Affinity purification mass spectrometry analysis of PD-1 uncovers SAP as a new checkpoint inhibitor

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The X-linked lymphoproliferative-disease gene product SAP regulates signals induced through the co-receptor SLAM

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Melanoma Cell-Intrinsic PD-1 Receptor Functions Promote Tumor Growth

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Cutaneous, gastrointestinal, hepatic, endocrine, and renal side-effects of anti-PD-1 therapy

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Selective effects of PD-1 on Akt and Ras pathways regulate molecular components of the cell cycle and inhibit T cell proliferation

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Shp2 regulates SRC family kinase activity and Ras/Erk activation by controlling Csk recruitment.

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Structural and Functional Analysis of the Costimulatory Receptor Programmed Death-1

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SH2 domains prevent tyrosine dephosphorylation of the EGF receptor: identification of Tyr992 as the high‐affinity binding site for SH2 domains of phospholipase C gamma.

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Prognostic, therapeutic, and mechanistic implications of a mouse model of leukemia evoked by Shp2 (PTPN11) mutations

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Interaction landscape of membrane-protein complexes in Saccharomyces cerevisiae

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High-throughput Phenotyping of Lung Cancer Somatic Mutations

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The Programmed Death-1 Ligand 1:B7-1 Pathway Restrains Diabetogenic Effector T Cells In Vivo

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The programmed death 1/programmed death ligand 1 inhibitory pathway is up‐regulated in rheumatoid synovium and regulates peripheral T cell responses in human and murine arthritis

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X-linked lymphoproliferative syndromes: brothers or distant cousins?

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SLAM-Family Receptors: Immune Regulators with or without SAP-Family AdaptorsPreprint

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MouseMine: a new data warehouse for MGI

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Programmed death-1 concentration at the immunological synapse is determined by ligand affinity and availability

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SPAK kinase is a substrate and target of PKCθ in T‐cell receptor‐induced AP‐1 activation pathway

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PKC-theta-mediated signal delivery from the TCR/CD28 surface receptors

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A ‘three‐pronged’ binding mechanism for the SAP/SH2D1A SH2 domain: structural basis and relevance to the XLP syndrome

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Proteomic analysis of neurons microdissected from formalin-fixed, paraffin-embedded Alzheimer’s disease brain tissue

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14-3-3 Proteins Play a Role in the Cell Cycle by Shielding Cdt2 from Ubiquitin-Mediated Degradation

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The SH2 Domain is Required for Stable Phosphorylation of p561ck at Tyrosine 505, the Negative Regulatory Site

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Analysis of Protein Tyrosine Phosphatases and Substrates

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The Adaptor Protein SAP Directly Associates with CD3ζ Chain and Regulates T Cell Receptor Signaling

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The ShcD signaling adaptor facilitates ligand-independent phosphorylation of the EGF receptor

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Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes

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The coreceptor programmed death 1 inhibits T-cell adhesion by regulating Rap1

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Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes

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Association of a single nucleotide polymorphism in the SH2D1A intronic region with systemic lupus erythematosus

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SH2 Binding Site Protection Assay: A Method for Identification of SH2 Domain Interaction Partners by Exploiting SH2 Mediated Phosphosite Protection

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Immune checkpoint signaling and cancer immunotherapy

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Revisiting the PD-1 pathway

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The Diverse Function of PD-1/PD-L Pathway Beyond Cancer

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SHP2 inhibition diminishes KRASG12C cycling and promotes tumor microenvironment remodeling

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Molecular mechanism of SHP2 activation by PD-1 stimulation

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The Extrinsic and Intrinsic Roles of PD‐L1 and Its Receptor PD‐1: Implications for Immunotherapy Treatment

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KRAS4A directly regulates hexokinase 1

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Immune checkpoint molecules in natural killer cells as potential targets for cancer immunotherapy

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Interaction of SHP‐2 SH2 domains with PD‐1 ITSM induces PD‐1 dimerization and SHP‐2 activation

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Shp-2 Is Dispensable for Establishing T Cell Exhaustion and for PD-1 Signaling In Vivo

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Quantitative Interactomics in Primary T Cells Provides a Rationale for Concomitant PD-1 and BTLA Coinhibitor Blockade in Cancer Immunotherapy

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Targeting protein phosphatases in cancer immunotherapy and autoimmune disorders

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PD-1 and BTLA regulate T cell signaling differentially and only partially through SHP1 and SHP2

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Allosteric SHP2 inhibitors in cancer: Targeting the intersection of RAS, resistance, and the immune microenvironment

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Allosteric Inhibition of SHP2 Stimulates Antitumor Immunity by Transforming the Immunosuppressive Environment

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Proteomics in Drug Development: The Dawn of a New Era?

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Immune Checkpoint Receptors Signaling in T Cells

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T cell interactions with B cells during germinal center formation, a three‐step model

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SLAM-family receptors come of age as a potential molecular target in cancer immunotherapy

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Molecular features underlying differential SHP1/SHP2 binding of immune checkpoint receptors

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SHP-2 in Lymphocytes' Cytokine and Inhibitory Receptor Signaling

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Structure of the human clamp loader reveals an autoinhibited conformation of a substrate-bound AAA+ switch

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Cryo-EM structures reveal high-resolution mechanism of a DNA polymerase sliding clamp loader

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The depths of PD-1 function within the tumor microenvironment beyond CD8+ T cells

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Transcription-associated histone pruning demarcates macroH2A chromatin domains

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Shp-2 is critical for ERK and metabolic engagement downstream of IL-15 receptor in NK cells

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Bispecific antibody targeting TGF-β and PD-L1 for synergistic cancer immunotherapy

Li, T., Wang, X., Niu, M., Wang, M., Zhou, J., Wu, K., & Yi, M. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1196970 · Cited by 50 · see citing works

SLAMF6 deficiency augments tumor killing and skews toward an effector phenotype revealing it as a novel T cell checkpoint

Hajaj, E., Eisenberg, G., Klein, S., Frankenburg, S., Merims, S., David, I. B., Eisenhaure, T., Henrickson, S. E., Villani, A., Hacohen, N., et al. (2020) · eLife · doi:10.7554/elife.52539 · Cited by 43 · see citing works

The PD‐1 Interactome

Wang, Q., Bardhan, K., Boussiotis, V. A., & Patsoukis, N. (2021) · Advanced Biology · doi:10.1002/adbi.202100758 · Cited by 39 · see citing works

Surfaceome nanoscale organization and extracellular interaction networks.

Bausch-Fluck, D., Milani, E., & Wollscheid, B. (2019) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2018.09.020 · Cited by 35 · see citing works

Mitochondrial STAT3 regulates antioxidant gene expression through complex I‐derived NAD in triple negative breast cancer

Lahiri, T., Brambilla, L., Andrade, J., Askenazi, M., Ueberheide, B. M., & Levy, D. E. (2021) · Molecular Oncology · doi:10.1002/1878-0261.12928 · Cited by 35 · see citing works

Phosphotyrosine couples peptide binding and SHP2 activation via a dynamic allosteric network

Marasco, M., Kirkpatrick, J., Nanna, V., Sikorska, J., & Carlomagno, T. (2021) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2021.04.040 · Cited by 36 · see citing works

Small molecule inhibitors for cancer immunotherapy and associated biomarkers – the current status

Schlicher, L., Green, L. G., Romagnani, A., & Renner, F. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1297175 · Cited by 34 · see citing works

SLAM Associated Protein Signaling in T Cells: Tilting the Balance Toward Autoimmunity

Gartshteyn, Y., Askanase, A., & Mor, A. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.654839 · Cited by 35 · see citing works

Combination Approaches to Target PD-1 Signaling in Cancer

Moore, E. K., Strazza, M., & Mor, A. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.927265 · Cited by 32 · see citing works

Specificity and regulation of phosphotyrosine signaling through SH2 domains

Marasco, M., & Carlomagno, T. (2020) · Journal of Structural Biology X · doi:10.1016/j.yjsbx.2020.100026 · Cited by 31 · see citing works

Potential role of diacylglycerol kinases in immune-mediated diseases

Baldanzi, G., Ragnoli, B., & Malerba, M. (2020) · Clinical Science · doi:10.1042/cs20200389 · Cited by 31 · see citing works

Current insights and future prospects for the pathogenesis and treatment for rheumatoid arthritis

Koga, T., Kawakami, A., & Tsokos, G. C. (2021) · Clinical Immunology · doi:10.1016/j.clim.2021.108680 · Cited by 30 · see citing works

Programmed Cell Death-1 Receptor (PD-1)-Mediated Regulation of Innate Lymphoid Cells

Mallett, G., Laurence, A. D. J., & Amarnath, S. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20112836 · Cited by 31 · see citing works

Mass Spectrometry-Based Protein Complex Profiling in Time and Space.

Zheng, J.-N., Chen, X., Yang, Y., Tan, C. S., & Tian, R.-J. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.0c04332 · Cited by 22 · see citing works

SHP2 Targets ITK Downstream of PD-1 to Inhibit T Cell Function

Strazza, M., Adam, K. R., Lerrer, S., Straube, J., Sandigursky, S., Ueberheide, B. M., & Mor, A. (2021) · Inflammation · doi:10.1007/s10753-021-01437-8 · Cited by 23 · see citing works

PD-1 endocytosis unleashes the cytolytic potential of checkpoint blockade in tumor immunity

Saad, E. B., Oroya, A., Anto, N. P., Bachais, M., & Rudd, C. E. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114907 · Cited by 20 · see citing works

Transmembrane adaptor protein PAG is a mediator of PD-1 inhibitory signaling in human T cells

Strazza, M., Azoulay‐Alfaguter, I., Peled, M., Adam, K. R., & Mor, A. (2021) · Communications Biology · doi:10.1038/s42003-021-02225-8 · Cited by 21 · see citing works

EF Hand Domain Family Member D2 Is Required for T Cell Cytotoxicity

Peled, M., Dragovich, M. A., Adam, K. R., Strazza, M., Tocheva, A. S., Vega, I. E., & Mor, A. (2018) · The Journal of Immunology · doi:10.4049/jimmunol.1800839 · Cited by 19 · see citing works

Current studies and future promises of PD-1 signal inhibitors in cervical cancer therapy

Awadasseid, A., Zhou, Y., Zhang, K., Tian, K., Wu, Y., & Zhang, W. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.114057 · Cited by 18 · see citing works

Proteomics from compartment-specific APEX2 labeling in Mycobacterium tuberculosis reveals Type VII secretion substrates in the cell wall

Jaisinghani, N., Previti, M. L., Andrade, J., Askenazi, M., Ueberheide, B. M., & Seeliger, J. C. (2023) · Cell chemical biology · doi:10.1016/j.chembiol.2023.10.013 · Cited by 17 · see citing works

Regulation of CD4+ T Cell Signaling and Immunological Synapse by Protein Tyrosine Phosphatases: Molecular Mechanisms in Autoimmunity

Castro-Sánchez, P., Aguilar-Sopeña, Ó., Alegre-Gómez, S., Ramirez-Munoz, R., & Roda‐Navarro, P. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.01447 · Cited by 15 · see citing works

SAP interacts with CD28 to inhibit PD-1 signaling in T lymphocytes

Sandigursky, S., Philips, M. R., & Mor, A. (2020) · Clinical Immunology · doi:10.1016/j.clim.2020.108485 · Cited by 15 · see citing works

Allosteric inhibition of SHP2 rescues functional T-cell abnormalities in SAP deficiency

Panchal, N., Houghton, B. C., Vassalou, E., Thrasher, A. J., & Booth, C. (2022) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2022.06.021 · Cited by 13 · see citing works

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 · see citing works

Diacylglycerol Kinase alpha in X Linked Lymphoproliferative Disease Type 1

Velnati, S., Centonze, S., Girivetto, F., & Baldanzi, G. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22115816 · Cited by 11 · see citing works

VRK2 inhibition synergizes with PD-1 blockade to improve T cell responses

Peled, M., Tocheva, A. S., Adam, K. R., & Mor, A. (2021) · Immunology Letters · doi:10.1016/j.imlet.2021.03.007 · Cited by 11 · see citing works

Identification of Radil as a Ras binding partner and putative activator

Choi, B. H., Kou, Z., Colon, T. M., Chen, C., Chen, Y., & Dai, W. H. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100314 · Cited by 10 · see citing works

PD‐1‐induced proliferating T cells exhibit a distinct transcriptional signature

Strazza, M., Bukhari, S., Tocheva, A. S., & Mor, A. (2021) · Immunology · doi:10.1111/imm.13388 · Cited by 9 · see citing works

Quantifying the contribution of transcription factor activity, mutations and microRNAs to CD274 expression in cancer patients

Bruns, I. B., & Beltman, J. B. (2022) · Scientific Reports · doi:10.1038/s41598-022-08356-0 · Cited by 10 · see citing works

Role of the Crosstalk B:Neoplastic T Follicular Helper Cells in the Pathobiology of Nodal T Follicular Helper Cell Lymphomas

Sainz, T. P., Sahu, V., Gomez, J. A., Dcunha, N. J., Basi, A., Kettlun, C. S., Sarami, I., Burks, J. K., Sampath, D., & Vega, F. (2024) · Laboratory Investigation · doi:10.1016/j.labinv.2024.102147 · Cited by 8 · see citing works

Immunoaffinity microflow liquid chromatography/tandem mass spectrometry for the quantitation of PD1 and PD‐L1 in human tumor tissues

Zhu, Y., Zalaznick, J., Sleczka, B. G., Parrish, K. E., Yang, Z., Olah, T. V., & Shipkova, P. A. (2020) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.8896 · Cited by 7 · see citing works

In Vitro Assays to Study PD‐1 Biology in Human T Cells

Tocheva, A. S., Lerrer, S., & Mor, A. (2020) · Current Protocols in Immunology · doi:10.1002/cpim.103 · Cited by 7 · see citing works

Wiskott-Aldrich syndrome protein interacts and inhibits diacylglycerol kinase alpha promoting IL-2 induction

Velnati, S., Centonze, S., Rossino, G., Purghè, B., Antona, A., Racca, L., Mula, S., Ruffo, E., Malacarne, V., Malerba, M., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1043603 · Cited by 7 · see citing works

The SLAMF3 rs509749 polymorphism correlates with malignant potential in multiple myeloma

Ishibashi, M., Sunakawa-Kii, M., Kaito, Y., Kinoshita, R., Asayama, T., Kuribayashi-Hamada, Y., Inokuchi, K., Morita, R., & Tamura, H. (2020) · Experimental Hematology · doi:10.1016/j.exphem.2020.08.006 · Cited by 7 · see citing works

PD-1 protects expanding human T cells from premature restimulation-induced cell death by modulating TCR and CD28 signaling

Lee, K. P., Elster, S., Epstein, B. E., Lake, C. M., & Snow, A. L. (2026) · Cell Death and Disease · doi:10.1038/s41419-026-08530-6 · Cited by 6 · see citing works

Proteomic Investigation of Immune Checkpoints and Some of Their Inhibitors

Agostini, M., Traldi, P., & Hamdan, M. H. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25179276 · Cited by 6 · see citing works

Checkpoint Molecules in Rheumatology—or the Benefits of Being Exhausted

Greisen, S. R., & Deleuran, B. W. (2021) · Current Rheumatology Reports · doi:10.1007/s11926-021-00991-2 · Cited by 6 · see citing works

Experiment-guided molecular simulations define a heterogeneous structural ensemble for the PTPN11 tandem SH2 domains

Marasco, M., Kirkpatrick, J., Carlomagno, T., Hub, J. S., & Anselmi, M. (2023) · Chemical Science · doi:10.1039/d3sc00746d · Cited by 6 · see citing works

Exclusion of PD-1 from the immune synapse: A novel strategy to modulate T cell function

Hao, L. Y., Lerrer, S., Paiola, M., Moore, E. K., Gartshteyn, Y., Song, R., Goeckeritz, M., Black, M. J., Bukhari, S., Hu, X., et al. (2024) · Molecular Therapy Oncology · doi:10.1016/j.omton.2024.200839 · Cited by 6 · see citing works

Efficacy of neoadjuvant PD-1/PD-L1 inhibitor in resectable NSCLC: a meta-analysis based on randomized controlled trials

Zhang, W., Dai, T., Wang, D., Zhu, Y., & Hua, W. (2024) · BMC Cancer · doi:10.1186/s12885-024-13311-5 · Cited by 5 · see citing works

X-linked lymphoproliferative disease type 1: a clinical and genetic update

Li, J., Lv, L., Wei, Q., Pang, W., He, C., Wu, H., & Guo, L. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1620327 · Cited by 4 · see citing works

Caspase-5c amplifies Wnt via APC cleavage to promote intestinal homeostasis

Jia, B., Shi, Y., Hong, Y., Yang, C.-B., Roycroft, D., Kamal, S., Mukherjee, S., Ueberheide, B., Grier, A., Witherspoon, M. S. L., et al. (2026) · Nature · doi:10.1038/s41586-026-10343-8 · Cited by 3 · see citing works

Synergistic blockade of SHP-2 and A2AR signal pathways with targeted nanoparticles restores anti-tumor immunity of CD8+ T cells

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 · see citing works

1H, 13C, 15N chemical shift assignments of SHP2 SH2 domains in complex with PD-1 immune-tyrosine motifs

Marasco, M., Kirkpatrick, J., & Carlomagno, T. (2020) · Biomolecular NMR Assignments · doi:10.1007/s12104-020-09941-y · Cited by 3 · see citing works

PD-L1 blockade in mitigating severe acute pancreatitis induced pancreatic damage through modulation of immune cell apoptosis

Yang, D., Chen, K., Lv, Z., Zhou, B., Zhou, Z., & Li, Y. (2024) · International Immunopharmacology · doi:10.1016/j.intimp.2024.112081 · Cited by 2 · see citing works

Changing the location of proteins on the cell surface is a promising strategy for modulating T cell functions

Strazza, M., Song, R., Hiner, S., & Mor, A. (2024) · Immunology · doi:10.1111/imm.13828 · Cited by 2 · see citing works

Cell wall proteomics in live Mycobacterium tuberculosis uncovers exposure of ESX substrates to the periplasmPreprint

Jaisinghani, N., Previti, M. L., Andrade, J., Askenazi, M., Ueberheide, B. M., & Seeliger, J. C. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.03.29.534792 · Cited by 2 · see citing works

Themis dominates T cell exhaustion by regulation of TCR and PD-1 signalingPreprint

Tang, J., Jia, X., Zeng, T., Bao, Y., Hu, Y., Dong, J., Xu, X., Chen, X. L., Liu, Y., Wang, J., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.02.17.634430 · Cited by 2 · see citing works

In vitro T cell responses to PD-1 blockade are reduced by IFN-α but do not predict therapy response in melanoma patients

Timmerman, L. M., Hensen, L. C. M., van Eijs, M. J. M., Verheijden, R. J., Suijkerbuijk, K. P. M., Meyaard, L., van der Vlist, M., Meyaard, L., Kuball, J. H. E., Oldenburg, B., et al. (2024) · Cancer Immunology Immunotherapy · doi:10.1007/s00262-024-03760-z · Cited by 1 · see citing works

Co-immunoprecipitation Assay for Studying Functional Interactions Between Receptors and Enzymes

Peled, M., Strazza, M., & Mor, A. (2018) · Journal of Visualized Experiments · doi:10.3791/58433 · Cited by 1 · see citing works

Analysis of biological networks in the endothelium with biomimetic microsystem platform

Kruse, K. J., Klomp, J. A., Sun, M., Chen, Z., Santana, D., Huang, F., Kanabar, P. N., Maienschein‐Cline, M., & Komarova, Y. A. (2019) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00392.2018 · Cited by 1 · see citing works

Structure of the human clamp loader bound to the sliding clamp: a further twist on AAA+ mechanismPreprint

Gaubitz, C., Liu, X., Magrino, J., Stone, N. P., Landeck, J. T., Hedglin, M., & Kelch, B. A. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.02.18.953257 · Cited by 1 · see citing works

Alternative splicing of SLAMF6 in human T cells creates a co-stimulatory isoform that counteracts the inhibitory effect of the full-length receptorPreprint

Hajaj, E., Zisman, E., Tzaban, S., Merims, S., Cohen, J. E., Klein, S., Frankenburg, S., Sade-Feldman, M., Tabach, Y., Yizhak, K., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.08.21.262238 · Cited by 1 · see citing works

Supplementary Tables and Methods from Targeting Mitochondrial Structure Sensitizes Acute Myeloid Leukemia to Venetoclax Treatment

Chen, X., Glytsou, C., Zhou, H., Narang, S., Reyna, D. E., Lopez, A., Sakellaropoulos, T., Gong, Y., Kloetgen, A., Yap, Y. S., et al. (2023) · doi:10.1158/2159-8290.22536728.v1

Investigating the Intrinsic Role of Programmed Death-Ligand 1 in Human Cancers.

Hudson, K. (2023) · Sheffield Hallam University · doi:10.7190/shu-thesis-00520

SLAM Family Receptors

Galindo, C. C., & Veillette, A. (2024) · Elsevier eBooks · doi:10.1016/b978-0-128-24465-4.00078-8

Quantitative interactomics of PD-1 and BTLA in primary T cells provides a rationale for concomitant coinhibitor blockade in cancer immunotherapy

Zhai, Y. (2019) · theses.fr (ABES) · doi:10.70675/8c9774d2zd5e4z45c6z8981z09af2d8452c2

Dissection et caractérisation par analyse de spectrométrie de masse des assemblages moléculaires encodant la signalisation des lymphocytes T

Ruminski, K. (2020) · theses.fr (ABES) · doi:10.70675/37615f59z6fb1z4c3ezaa64zc1ba80efd6bd

Understanding the Therapeutic Potential of PD-1 Agonism in Inflammatory and Autoimmune Disorders

Justin, Z., Song, R., Kerrouche, N., Yu, X., Levin, Y., & Mor, A. (2026) · BioDrugs · doi:10.1007/s40259-026-00785-x

SAP loss limits anti-insulin atypical B cell activation and pro-inflammatory CD8 T cells despite preserved Tfh responses to protect against type 1 diabetesPreprint

Clark, L. M., McNitt, D. H., McAninch, J., Bass, L. E., Padgett, M. L., Moreno, A. F., Brannon, C. T., Nichols, C. M., Stier, M. T., & Bonami, R. H. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.07.29.741363

Abstract A059: Combinatorial proteomic analysis of the receptor programmed cell death (PD)-1 uncovers new checkpoint modulators

Peled, M., & Mor, A. (2016) · Cancer Immunology Research · doi:10.1158/2326-6066.imm2016-a059

Quantitative phosphoproteomic analysis reveals involvement of PD-1 in multiple T cell functions

Tocheva, A. S., Peled, M., Strazza, M., Adam, K. R., Lerrer, S., Nayak, S., Azoulay‐Alfaguter, I., Foster, C., Philips, E. A., Neel, B. G., et al. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.014745 · Cited by 34 · see citing works

SHP-1 and SHP-2 Associate with Immunoreceptor Tyrosine-Based Switch Motif of Programmed Death 1 upon Primary Human T Cell Stimulation, but Only Receptor Ligation Prevents T Cell Activation

Chemnitz, J. M., Parry, R. V., Nichols, K. E., June, C. H., & Riley, J. L. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.173.2.945 · Cited by 1,246 · see citing works

T lymphocyte–specific deletion of SHP1 and SHP2 promotes activation-induced cell death of CD4 + T cells and impairs antitumor response

Foster, C., Du, J., Pundel, O. J., Geer, M. J., Ripert, R. C., Liu, J., Heim, T. A., Araki, K. Y., Lund, A. W., Wang, J., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2427254122 · Cited by 10 · see citing works

PD-1 inhibits the TCR signaling cascade by sequestering SHP-2 phosphatase, preventing its translocation to lipid rafts and facilitating Csk-mediated inhibitory phosphorylation of Lck.

Bardhan, K., Patsoukis, N., Weaver, J. D., Freeman, G. J., Li, L., & Boussiotis, V. A. (2016) · The Journal of Immunology · doi:10.4049/jimmunol.196.supp.128.15 · Cited by 12 · see citing works