, D., Fairman, A. E., Antoci, V., Yang, W., Moore, D., & Shukla, A. (2020) · RSC Advances · doi:10.1039/d0ra03864d · Cited by 8
Apo-Form Selective Inhibition of IDO for Tumor Immunotherapy
Liu, W., Zou, Y., Li, K., Zhong, H., Yu, L., Ge, S., Lai, Y., Dong, X., Xu, Q., & Guo, W. (2022) · The Journal of Immunology · doi:10.4049/jimmunol.2100938 · Cited by 9
Self-citationAllosteric SHP2 inhibition enhances regorafenib's effectiveness in colorectal cancer treatment
Han, X., Wang, W., Wang, R., Zhang, W., Zhu, L., Xu, Q., Guo, W., & Gu, Y. (2024) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2024.149812 · Cited by 7
Self-citationWang, K., Zhang, X., Hu, Y., Guo, J., Shen, G., Zhang, K., Jiang, S., & Wang, T. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.117036 · Cited by 7
Napoleon, J. V., Zhang, B., Luo, Q., Srinivasarao, M., & Low, P. S. (2022) · Angewandte Chemie International Edition · doi:10.1002/anie.202113341 · Cited by 7
Song, X., & Li, J. (2022) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2022/9942373 · Cited by 7
The insulin receptor endocytosis
Wu, J., Park, S. H., & Choi, E. (2022) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2022.06.020 · Cited by 7
PD-L1/SHP2 dual PROTACs inhibit melanoma by enhancing T-cell killing activity
Liu, Y., Liang, J., Zheng, M., Song, H., Chen, L., & Li, H. (2024) · Chinese Chemical Letters · doi:10.1016/j.cclet.2024.110317 · Cited by 8
Breaking the mold: Overcoming resistance to immune checkpoint inhibitors
Zhao, M., Yan, C.-Y., Wei, Y.-N., & Zhao, X. (2023) · Antiviral Research · doi:10.1016/j.antiviral.2023.105720 · Cited by 7
Self-citationZhou, Z., Lin, Z., Wang, M., Wang, L., Ji, Y., Yang, J., Yang, Y., Zhu, G., & Liu, T. (2024) · European journal of medical research · doi:10.1186/s40001-023-01587-5 · Cited by 6
Shp2 in Alveolar Macrophages Regulates Macrophage I Phenotype in Acute Lung Injury
Wang, D., & Cao, Q. (2022) · International Journal of Toxicology · doi:10.1177/10915818221105227 · Cited by 6
Yamaguchi, H., Nagamura, Y., & Miyazaki, M. (2022) · Cancers · doi:10.3390/cancers14153750 · Cited by 6
Discovery of novel substituted pyridine carboxamide derivatives as potent allosteric SHP2 inhibitors
Lv, X., Li, P., Chen, Z., Huang, S., Zhang, S., Ji, B., Liu, J., Du, T., Zhang, T., Chen, X., et al. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116830 · Cited by 4
Matous, J. G., Snook, J. P., Contreras, N. A., Ramstead, A. G., Charley, K. R., Kolawole, E. M., Kisiolek, J. N., Flint, K. A., Soedel, A. J., Robinson, B., et al. (2025) · Journal for ImmunoTherapy of Cancer · doi:10.1136/jitc-2024-010879 · Cited by 5
Zhu, C., Li, L., Yu, Y., Wang, X., Shi, Y., Gao, Y., Chen, K., Liu, X., Cui, Y., Zhang, T., et al. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.117078 · Cited by 5
Li, X., Wang, X., Zhao, M., Zhang, H., & Liu, C. (2022) · Molecules · doi:10.3390/molecules27175678 · Cited by 5
Self-citationMoreno, S. F. L., Lenz, S. A., Casso-Chapa, B., Paniagua-Bojorges, A., Kim, J. H., Palaskas, N. L., Nead, K. T., Samanthapudi, V. S. K., Mejia, G. F., Hoang, O. N., et al. (2025) · Antioxidants · doi:10.3390/antiox14121388 · Cited by 5
Wang, X., Shao, X., Wang, M., Li, Y., Geng, T., Wang, Y., Ding, X., He, Y., Jin, H., Sun, Y., et al. (2025) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2025.117687 · Cited by 4
Self-citationMarotta, M., Zirpoli, S., Prevete, N., Simone, C. D., Cristofano, A. D., Liotti, F., & Melillo, R. M. (2025) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2025.118384 · Cited by 4
Zhai, Z., Zhang, X., Zhou, L., Lin, Z., Kuang, N., Li, Q., Ma, Q., Tao, H., Gao, J., Ma, S., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac872 · Cited by 4
Li, H., Jing, Y.-M., Xue, S., Tang, M., Shen, H., Li, X., Wang, Z., & Su, F. (2024) · World Journal of Gastrointestinal Oncology · doi:10.4251/wjgo.v16.i9.3913 · Cited by 4
Emerging roles of KIR2DL4 in cancer immunotherapy
Li, W., Zheng, G., & Zhang, S. (2025) · Breast Cancer · doi:10.1007/s12282-025-01738-y · Cited by 3
A first-in-human phase 1 study of the SHP2 inhibitor BBP-398 in patients with advanced solid tumors
Falchook, G. S., Xavier, C. B., Veenhuyzen, D. F. V., Malhotra, J. D., Sadeghi, S., Kalebasty, A. R., Wood, L., Rahman, F., Li, E., Pak, Y., et al. (2026) · npj Precision Oncology · doi:10.1038/s41698-026-01340-1 · Cited by 3
Chen, M., Zhang, L., Lin, W., Zhou, Z., Wang, Y., Wang, L., Gu, H., Li, J., & Xu, Z. P. (2025) · Journal of Controlled Release · doi:10.1016/j.jconrel.2025.113889 · Cited by 3
Song, Y., Zhu, H., Wei, J., & Yin, S. (2025) · Cancer Cell International · doi:10.1186/s12935-025-03855-2 · Cited by 3
Wang, J., Zhang, L., Pratilas, C. A., & Llosa, N. J. (2021) · Journal of Cancer Immunology · doi:10.33696/cancerimmunol.3.038 · Cited by 4
Luo, H., Wu, J., Yan, Y., Xu, D., Zhang, J., Zhou, X., Yang, G., & Zhong, X. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1681539 · Cited by 2
Zhang, Y., Zhu, C., Si, C., Lin, Y., Guo, Q., Zhou, H., & Yu, Z. (2026) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2026.118708 · Cited by 3
Sahu, P., Mitra, A., & Ganguly, A. (2024) · International review of cytology · doi:10.1016/bs.ircmb.2024.01.005 · Cited by 2
Wang, M., Yu, K., Fu, W., & Yang, L. (2024) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2024.150262 · Cited by 2
Combined SHP2 and ERK inhibition for the treatment of KRAS-driven Pancreatic Ductal AdenocarcinomaPreprint
Ciecielski, K. J., Mulero‐Sánchez, A., Berninger, A., Cañas, L. R., Bosma, A. R., Görgülü, K., Wu, N., Diakopoulos, K. N., Kaya-Aksoy, E., Ruess, D. A., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.12.14.472574 · Cited by 2
Zhang, M., Wu, S., Liu, M., Li, H., Wang, L., Duan, F., Han, R., Shan, C., Jiang, Z., Liao, J., et al. (2025) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2025.117988 · Cited by 1
Davoudi, Z., Dexheimer, T. S., Coussens, N. P., Silvers, T. E., Fox, R. G., Kemp, S. B., Juneja, P., Morris, J., Hollingshead, M. G., Takebe, N., et al. (2025) · Cancer Research Communications · doi:10.1158/2767-9764.crc-24-0582 · Cited by 2
Schneider, J. L., Muzikansky, A., Krueger, E., Gainor, J. F., Lin, J. J., Symes, S., Shaw, A. T., & Dagogo‐Jack, I. (2026) · Lung Cancer · doi:10.1016/j.lungcan.2026.108945 · Cited by 1
Zhang, Y., Wang, H., Wei, Y., Pan, Y., Song, X., Shao, J., Yu, L., Shi, T., & Wang, Y. (2026) · eLife · doi:10.7554/elife.104060.3 · Cited by 1
Zhu, C., Zhang, Y., Jin, Y., Yu, Y., Zhang, N., Yang, L., Gao, Y., Zhang, M., Shi, Y., Gao, Y., et al. (2026) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c03184 · Cited by 2
Wang, S., Zhao, X., Dong, J. X., Zhang, J., Wang, Y., Jin, H., Jiang, X., Chen, L., Zhang, M., Ji, L., et al. (2026) · Journal of Translational Medicine · doi:10.1186/s12967-026-08477-4 · Cited by 1
Napoleon, J. V., Zhang, B., Luo, Q., Srinivasarao, M., & Low, P. S. (2022) · Angewandte Chemie · doi:10.1002/ange.202113341 · Cited by 1
Hsu, M.-F., Koike, S., Chen, C.-S., Najjar, S. M., Meng, T., & Haj, F. G. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.116590 · Cited by 1
Davoudi, Z., Dexheimer, T. S., Coussens, N. P., Silvers, T. E., Morris, J., Takebe, N., Doroshow, J. H., & Teicher, B. A. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.11.17.623998 · Cited by 1
Metabolic Profile of Adaptive Immune Cells
Domínguez-Amorocho, O. A., Soto‐Heredero, G., & Mittelbrunn, M. (2021) · Springer eBooks · doi:10.1007/978-3-030-86684-6_6
Coleman, J. L. (2020) · UEA Digital Repository (University of East Anglia)
Research Progress in Allosteric SHP2 Inhibitors
堵, 桐. (2022) · Hans Journal of Medicinal Chemistry · doi:10.12677/hjmce.2022.102021
Therapeutic Effect of Shp2 Inhibition Combined with Regorafenib in Advanced Colorectal CancerPreprint
Han, X., Wang, W., Zhang, W., Zhu, L., Xu, L., Li, X., Xu, Q., Guo, W., & Gu, Y. (2023) · SSRN Electronic Journal · doi:10.2139/ssrn.4534174
Self-citationLv, X., Li, P., Chen, Z., Huang, S., Du, T., Ji, B., Zhang, S., Liu, J., Zhang, T., Chen, X., et al. (2024) · SSRN Electronic Journal · doi:10.2139/ssrn.4871858
Network mechanism of opioids in treating abdominal pain caused by T-cell lymphoma
Li, X.-Y. (2024) · New medicine. · doi:10.61958/nmsg1394
Paired CRISPR screens to map gene regulation in cis and transPreprint
Xue, X., Gajic, Z. Z., Caragine, C. M., Legut, M., Walker, C. R., Kim, J. Y. S., Wang, X., Yan, R., Wessels, H., Lu, C., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.11.27.625752
Zhang, Y., Wang, H., Wei, Y., Pan, Y., Song, X., Shi, T., Shao, J., Yu, L., Liu, B., Wang, Y., et al. (2025) · eLife · doi:10.7554/elife.104060.1
Zhang, Y., Wang, H., Wei, Y., Pan, Y., Song, X., Shao, J., Yu, L., Shi, T., & Wang, Y. (2025) · eLife · doi:10.7554/elife.104060
Wang, X., Shao, X., Wang, M., Li, Y., Geng, T., Wang, Y., Ding, X., He, Y., Jin, H., Sun, Y., et al. (2025) · SSRN Electronic Journal · doi:10.2139/ssrn.5122801
Self-citationRecent advances in phosphatase drug discovery and development
LaMarche, M. J. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-29808-0.00065-0
Inhibition of SHP-1 /2 blocks antigen cross-presentation by human macrophages and dendritic cellsPreprint
de Wit, A. S., Warner, H. M., Huang, H., Verdoes, M., van den Bogaart, G., & Bianchi, F. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.21.683666
Discovery a plasiatine-based potent SHP2 activator as a potential anti-atherosclerotic agent
Ding, X., Geng, T., Li, Y., Pan, P., Li, Z., Li, Z., & Meng, X. (2025) · Chinese Chemical Letters · doi:10.1016/j.cclet.2025.112140
Self-citationBao, R., Stapor, D., & Luke, J. J. (2020) · Figshare · doi:10.6084/m9.figshare.13147225
Zhang, Y., Wang, H., Wei, Y., Pan, Y., Song, X., Shao, J., Yu, L., Shi, T., & Wang, Y. (2026) · eLife · doi:10.7554/elife.104060.2
Vladimirov, T., Bárány, L., Jeising, S., Schnell, O., Delev, D., & Heiland, D. H. (2026) · Research Square · doi:10.21203/rs.3.rs-9415669/v1
Probing 3‐Amino‐2 H ‐Azaindazoles as Allosteric Inhibitors of the Protein Tyrosine Phosphatase SHP2
Amoussa, M., Efrém, N., Li, F., Guo, Z., Roske, Y., Frank, K. J., Pach, S., Wolf, C. A., Bo, F., Lesina, M., et al. (2026) · ChemMedChem · doi:10.1002/cmdc.70341
Wang, K., Liu, Y., Zhang, Z., Hu, Y., Zhong, Y., Jiang, S., Zhang, X., Zhang, K., & Wang, T. (2026) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6c00353
Jin, X., Wang, B., Guo, H., Zhao, S. P., Zhang, W., & Yin, Z. (2026) · European journal of medical research · doi:10.1186/s40001-026-04825-8
Li, X., Duan, X., Liu, N., Tang, W., He, Y., Zhou, D., Yan, J., & Zhou, Y. (2026) · Cell Biochemistry and Function · doi:10.1002/cbf.70315
BindingDB (2022) · UC San Diego · doi:10.7270/q2cc14bb
BindingDB Entry 50018630: If small molecules immunotherapy comes, can the prime be far behind?
BindingDB (2024) · UC San Diego · doi:10.7270/q26h4np0
BindingDB (2025) · UC San Diego · doi:10.7270/q2hd81cs
BindingDB Entry 50022804: Advances in SHP2 tunnel allosteric inhibitors and bifunctional molecules.
BindingDB (2026) · UC San Diego · doi:10.7270/q2v98dw4
Metadata
- Authors
- Zhao, M., Guo, W., Wu, Y., Yang, C., Zhong, L., Deng, G., Zhu, Y., Liu, W., Gu, Y., Lu, Y., Kong, L., Meng, X., Xu, Q., & Sun, Y.
- Affiliations
- State Key Laboratory of Pharmaceutical Biotechnology (CN)
- Nanjing University of Chinese Medicine (CN)
- Peking University (CN)
- Jiangsu Province Hospital (CN)
- Corresponding author
- Meng, Xiangbao
- Xu, Qiang
- Sun, Yang
- ORCID
- Venue
- Acta Pharmaceutica Sinica B
- Publisher
- Elsevier BV
- Published
- 2019-03
- Volume
- 9
- Issue
- 2
- Pages
- 304-315
- ISSN
- 2211-3835 (ISSN-L)
- PMC
- PMC6437555
- OpenAlex
- W2891517856
- Cited by
- 190
- References
- 38
- Citations by year
- 2026: 15 · 2025: 25 · 2024: 25 · 2023: 18 · 2022: 37 · 2021: 27 · 2020: 33 · 2019: 10
- FWCI
- 6.23
- Type
- journal article
- Language
- en
- Update notices
- erratum (2025-05-01)
- Open access
- gold
- doi.org
- Licence
- Locations
- Acta Pharmaceutica Sinica B (publishedVersion, cc-by-nc-nd)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Natural Science Foundation of China (81673436, 81673437, 21472091, 81872877)
- Nanjing University
- Priority Academic Program Development of Jiangsu Higher Education Institutions
- State Key Laboratory of Pharmaceutical Biotechnology (KF-GN-201703)
- Jiangsu Key Laboratory for Pharmacology and Safety Evaluation of Chinese Materia Medica (JKLPSE201802)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Health Sciences › Medicine › Oncology › Cancer Immunotherapy and Biomarkers
- Life Sciences › Immunology and Microbiology › Immunology › Immunotherapy and Immune Responses
- Keywords
- SHP2, SHP099, protein tyrosine phosphatase inhibition, antitumor immunity, anti-PD-1 therapy, combination immunotherapy, colon cancer, CD8+ T cells, cytotoxic T lymphocytes, T cell exhaustion, allosteric inhibitors
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
