Cited by 797TGF-β signaling in diseasesDevelopmental Biology and Gene RegulationSignaling Pathways in Disease

The DOI matches its Crossref record; 346 of the 347 references it cites were found in a registry or an index.

Specificity, versatility, and control of TGF-β family signaling

Open access

Derynck, Rik, Budi, Erine H.·2019·Science Signaling

DOI 10.1126/scisignal.aav5183PMC PMC6800142

Open this paper in CoChat — free account Open PDF

Abstract

Molecular function and pathway cross-talk in TGF-β signaling reveal its complexity and open questions.

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

Crossref · 10.1126/scisignal.aav5183

Cites

346 of 346 references verified0 citation errors · 0 not checkable

Statistics

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

The protein kinase complement of the human genome
Manning, G., Whyte, D. B., Martinez, R., Hunter, T., & Sudarsanam, S. (2002) · Science · doi:10.1126/science.1075762 · Cited by 8,145 · cited 1×
“On the basis of sequence characteristics, the type I and type II receptors are predicted dual-specificity kinases, able to phosphorylate on serine and threonine, as well as tyrosine, and are phylogenetically clustered proximal to other dual-specificity kinases such asMEK kinases (65, 66).”
Background
Molecular mechanisms of epithelial–mesenchymal transition
Lamouille, S., Xu, J., & Derynck, R. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3758 · Cited by 8,091
Self-citation
mTOR Signaling in Growth, Metabolism, and Disease
Saxton, R. A., & Sabatini, D. M. (2017) · Cell · doi:10.1016/j.cell.2017.02.004 · Cited by 7,555
TGFβ in Cancer
Massagué, J. (2008) · Cell · doi:10.1016/j.cell.2008.07.001 · Cited by 3,907
TGFβ signalling in context
Massagué, J. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3434 · Cited by 3,239
The PI3K Pathway in Human Disease
Fruman, D. A., Chiu, H., Hopkins, B. D., Bagrodia, S., Cantley, L. C., & Abraham, R. T. (2017) · Cell · doi:10.1016/j.cell.2017.07.029 · Cited by 2,749
Smad transcription factorsPreprint
Massagué, J., Seoane, J., & Wotton, D. (2005) · Genes & Development · doi:10.1101/gad.1350705 · Cited by 2,519
Ubiquitin modifications
Swatek, K. N., & Komander, D. (2016) · Cell Research · doi:10.1038/cr.2016.39 · Cited by 2,141
mTOR Signaling in Growth, Metabolism, and Disease
Saxton, R. A., & Sabatini, D. M. (2017) · Cell · doi:10.1016/j.cell.2017.03.035 · Cited by 2,112 · cited 1×
“12, eaav5183 (2019) 26 February 2019 rylates and thus activates mTOR, which, among other responses, promotes protein synthesis and cell metabolism, is required for cell migration, and phosphorylates AKT in a positive feedback loop (311, 312).”
Background
SPECIFICITY AND VERSATILITY IN TGF-β SIGNALING THROUGH SMADS
Feng, X.-H., & Derynck, R. (2005) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.21.022404.142018 · Cited by 1,869
Self-citation

Flagged first, then by citations

Show all 347 references

1 of the 347 references couldn’t be matched to a known paper.

Research works printed but not linked: 1

R. Derynck K. Miyazono The Biology of the TGF-β Family (Cold Spring Harbor Laboratory Press 2017) pp. 1164.

Sorted by citations

Items 401–500 of 797

FOXO1 mitigates the SMAD3/FOXL2C134W transcriptomic effect in a model of human adult granulosa cell tumor
Secchi, C., Benaglio, P., Mulas, F., Belli, M., Stupack, D. G., & Shimasaki, S. (2021) · Journal of Translational Medicine · doi:10.1186/s12967-021-02754-0 · Cited by 10
Molecular Activation of the Kv11.1 Channel Reprograms EMT in Colon Cancer by Inhibiting TGFβ Signaling via Activation of Calcineurin
Eskandari, N., Senyuk, V., Moore, J. M., Kalik, Z. M., Luan, Q.-Y., Papautsky, I., Moshiri, A., Bocchetta, M., Salami, S., Oryan, S., et al. (2021) · Cancers · doi:10.3390/cancers13236025 · Cited by 9
“The TGFβ response starts when the surface membrane TGFβ receptor I (TFGBRI) and the TGFβ receptor II (TGFBRII) form a complex upon TGFβ ligand binding (TGFβ1, TGFβ2, TGFβ3) [16].”
Background
Targeted inhibition of ZAK ameliorates renal interstitial fibrosis
Shu, S., Liu, H., Yang, J., Tang, H., Li, H., Liu, Z., Zhou, M., Zhu, F., Hu, Z. M., Ding, K., et al. (2022) · Translational research · doi:10.1016/j.trsl.2022.03.002 · Cited by 10
Molecular Regulation of Notch Signaling by Gremlin
Márquez‐Expósito, L., Cantero‐Navarro, E., Rodrigues-Díez, R. R., Orejudo, M., Tejera‐Muñoz, A., Tejedor-Santamaria, L., Rayego‐Mateos, S., Rández‐Garbayo, J., Santos‐Sanchez, L., Mezzano, S. A., et al. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-36422-9_6 · Cited by 11
Activin E is a transforming growth factor β ligand that signals specifically through activin receptor-like kinase 7
Vestal, K. A., Kattamuri, C., Koyiloth, M., Ongaro, L., Howard, J. A., Deaton, A. M., Ticau, S., Dubey, A., Bernard, D. J., & Thompson, T. B. (2024) · Biochemical Journal · doi:10.1042/bcj20230404 · Cited by 10
Unveiling the power of microenvironment in liver regeneration: an in-depth overview
Hu, Y., Wang, R., An, N. A., Li, C., Wang, Q., Cao, Y., Li, C., Liu, J., & Wang, Y. (2023) · Frontiers in Genetics · doi:10.3389/fgene.2023.1332190 · Cited by 12
“One hour after PH, TGF-β 1 was released from the liver to reduce its content.”
BackgroundInfluential
Hearing loss promotes Alzheimer’s disease
Zhao, H., & Yang, Y. (2024) · Nature Aging · doi:10.1038/s43587-024-00606-2 · Cited by 9
Affinity-tagged SMAD1 and SMAD5 mouse lines reveal transcriptional reprogramming mechanisms during early pregnancy
Liao, Z., Tang, S., Nozawa, K., Shimada, K., Ikawa, M., Monsivais, D., & Matzuk, M. M. (2024) · eLife · doi:10.7554/elife.91434.4 · Cited by 9
LP340, a novel histone deacetylase inhibitor, decreases liver injury and fibrosis in mice: role of oxidative stress and microRNA-23a
Samuvel, D. J., Lemasters, J. J., Chou, C. J., & Zhong, Z. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1386238 · Cited by 10
Halofuginone prevents inflammation and proliferation of high-altitude pulmonary hypertension by inhibiting the TGF-β1/Smad signaling pathway
Wang, J., Guan, L., Yu, J., Ma, B., Shen, H., Xing, G., Xu, Y., Li, Q., Liu, J., Qin, X., et al. (2025) · Scientific Reports · doi:10.1038/s41598-025-88258-z · Cited by 9
“…and BMPs. Smad proteins are the classical downstream molecules of TGF-β superfamily, with TGF-βs mediating Smad2/3 phosphorylation and BMPs mediating Smad1/5/8 phosphorylation, both of which exert regulatory effects by transmitting upstream signals from the plasma membrane to the nucleus 34,35 .”
Cbfβ: A key regulator in skeletal stem cell differentiation, bone development, and disease
Zheng, C., Zhang, C., He, Y., Lin, S., Zhu, Z., Wang, H., & Chen, G. (2025) · The FASEB Journal · doi:10.1096/fj.202500030r · Cited by 9
Recent Advances in the Investigation of the Role and Immunoregulatory Mechanisms of Polysaccharides From Traditional Chinese Medicine in the Intervention of Liver Cirrhosis
Cui, H., Ji, H., Zhang, L., Zhang, W., Kang, R., Ni, Y., & Hao, X. (2025) · Phytotherapy Research · doi:10.1002/ptr.70045 · Cited by 9
“Following C-terminal phosphorylation, pSmad2 and pSmad3 form a heterotrimeric complex with common-mediator Smad4, which is then translocated to the nucleus where it binds DNA to directly regulate fibrogenic genes such as collagen type I, fibronectin, tissue inhibitors of metalloproteinases (TIMPs) (Uemura et al. 2005)…”
Mechanism of Disease: Recessive ADAMTSL4 Mutations and Craniosynostosis with Ectopia Lentis
Gustafson, J. A., Björk, M., van Ravenswaaij‐Arts, C. M. A., & Cunningham, M. L. (2022) · Case Reports in Genetics · doi:10.1155/2022/3239260 · Cited by 9
“Activated receptor SMADs (2 and 3) complex with SMAD4 and translocate to the nucleus where they help regulate gene transcription (Reviewed in [8, 9]).”
Background
Transmembrane anterior posterior transformation 1 regulates BMP signaling and modulates the protein stability of SMAD1/5
Wang, B., Zhao, Q., Gong, X., Wang, C., Bai, Y. Q., Wang, H., Zhou, J., & Rong, X. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102684 · Cited by 9
“Subsequently, activated type I receptor kinases phosphorylate the receptor-regulated intracellular effector SMADs (RSMADs) (SMAD1/5), at two C-terminal serines (6).”
Background
RETRACTED: lncRNA NEAT1/miR‐495‐3p regulates angiogenesis in burn sepsis through the TGF‐β1 and SMAD signaling pathways
Meng, Y., Hao, Z., Zhang, H., Bai, P., Guo, W., Tian, X., & Xu, J. (2023) · Immunity Inflammation and Disease · doi:10.1002/iid3.758 · Cited by 9
“Association of the ligand to the heteromeric receptor complexes sequentially triggers the phosphorylation of the type II receptor and the type I receptor, which activates downstream transcription factors known as SMADs and consequently induces the expression of TGF‐β target genes.(32,33) Accumulating evidence suggests…”
Background
Retracted
Differential kinase activity of ACVR1 G328V and R206H mutations with implications to possible TβRI cross-talk in diffuse intrinsic pontine glioma
Cao, H., Jin, M., Gao, M., Zhou, H., Tao, Y. J., & Skolnick, J. (2020) · Scientific Reports · doi:10.1038/s41598-020-63061-0 · Cited by 8
High‑dose TGF‑β1 degrades human nucleus pulposus cells via ALK1‑Smad1/5/8 activation
Qu, Z., Zhang, F., Chen, W., Lin, T., & Sun, Y. A. (2020) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2020.9088 · Cited by 9
“However, activated ALK1 can mediate Smad1/5/8 phosphorylation and has the opposite effect in numerous tissues (32,33).”
Background
Screening and Bioinformatics Analysis of Competitive Endogenous RNA Regulatory Network ––Related to Circular RNA in Breast Cancer
Wang, T., Zhang, Y., He, Y., Liu, Y., & Qi, P. (2021) · BioMed Research International · doi:10.1155/2021/5575286 · Cited by 9
Aberrant Activation Mechanism of TGF-β Signaling in Epithelial-mesenchymal Transition
Yuki, R. (2021) · YAKUGAKU ZASSHI · doi:10.1248/yakushi.21-00143 · Cited by 10
Imbalance in the estrogen/androgen ratio may affect prostate fibrosis through the TGF-β/Smad signaling pathway
Cao, Y., Tian, Y., Zhang, H., Luo, G., Sun, Z.-L., & Xia, S.-J. (2022) · International Urology and Nephrology · doi:10.1007/s11255-021-03079-z · Cited by 9
“Under pathological conditions, however, its activation can increase the synthesis of collagen, fibronectin, hyaluronic acid, and other extracellular matrix, induces neovascularization, and promotes the fibrosis of tissues and organs [18].”
Background
A Pilot Study of Subclinical Non-Capillary Peripapillary Perfusion Changes in Thyroid-Related Orbitopathy Detected Using Optical Coherence Tomography Angiography
Pinhas, A., Romo, J. S. A., Lynch, G., Zhou, D. B., Toral, M. V. C., Tenzel, P. A., Otero-Marquez, O., Yakubova, S., Barash, A., Rocca, D. D., et al. (2022) · Clinical ophthalmology · doi:10.2147/opth.s356631 · Cited by 9
“In TRO, orbital fibroblasts upregulate transforming growth factor (TGF)-β, a potent soluble multifunctional cytokine involved in cell differentiation, proliferation, survival and apoptosis.(26) TGF-β is well known to induce myofibroblast differentiation and proliferation and to promote hyaluronan synthesis in TRO, lea…”
Background
At the Crux of Joint Crosstalk: TGFβ Signaling in the Synovial Joint
Bailey, K. N., & Alliston, T. N. (2022) · Current Rheumatology Reports · doi:10.1007/s11926-022-01074-6 · Cited by 10
Foxd4l1.1 Negatively Regulates Chordin Transcription in Neuroectoderm of Xenopus Gastrula
Kumar, V., Goutam, R. S., Umair, Z., Park, S., Lee, U., & Kim, J. (2021) · Cells · doi:10.3390/cells10102779 · Cited by 9
“1-interacting domain in the two Smads, we designed truncated Smad2/3 protein constructs (separately).”
Multiple roles of mothers against decapentaplegic homolog 4 in tumorigenesis, stem cells, drug resistance, and cancer therapy
Dai, C., Cao, Y., Huang, F., & Wang, Y. (2022) · World Journal of Stem Cells · doi:10.4252/wjsc.v14.i1.41 · Cited by 9
Recombinant production, purification, crystallization, and structure analysis of human transforming growth factor β2 in a new conformation
del Amo-Maestro, L., Marino‐Puertas, L., Goulas, T., & Gomis‐Rüth, F. X. (2019) · Scientific Reports · doi:10.1038/s41598-019-44943-4 · Cited by 9
Dominant Negative TGF-β Receptor Type II in T Lymphocytes Promotes Anti-Tumor Immunity by Inducing the Proliferation and Differentiation of T Cells and Enhancing CTL Responses
Li, H. M., Guan, Y., Han, C., Zhang, Y., Chen, Y., Jiang, L., Zhang, P., Chen, X., Wei, W., & Ma, Y. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.112754 · Cited by 9
Regulation of TGFβ/SMAD signaling by long non-coding RNAs in different cancers: Dark Knight in the Castle of molecular oncology
Adylova, A., Муханбетжановна, А. А., Attar, R., Ishmuratova, M., & Farooqı, A. A. (2021) · Non-coding RNA Research · doi:10.1016/j.ncrna.2020.12.003 · Cited by 8
Periostin attenuates oxygen and glucose deprivation-induced death of mouse neural stem cells via inhibition of p38 MAPK activation
Liu, Y., Luan, Y., Guo, Z., Liu, Y., & Liu, C. (2022) · Neuroscience Letters · doi:10.1016/j.neulet.2022.136526 · Cited by 8
Reduced frequencies of Foxp3+GARP+ regulatory T cells in COPD patients are associated with multi-organ loss of tissue phenotype
Hou, J., Wang, X., Su, C., Ma, W., Zheng, X., Ge, X., & Duan, X. (2022) · Respiratory Research · doi:10.1186/s12931-022-02099-2 · Cited by 8
“GARP, the membrane binding receptor of latent-TGF-β [28], plays a pivotal role in promoting TGF-β activation by enabling the interplay of TGF-β with integrins αvβ6 or αvβ8 [29], which is thought to be a primer step for releasing bioactive TGF-β.”
Background
Anti-Fibrotic Effects of DL-Glyceraldehyde in Hepatic Stellate Cells via Activation of ERK-JNK-Caspase-3 Signaling Axis
Samsuzzaman, M., & Kim, S. Y. (2023) · Biomolecules & Therapeutics · doi:10.4062/biomolther.2022.131 · Cited by 8
“Transforming growth factor-β 1 (TGF-β 1) is known for its profibrotic function, mainly through the activation of the Smad2/3 signaling pathway (Derynck and Budi, 2019).”
Background
Therapeutic Potential of Targeting Transforming Growth Factor-beta (TGF-β) and Programmed Death-ligand 1 (PD-L1) in Pancreatic Cancer
Pourali, G., Zafari, N., Velayati, M., Mehrabadi, S., Maftooh, M., Hassanian, S. M., Mobarhan, M. G., Ferns, G. A., Avan, A., & Khazaei, M. (2023) · Current Drug Targets · doi:10.2174/0113894501264450231129042256 · Cited by 9
SMAD4 promotes somatic-germline contact during murine oocyte growth
Granados-Aparici, S., Yang, Q., & Clarke, H. J. (2024) · eLife · doi:10.7554/elife.91798 · Cited by 8
“The TGFβ signalling pathway regulates the functions and interactions of a wide range of cell types under various physiological and pathological conditions (Derynck and Budi, 2019, Peng et al., 2022).”
Background
Fibromodulin facilitates the osteogenic effect of Masquelet's induced membrane by inhibiting the TGF-β/SMAD signaling pathway
Wang, K., Zhou, M., Zhang, Y., Jin, Y., Xue, Y., Mao, D., & Rui, Y.-J. (2024) · Biomaterials Science · doi:10.1039/d3bm01665j · Cited by 8
Reproducible lung protective effects of a TGFβR1/ALK5 inhibitor in a bleomycin‐induced and spirometry‐confirmed model of IPF in male mice
Petersen, A. G., Korntner, S. H., Bousamaki, J., Oró, D., Manresa-Arraut, A., Pors, S. E., Salinas, C. G., Andersen, M. W., Madsen, M. R., Nie, Y., et al. (2024) · Physiological Reports · doi:10.14814/phy2.70077 · Cited by 7
“Accordingly, a subset of canonical TGF β R1 (also known as activin receptor-like kinase 5, Alk5 (Derynck & Budi, 2019; Massagué, 2012)) signaling transduction markers were upregulated ( Tgfb1 , Tgfbr1 ) while others were unaffected ( Smad2 , Smad3 ).”
Background
Sivelestat sodium alleviated sepsis-induced acute lung injury by inhibiting TGF-β/Smad signaling pathways through upregulating microRNA-744-5p
Qian, J., Liu, K.-J., Zhong, C.-H., Xian, L., & Hu, Z.-H. (2024) · Journal of Thoracic Disease · doi:10.21037/jtd-24-65 · Cited by 8
“Inflammatory cytokines, which include members of the transforming growth factor-β (TGF-β ) superfamily and interleukins are the main driving force behind ALI (8).”
Knockdown of long non‑coding RNA ANRIL inhibits the proliferation and promotes the apoptosis of Burkitt lymphoma cells through the TGF‑β1 signaling pathway
Mao, S., Jin, J., Li, Z., & Yang, W. (2020) · Molecular Medicine Reports · doi:10.3892/mmr.2020.11785 · Cited by 8
Interplay of Inflammatory, Antigen and Tissue-Derived Signals in the Development of Resident CD8 Memory T Cells
Pritzl, C. J., Daniëls, M. A., & Teixeiro, E. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.636240 · Cited by 9
“However, Smad4 appears to be dispensable for CD8 TRM development (72, 73).”
Background
IFN-α-2b Inhibits the Proliferation and Migration of Fibroblasts via the TGFβ/Smad Signaling Pathway to Reduce Postoperative Epidural Fibrosis
Liu, Z., Chen, H., Fan, Z., Dai, J., Sun, Y. L., Yan, L., Wang, R., Li, X., & Wang, J. (2021) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.2020.0231 · Cited by 8
MEX3B inhibits collagen production in eosinophilic nasal polyps by downregulating epithelial cell TGFBR3 mRNA stability
Liu, J., Chen, A., Yu, Q., Shi, K., Liu, Y., Guo, C., Wang, Z.-Z., Yao, Y., Pan, L., Lu, X., et al. (2023) · JCI Insight · doi:10.1172/jci.insight.159058 · Cited by 8
“TGF-βR3 promotes TGF-β2 signaling by forming the TGF-β2/TGF-βR3 complex and then recruiting and activating TGF-βR2 and TGF-βR1 (28, 29, 31).”
BackgroundInfluential
A negative feedback loop centered on SMAD3 expression in transforming growth factor β1-induced corneal myofibroblast differentiation
Tang, Y., Du, E., Wang, G., Qin, F., Meng, Z., Dai, L., Wang, Y., & Ren, S. (2023) · Experimental Eye Research · doi:10.1016/j.exer.2023.109654 · Cited by 8
PRRX1 induced by BMP signaling decreases tumorigenesis by epigenetically regulating glioma‐initiating cell properties via DNA methyltransferase 3A
Tanabe, R., Miyazono, K., Todo, T., Saito, N., Iwata, C., Komuro, A., Sakai, S., Raja, E., Koinuma, D., Morikawa, M., et al. (2021) · Molecular Oncology · doi:10.1002/1878-0261.13051 · Cited by 10
Human umbilical cord mesenchymal stem cells improve uterine incision healing after cesarean delivery in rats by modulating the TGF-β/Smad signaling pathway
Sun, Q., Zhang, D., Ai, Q., Yang, Y., Wang, H., Tang, L. M., Yi, X., Wang, S., & Zheng, Y. (2024) · Archives of Gynecology and Obstetrics · doi:10.1007/s00404-024-07381-w · Cited by 7
“TGF-β is considered to be an important fibrogenic factor, and the typical signaling pathway of TGF-β involves the downstream Smad molecule [12].”
A modest proposal: targeting αv integrin-mediated activation of latent TGFbeta as a novel therapeutic approach to treat scleroderma fibrosis
Leask, A., Fadl, A., & Naik, A. (2024) · Expert Opinion on Investigational Drugs · doi:10.1080/13543784.2024.2323528 · Cited by 7
“…of pro-segments, although cleaved from the mature polypeptides, remain non-covalently associated with mature TGF-β in the form of ‘latent’ complex, often called ‘latency-associated polypeptide’ (LAP), that prevent TGF-β from binding to the cell surface receptors and, hence, signaling [23,24].”
Background
Genetic and molecular mechanisms of hydrocephalus
Deng, X., Chen, Y., Duan, Q., Ding, J., Wang, Z., Wang, J. D., Chen, X., Zhou, L., & Zhao, L. (2025) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2024.1512455 · Cited by 7
Commercially available transfection reagents and negative control siRNA are not inert
Kleefeldt, J. M., Pozarska, A., Nardiello, C., Pfeffer, T., Vadász, I., Herold, S., Seeger, W., & Morty, R. E. (2020) · Analytical Biochemistry · doi:10.1016/j.ab.2020.113828 · Cited by 7
A Novel Approach for Screening Sericin-Derived Therapeutic Peptides Using Transcriptomics and Immunoprecipitation
Wang, R., Wang, Y., Song, J., Tan, H., Tian, C., Zhao, D., Xu, S., Zhao, P., & Xia, Q. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24119425 · Cited by 7
“The non-classical TGFβ signaling pathways always cooperate with three para-signaling pathways to promote cell proliferation, including the JNK, ERK, and P38 signaling pathways [33].”
Background
Proteomics Sequencing Reveals the Role of TGF-β Signaling Pathway in the Peripheral Blood of Offspring Rats Exposed to Fluoride
Yu, F., Yu, S.-Y., Duan, L., Yang, S., Hou, X., Du, Y., Gao, M., Zuo, J., Sun, L., Fu, X., et al. (2023) · Biological Trace Element Research · doi:10.1007/s12011-023-03805-x · Cited by 7
“In many species, transforming growth factor-βs (TGF-βs) mediate multiple signaling functions, providing tissue-specific control of differentiation, proliferation, and cell-specific or tissue-specific motility [8–11].”
TGF-β Regulates m6A RNA Methylation after PM2.5 Exposure
Wu, T., Liu, B., Wei, Y., & Li, Z. (2023) · Toxics · doi:10.3390/toxics11121026 · Cited by 7
“…accepted model of TGF-β signal transduction is that the TGF-β dimer binds to the TGF-β receptor, then sequentially transfers phosphate groups to Smad2 and Smad3 proteins, which are translocated to the target gene DNA sequence to activate or inhibit the expression of the target gene [35,36].”
Background
Single‐cell transcriptomics reveal the remodeling landscape of bladder in patients with obstruction‐induced detrusor underactivity
Chen, J., Peng, L., Chen, G., Chen, Y., Zeng, X., Zhang, J., Zhang, C., Shen, H., Liao, B., & Luo, D. (2024) · MedComm · doi:10.1002/mco2.490 · Cited by 7
Myocardial TGFβ2 Is Required for Atrioventricular Cushion Remodeling and Myocardial Development
Bhattacharya, A., Al-Sammarraie, N., Gebere, M. G., Johnson, J., Eberth, J. F., & Azhar, M. (2021) · Journal of Cardiovascular Development and Disease · doi:10.3390/jcdd8030026 · Cited by 7
Connective tissue growth factor mediates bone morphogenetic protein 2-induced increase in hyaluronan production in luteinized human granulosa cells
Chang, H., Bai, L., Zhu, Y., & Leung, P. C. K. (2022) · Reproductive Biology and Endocrinology · doi:10.1186/s12958-022-00937-y · Cited by 7
“A large number of studies have demonstrated that the interaction modes between the ligands and their corresponding receptors are diverse in different tissues or cell types [46].”
Background
An engineered (CAGA)12-EGFP cell-based biosensor for high-content and accurate detection of active TGF-β
Ruan, Q., Lin, X., Wang, L., Wang, N., Zhao, Y., Wang, H., Tian, F., Hu, N., Li, Y., & Zhao, B. (2022) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2022.114884 · Cited by 8
Therapeutic potency of compound RMY-205 for pulmonary fibrosis induced by SARS-CoV-2 nucleocapsid protein
Zhang, Z., Ju, C.-Y., Wu, L.-Z., Yan, H., Hong, W., Chen, H., Yang, P., Wang, B., Gou, T., Chen, X.-Y., et al. (2023) · Cell chemical biology · doi:10.1016/j.chembiol.2023.02.004 · Cited by 7
Site-1 protease inhibits mitochondrial respiration by controlling the TGF-β target gene Mss51
Mousa, M. G., Vuppaladhadiam, L., Kelly, M. O., Pietka, T., Ek, S., Shen, K. C., Meyer, G. A., Finck, B. N., & Brookheart, R. T. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112336 · Cited by 8
Increased expression of the transforming growth factor β–inducible gene HIC-5 in systemic sclerosis skin and fibroblasts: a novel antifibrotic therapeutic target
Piera-Velázquez, S., Fertala, J., Huaman, G., Louneva, N., & Jiménez, S. A. (2020) · Lara D. Veeken · doi:10.1093/rheumatology/keaa200 · Cited by 7
Human transforming growth factor beta2 in a tetragonal crystal form
Gomis‐Rüth, F. X., Marino‐Puertas, L., del Amo-Maestro, L., & Goulas, T. (2018) · Worldwide Protein Data Bank · doi:10.2210/pdb6i9j/pdb · Cited by 7
Activin A–Activated ALK4 Induces Pathogenic Th17‐Involved Endothelial–Mesenchymal Transition in Systemic Lupus Erythematosus–Associated Pulmonary Arterial Hypertension
Jing, S., Qian, J., Ying, H., Mao, P., Yao, M., Wu, Z., Bogaard, H. J., Wang, L., Li, M., & Yang, J. H. (2025) · Arthritis & Rheumatology · doi:10.1002/art.43235 · Cited by 6
“12,13 17 Patients with PAH have increased Activin A levels in peripheral blood and elevated levels of proin ﬂ amma-tory cytokines 18 – 20 such as IL-6.”
Transforming Growth Factor-β Signaling in Alcohol-Associated Liver Disease
Zou, H., Wang, S., Huang, C., Dooley, S., & Meindl‐Beinker, N. M. (2025) · American Journal Of Pathology · doi:10.1016/j.ajpath.2025.09.017 · Cited by 7
Fructose and follistatin potentiate acute MASLD during complete hepatic insulin resistance
Tao, R., Stöhr, O., Tok, O., Andrés-Hernando, A., Qiu, W., He, B., Wang, C., Grøntved, L., Burant, C., Hui, S. T., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-66296-5 · Cited by 6
A Phase 1a Study to Evaluate Safety, Tolerability, Pharmacokinetics, and Pharmacodynamics of RO7303509, an Anti-TGFβ3 Antibody, in Healthy Volunteers
Han, L. W., Jamalian, S., Hsu, J. C., Sheng, X. R., Yang, X., Yang, X., Monemi, S., Hassan, S., Yadav, R., Tuckwell, K., et al. (2024) · Rheumatology and Therapy · doi:10.1007/s40744-024-00670-5 · Cited by 6
Liebig’s law of the minimum in the TGF-β/SMAD pathway
Li, Y., Deng, D., Höfer, C. T., Kim, J., Heo, W. D., Xu, Q., Liu, X., & Zi, Z. (2024) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1012072 · Cited by 6
Bioactives in Oral Nutritional Supplementation: A Pediatric Point of View
Cecchi, N., Romanelli, R., Ricevuti, F., Carbone, M. G., Dinardo, M., Cesarano, E., Michele, A. D., Messere, G., Morra, S., Scognamiglio, A., et al. (2024) · Nutrients · doi:10.3390/nu16132067 · Cited by 7
“…in IBD is the transforming growth factor (TGF)- β superfamily (thirty-three genes that encode for homodimeric or heterodimeric secreted cytokines) [33], which includes TGF-β (TGF-β 1, TGF-β 2, and TGF-β 3) and related proteins (activins, growth and di ﬀ erentiation factors (GDFs), the bone…”
Background
Exploring Perianal Fistulas: Insights into Biochemical, Genetic, and Epigenetic Influences—A Comprehensive Review
Kawecki, M., Kruk, A. M., Drążyk, M., Domagała, Z., & Woźniak, S. (2025) · Gastroenterology Insights · doi:10.3390/gastroent16010010 · Cited by 6
“The production of TGF-β may increase due to TNF-α ; thus, it is also capable of inducing EMT via secondary messengers: Smad2, Smad3, and Smad4 [11,23,24].”
Divergence in chondrogenic potential between in vitro and in vivo of adipose- and synovial-stem cells from mouse and human
Chijimatsu, R., Miwa, S., Okamura, G., Miyahara, J., Tachibana, N., Ishikura, H., Higuchi, J., Maenohara, Y., Tsuji, S., Sameshima, S., et al. (2021) · Stem Cell Research & Therapy · doi:10.1186/s13287-021-02485-5 · Cited by 6
“Moreover, the non-Smad pathways also regulate cellular function and differentiation, including chondrogenesis [34, 47].”
Background
Activin A Modulates Betaglycan Shedding via the ALK4-SMAD3-Dependent Pathway in Endometriotic Cells
Mwaura, A. N., Riaz, M. A., Maoga, J. B., Mecha, E. O., Omwandho, C. O. A., Scheiner‐Bobis, G., Meinhold-Heerlein, I. M., & Konrad, L. (2022) · Biomolecules · doi:10.3390/biom12121749 · Cited by 7
In vivo characterization of the maturation steps of a pigment dispersing factor neuropeptide precursor in the Drosophila circadian pacemaker neurons
Lee, G., Zeng, K., Duffy, C. M., Sriharsha, Y., Yoo, S., & Park, J. H. (2023) · Genetics · doi:10.1093/genetics/iyad118 · Cited by 5
MOBILE pipeline enables identification of context-specific networks and regulatory mechanisms
Erdem, C., Gross, S. M., Heiser, L. M., & Birtwistle, M. R. (2023) · Nature Communications · doi:10.1038/s41467-023-39729-2 · Cited by 7
Crosstalk between ALK3(BMPR1A) deficiency and autophagy signaling mitigates pathological bone loss in osteoporosis
Niu, Z., Zhou, Y., Liang, M., Su, F., Guo, Q., Jing, J., Xie, J., Zhang, D., & Liu, X. (2024) · Bone · doi:10.1016/j.bone.2024.117052 · Cited by 6
Transforming Growth Factor Beta and Alveolar Rhabdomyosarcoma: A Challenge of Tumor Differentiation and Chemotherapy Response
Bhushan, B., Iranpour, R., Eshtiaghi, A., Rosa, S. C. D. S., Lindsey, B. W., Gordon, J. W., & Ghavami, S. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25052791 · Cited by 6
“TGF-β in cellular development, different members of the TGF-β superfamily are intensely studied for their widespread role in various diseases, including cancer [29,30].”
BackgroundInfluential
Mechanistic investigation of wogonin in delaying the progression of endothelial mesenchymal transition by targeting the TGF-β1 pathway in pulmonary hypertension
Wang, X., Cui, L., Wang, Y., Zeng, Z., Wang, H., Tian, L., Guo, J., & Chen, Y. (2024) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2024.176786 · Cited by 6
Regulatory expression of uncoupling protein 1 and its related genes by endogenous activity of the transforming growth factor‐β family in bovine myogenic cells
Eldaim, M. A. A., Zhao, K., Murakami, M., Yoshioka, H., Itoyama, E., Kitamura, S., Nagase, H., Matsui, T., & Funaba, M. (2020) · Cell Biochemistry and Function · doi:10.1002/cbf.3592 · Cited by 6
“Ucp1 expression levels were evaluated by RT-qPCR (n = 4); the Ucp1 expression level in cells treated without RA was set to 1 phosphorylation and hence activation of Smad2/3, whereas BMP transmits its signal via phosphorylated Smad1/5/8.”
BackgroundInfluential
Experimental Replacement of the Surface Defect of Rat Hyaline Cartilage by a Cell-Engineered Construct
Bozhokin, M. S., Божкова, С. А., Netylko, G. I., Наконечный, Д. Г., Nashchekina, Y. A., Blinova, M. I., & Anisimova, L. O. (2021) · Regenerative Engineering and Translational Medicine · doi:10.1007/s40883-021-00205-2 · Cited by 6
TGF-β1 contributes to the hepatic inflammation in animal models with nonalcoholic steatohepatitis by Smad3/TLR2 signaling pathway
Chen, Q., Yi, J., Liu, F., Li, J., Lu, K., Wang, X., Zhang, F., Li, Y., Wu, L., Yang, X., et al. (2022) · Molecular Immunology · doi:10.1016/j.molimm.2022.10.014 · Cited by 6
Renal transplant: long-term effects of immunosuppression.
Hasselder, A. (1999) · PubMed · Cited by 6
Cellular Compartmentalization as a Physical Regulatory Mechanism of Signaling Pathways
Fayad, A. N., Mazo-Durán, D., & Míguez, D. G. (2024) · Biophysica · doi:10.3390/biophysica4040042 · Cited by 5
“These dimeric polypeptide growth factors involve thirty-three secreted cytokines [23,24], and the different family members have been given various names according to their molecular identification history: TGF-β s (three isoforms of TGF-β s: TGF-β 1, TGF-β 2 and TGF-β 3), activins, bone…”
Activin Actions in Adipocytes
Ongaro, L., & Bernard, D. J. (2025) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/clinem/dgaf233 · Cited by 5
Nuclear hormone-sensitive lipase regulates adipose tissue mass and adipocyte metabolism
Dufau, J., Recazens, E., Bottin, L., Bergoglio, C., Mairal, A., Chaoui, K., Marqués, M.-A., Jiménez, V., García, M., Wang, T., et al. (2025) · Cell Metabolism · doi:10.1016/j.cmet.2025.09.014 · Cited by 5
Comprehensive analysis of the TGF-β signaling pathway: molecular mechanisms, disease drivers, and frontiers in clinical translation
Zhang, Y., Tang, H., Zhou, Z., Liao, J., Zhou, X., Chu, X., Shao, M., Zhang, C., & Jiang, L. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1831213 · Cited by 5
EZH2 Activates HTLV‐1 bZIP Factor‐Mediated TGF‐β Signaling in Adult T‐Cell Leukemia
Zhang, X., Yi, K., Wang, B., Chu, K., Liu, J., Zhang, J., Fang, J., & Zhao, T. (2024) · Journal of Medical Virology · doi:10.1002/jmv.70025 · Cited by 5
“The activated Smad complex can also recruit transcriptional co ‐ activators (CBP/p300), co ‐ repressors (c ‐ Ski), and chromatin re-modeling factors (histone deacetylases) [14, 15].”
Association of the TGFB1 Gene Polymorphisms with Pain Symptoms and the Effectiveness of Platelet-Rich Plasma in the Treatment of Lateral Elbow Tendinopathy: A Prospective Cohort Study
Jarosz, A., Wrona, J., Balcerzyk, A., Szyluk, K., Nowak, T., Iwanicki, T., Iwanicka, J., Kalita, M., Kania, W., Gawron, K., et al. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26062431 · Cited by 5
“Although initially thought to stimulate cell proliferation, TGF-β 1 is a bifunctional regulator that inhibits or stimulates cell division [6] and significantly accelerates wound healing [6,11,12].”
New insights into Gremlin-1: A tumour microenvironment landscape re-engineer and potential therapeutic target
Sun, C., Ding, Z., Li, B., Chen, S., Li, E., & Yang, Q. (2025) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2025.119962 · Cited by 5
Navigating Drug Discovery for Myhre Syndrome: The Complexity of a Multisystemic Rare Disease
Pindon, A., Brunetti‐Pierri, N., Young, K. H., Young, M. K., Macías, M. J., & Mo, X. (2025) · American Journal of Medical Genetics Part C Seminars in Medical Genetics · doi:10.1002/ajmg.c.32156 · Cited by 5
Overview of the signaling pathways involved in metastasis: An intriguing story-tale of the metastatic journey of ovarian cancer cells
Attar, R., Panah, T., Romero, M. A., Yulaevna, I. M., Gazouli, M., Berardi, R., Wieczorek, E., & Farooqı, A. A. (2021) · Cellular and Molecular Biology · doi:10.14715/cmb/2021.67.3.34 · Cited by 5
“Accordingly, "crosstalk" in the nucleus permits SMADs to modulate a wide-ranging array of transcriptional outputs in response to TGFβ stimulation of cancer cells (3-5).”
Background
Establishment of Embryonic Zebrafish Xenograft Assays to Investigate TGF-β Family Signaling in Human Breast Cancer Progression
Li, C., Ma, J., Groenewoud, A., Ren, J., Liu, S., Snaar-Jagalska, E. B., & ten Dijke, P. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2277-3_6 · Cited by 5
Fast Quantitation of TGF-β Signaling Using Adenoviral Reporter
Teixeira, A. F., Iaria, J., & Zhu, H. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2277-3_2 · Cited by 5
Mitochondria-specific peptide amphiphiles induce mitochondrial dysfunction and peripheral T-cell lymphomas (PTCL) damage
Sun, Q., Gui, A., Zou, A., Yan, Y., Qiu, S., Zhu, S. N., Liu, W., Zuo, J., Zhang, Q., & Yang, L. (2022) · Annals of Translational Medicine · doi:10.21037/atm-22-2233 · Cited by 5
“Moreover, TCR-mediated activation is tightly related to the cellular metabolic changes, TCR activation can promote the aerobic glycolysis and enhance the T cell function (9,10).”
Linc-ROR Promotes EMT by Targeting miR-204-5p/SMAD4 in Endometriosis
Yi, M., Wang, S., Zhang, X., Li, J., Xia, X., Zhang, T., & Fang, X. (2023) · Reproductive Sciences · doi:10.1007/s43032-023-01204-0 · Cited by 6
Ligand-specific regulation of transforming growth factor beta superfamily factors by leucine-rich repeats and immunoglobulin-like domains proteins
Abdullah, A., Herdenberg, C., & Hedman, H. (2023) · PLoS ONE · doi:10.1371/journal.pone.0289726 · Cited by 5
“The mature and bioactive TGF β ligands comprise homodimers and heterodimers formed by two covalently associated TGF β family peptides, which in mammals are encoded by 33 different genes [3].”
Background
The Role of Neuromodulation and Potential Mechanism in Regulating Heterotopic Ossification
Li, D., Liu, C., Wang, H., Li, Y., Wang, Y., An, S., & Sun, S. (2024) · Neurochemical Research · doi:10.1007/s11064-024-04118-8 · Cited by 6
“It orchestrates a vast range of biological processes, activating both non-Smad and Smad pathways, with the intricate involvement of upstream and downstream signaling molecules [140, 141].”
The master developmental regulator Jab1/Cops5/Csn5 is essential for proper bone growth and survival in mice
Samsa, W. E., Mamidi, M. K., Hausman, B. S., Bashur, L. A., Greenfield, E. M., & Zhou, G. D. (2020) · Bone · doi:10.1016/j.bone.2020.115733 · Cited by 5
“Activated RSmads then bind with Smad4, and translocate to the nucleus to promote transcription of TGFβ/BMP target genes (3, 4).”
BackgroundInfluential
Aggravation of hepatic ischemia‑reperfusion injury with increased inflammatory cell infiltration is associated with the TGF‑β/Smad3 signaling pathway
Li, H., Shen, X., Tong, Y., Ji, T., Feng, Y., Tang, Y., Mai, R., Ye, J., Que, T., & Luo, X. (2021) · Molecular Medicine Reports · doi:10.3892/mmr.2021.12219 · Cited by 4
Thrombospondin type 1 repeat-derived C-mannosylated peptide attenuates synaptogenesis of cortical neurons induced by primary astrocytes via TGF-β
Nishitsuji, K., Ikezaki, M., Manabe, S., Uchimura, K., Ito, Y., & Ihara, Y. (2021) · Glycoconjugate Journal · doi:10.1007/s10719-021-10030-y · Cited by 4
“First, we successfully detected the latent and active form of TGF-β1 by Western blotting with reductive SDS-PAGE, and the dimeric form of active TGF-β1, which is the receptor-binding form of active TGF-β1 [33], by Western blotting with non-reductive SDS-PAGE (Fig.”
Method
Label-free serum proteomics for the identification of the putative biomarkers of postoperative pain in patients with gastric cancer
Li, J., Li, S., Zhang, T., Yu, L., Wei, J., Wu, M., Xie, Y., & Tan, H. (2023) · Molecular Omics · doi:10.1039/d2mo00296e · Cited by 5
SHP2 inhibitors maintain TGFβ signalling through SMURF2 inhibition
Lai, X., Lui, S. K. L., Lam, H. Y., Adachi, Y., Sim, W. J., Vasilevski, N., Armstrong, N. J., Bridgeman, S. C., Main, N., Tan, T. Z., et al. (2023) · npj Precision Oncology · doi:10.1038/s41698-023-00486-6 · Cited by 6
A review on decoding the roles of YAP/TAZ signaling pathway in cardiovascular diseases: Bridging molecular mechanisms to therapeutic insights
Zhang, Y., Ren, Y., Li, X., Li, M., Fu, M., Zhou, W., Yu, Y., & Xiong, Y. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.132473 · Cited by 5
Effect of Hepatocyte Growth Factor-Transfected Human Umbilical Cord Mesenchymal Stem Cells on Hepatic Stellate Cells by Regulating Transforming Growth Factor-β1/Smads Signaling Pathway
Yin, F., Mao, L.-C., Cai, Q.-Q., & Jiang, W.-H. (2021) · Stem Cells and Development · doi:10.1089/scd.2021.0136 · Cited by 5
Selenium bioavailability modulates the sensitivity of thyroid cells to iodide excess
Oglio, R., Rodriguez, C., Salvarredi, L. A., Rossich, L. E., Perona, M., Dagrosa, A., Juvenal, G. J., & Thomasz, L. (2023) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2023.110810 · Cited by 4
Targeting TGF-β signaling in glioblastoma: therapeutic implications and novel drug development strategies
Sadeghzadeh, S., Askari, R. E., Zareiye, A., Meshkin, A., Aghabozorgi, R., Lotfi, M., Ghanbari, F., Shahcheraghi, S. H., & Aghili, Z. S. (2025) · Brain Tumor Pathology · doi:10.1007/s10014-025-00505-3 · Cited by 4
“LncRNAs have developed as TGF-β targets, and whole-genome transcriptomics recognized lncRNA qualities directed by TGF-β [48].”
Liraglutide inhibits the development of colorectal cancer by regulating TGF-β/Smad3 signaling pathway and affecting epithelial-mesenchymal transition
Li, X., Fan, M., Huang, R., Wang, K., & Huang, H. (2025) · Discover Oncology · doi:10.1007/s12672-025-03223-6 · Cited by 4
“In intracellular molecular regulation and TGF-β signaling, Smads protein is the key, which can directly transduce TGF-β signal through the cell membrane into the nucleus, and activation leads to nuclear transport and gene expression [45].”
Inhibiting TGF-β signaling pathway for disease therapy: challenges and opportunities
Gao, X., Li, X., Zhang, C., Zhou, J., Gu, K., Liu, X., & Bai, C. (2025) · Cytokine · doi:10.1016/j.cyto.2025.157048 · Cited by 4

Authors: Derynck, R., & Budi, E. H.
Affiliations: University of California, San Francisco (US)
Corresponding author: Derynck, Rik
ORCID: Derynck, Rik
Budi, Erine H.
Venue: Science Signaling
Publisher: American Association for the Advancement of Science (AAAS)
Published: 2019-02-26
Volume: 12
Issue: 570
ISSN: 1937-9145 (ISSN-L)
1945-0877
DOI: 10.1126/scisignal.aav5183
PMC: PMC6800142
OpenAlex: W2917714624
Cited by: 785
References: 347
Citations by year: 2026: 83 · 2025: 85 · 2024: 129 · 2023: 118 · 2022: 102 · 2021: 152 · 2020: 77 · 2019: 35
FWCI: 8.08
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Science Signaling (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
eScholarship (California Digital Library) (submittedVersion)
Funders: National Cancer Institute (RO1-CA63101, RO1-CA136690)
JDRF (3-APF-2017-392-A-N)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › TGF-β signaling in diseases
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
Keywords: Smad proteins, TGF-beta receptor, dual-specificity kinase, signaling crosstalk, non-Smad signaling, cancer, fibrosis, developmental anomalies
MeSH terms: Animals, Cell Differentiation, Gene Expression Regulation, Humans, Ligands, Neoplasms, Protein Binding, Signal Transduction, Transforming Growth Factor beta, Receptors, Transforming Growth Factor beta

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

Specificity, versatility, and control of TGF-β family signaling

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks