A Domain in TNF Receptors That Mediates Ligand-Independent Receptor Assembly and Signaling

Chan, Francis Ka-Ming; Chun, Hyung J.; Zheng, Lixin; Siegel, Richard M.; Bui, Kimmie L.; Lenardo, Michael J.

doi:10.1126/science.288.5475.2351

Cited by 856NF-κB Signaling PathwaysCytokine Signaling Pathways and InteractionsCell death mechanisms and regulation

A Domain in TNF Receptors That Mediates Ligand-Independent Receptor Assembly and Signaling

Chan, Francis Ka-Ming, Chun, Hyung J., Zheng, Lixin, Siegel, Richard M., Bui, Kimmie L., Lenardo, Michael J.·2000·Science

DOI 10.1126/science.288.5475.2351

Open this paper in CoChat — free account

Abstract

A conserved domain in the extracellular region of the 60- and 80-kilodalton tumor necrosis factor receptors (TNFRs) was identified that mediates specific ligand-independent assembly of receptor trimers. This pre–ligand-binding assembly domain (PLAD) is physically distinct from the domain that forms the major contacts with ligand, but is necessary and sufficient for the assembly of TNFR complexes that bind TNF-α and mediate signaling. Other members of the TNFR superfamily, including TRAIL receptor 1 and CD40, show similar homotypic association. Thus, TNFRs and related receptors appear to function as preformed complexes rather than as individual receptor subunits that oligomerize after ligand binding.

Integrity signals

Registry

Crossref · 10.1126/science.288.5475.2351

Cites

46 of 46 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

FAS and TRAILR ligands stabilize preformed receptor homotrimers to induce a conformational change enabling DD-dependent FADD association.
“In the case of FAS and TRAILRs, the cognate ligands—namely, FAS ligand (FASLG; also known as CD95L or APO-1L) and TNF superfamily member 10 (TNFSF10; best known as TRAIL), respectively—stabilize preformed receptor homotrimers to induce a conformational change at their intracellular tails that enables the death domain (DD)-dependent association of the adapter Fas associated via death domain (FADD)”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [281]

THE GREEN FLUORESCENT PROTEIN
Tsien, R. Y. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.509 · Cited by 6,178 · see citing works
Death Receptors: Signaling and Modulation
Ashkenazi, A., & Dixit, V. M. (1998) · Science · doi:10.1126/science.281.5381.1305 · Cited by 5,866 · see citing works
FADD, a novel death domain-containing protein, interacts with the death domain of fas and initiates apoptosis
Chinnaiyan, A. M., O'Rourke, K., Tewari, M., & Dixit, V. M. (1995) · Cell · doi:10.1016/0092-8674(95)90071-3 · Cited by 2,431 · see citing works
Involvement of MACH, a Novel MORT1/FADD-Interacting Protease, in Fas/APO-1- and TNF Receptor–Induced Cell Death
Boldin, M. P., Goncharov, T. M., Goltseve, Y. V., & Wallach, D. (1996) · Cell · doi:10.1016/s0092-8674(00)81265-9 · Cited by 2,292 · see citing works
The TNF receptor superfamily of cellular and viral proteins: Activation, costimulation, and death
Smith, C. A., Farrah, T., & Goodwin, R. G. (1994) · Cell · doi:10.1016/0092-8674(94)90372-7 · Cited by 1,909 · see citing works
TUMOR NECROSIS FACTOR RECEPTOR AND Fas SIGNALING MECHANISMS
Wallach, D., Varfolomeev, E. E., Malinin, N. L., Goltsev, Y. V., Kovalenko, A. V., & Boldin, M. (1999) · Annual Review of Immunology · doi:10.1146/annurev.immunol.17.1.331 · Cited by 1,299 · see citing works
TNF-Dependent Recruitment of the Protein Kinase RIP to the TNF Receptor-1 Signaling Complex
Hsu, H., Huang, J., Shu, H.-B., Baichwal, V., & Goeddel, D. V. (1996) · Immunity · doi:10.1016/s1074-7613(00)80252-6 · Cited by 1,182 · see citing works
Crystal structure of the soluble human 55 kd TNF receptor-human TNFβ complex: Implications for TNF receptor activation
Banner, D. W., D'Arcy, A., Janes, W., Gentz, R., Schönfeld, H., Broger, C., Loetscher, H., & Lesslauer, W. (1993) · Cell · doi:10.1016/0092-8674(93)90132-a · Cited by 1,097 · see citing works
Tumor necrosis factor: a pleiotropic cytokine and therapuetic target
Tracey, M. D., & Cerami, P. D. (1994) · Annual Review of Medicine · doi:10.1146/annurev.med.45.1.491 · Cited by 1,063 · see citing works
A Novel Protein That Interacts with the Death Domain of Fas/APO1 Contains a Sequence Motif Related to the Death Domain
Boldin, M. P., Varfolomeev, E. E., Pancer, Z., Mett, I. L., Camonis, J. H., & Wallach, D. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.14.7795 · Cited by 993 · see citing works
MATURE T LYMPHOCYTE APOPTOSIS—Immune Regulation in a Dynamic and Unpredictable Antigenic Environment
Lenardo, M. J., Chan, F. K.-M., Hornung, F., McFarland, H. F., Siegel, R. M., Wang, J., & Zheng, L. (1999) · Annual Review of Immunology · doi:10.1146/annurev.immunol.17.1.221 · Cited by 931 · see citing works
Self-citation
Tumor Necrosis Factor, Other Cytokines and Disease
Tracey, K. J., & Cerami, A. (1993) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.09.110193.001533 · Cited by 794 · see citing works
Fas Preassociation Required for Apoptosis Signaling and Dominant Inhibition by Pathogenic Mutations
Siegel, R. M., Frederiksen, J. K., Zacharias, D. A., Chan, F. K.-M., Johnson, M. M., Lynch, D. H., Tsien, R. Y., & Lenardo, M. J. (2000) · Science · doi:10.1126/science.288.5475.2354 · Cited by 659 · see citing works
Self-citation
Erythropoietin Receptor Activation by a Ligand-Induced Conformation Change
Remy, I., Wilson, I. A., & Michnick, S. W. (1999) · Science · doi:10.1126/science.283.5404.990 · Cited by 636 · see citing works
Crystallographic Evidence for Preformed Dimers of Erythropoietin Receptor Before Ligand Activation
Livnah, O., Stura, E. A., Middleton, S. A., Johnson, D. L., Jolliffe, L. K., & Wilson, I. A. (1999) · Science · doi:10.1126/science.283.5404.987 · Cited by 598 · see citing works
RIP mediates tumor necrosis factor receptor 1 activation of NF‐kappaB but not Fas/APO‐1‐initiated apoptosis.
Ting, A. T., Pimentel‐Muiños, F. X., & Seed, B. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb01007.x · Cited by 550 · see citing works
Oligomerization of epidermal growth factor receptors on A431 cells studied by time-resolved fluorescence imaging microscopy. A stereochemical model for tyrosine kinase receptor activation.
Gadella, T. W. J., & Jovin, T. M. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.129.6.1543 · Cited by 438 · see citing works
The tumor necrosis factor receptor 2 signal transducers TRAF2 and c-IAP1 are components of the tumor necrosis factor receptor 1 signaling complex
Shu, H., Takeuchi, M., & Goeddel, D. V. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.24.13973 · Cited by 418 · see citing works
Prevention of Constitutive TNF Receptor 1 Signaling by Silencer of Death Domains
Jiang, Y., Woronicz, J. D., Liu, W., & Goeddel, D. V. (1999) · Science · doi:10.1126/science.283.5401.543 · Cited by 415 · see citing works
Self-association of the “Death Domains” of the p55 Tumor Necrosis Factor (TNF) Receptor and Fas/APO1 Prompts Signaling for TNF and Fas/APO1 Effects
Boldin, M., Mett, I. L., Varfolomeev, E. E., Chumakov, I., Shemer‐Avni, Y., Camonis, J., & Wallach, D. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.1.387 · Cited by 386 · see citing works
CD30: expression and function in health and disease.
Horie, R., & Watanabe, T. (1998) · Seminars in Immunology · doi:10.1006/smim.1998.0156 · Cited by 338 · see citing works
Molecular docking towards drug discovery
Gschwend, D. A., Good, A. C., & Kuntz, I. D. (1996) · Journal of Molecular Recognition · doi:10.1002/(sici)1099-1352(199603)9:2 · Cited by 302 · see citing works
The p70 tumor necrosis factor receptor mediates cytotoxicity
Holler, R. A., Song, K. B., Fan, N. C., & Chang, D. J. (1992) · Cell · doi:10.1016/0092-8674(92)90532-h · Cited by 266 · see citing works
Flow cytometric measurement of fluorescence resonance energy transfer on cell surfaces. Quantitative evaluation of the transfer efficiency on a cell-by-cell basis
Trón, L., Szöllõsi, J., Damjanovich, S., et al. (1984) · Biophysical Journal · doi:10.1016/s0006-3495(84)84240-x · Cited by 201 · see citing works
Crystallographic Evidence for Dimerization of Unliganded Tumor Necrosis Factor Receptor
Naismith, J. H., Devine, T. Q., Brandhuber, B. J., & Sprang, S. R. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.22.13303 · Cited by 190 · see citing works
Enhancement of TNF receptor p60-mediated cytotoxicity by TNF receptor p80: requirement of the TNF receptor-associated factor-2 binding site
Weiss, T., Grell, M., Hessabi, B., Bourteele, S., Müller, G., Scheurich, P., & Wajant, H. (1997) · The Journal of Immunology · doi:10.4049/jimmunol.158.5.2398 · Cited by 184 · see citing works
Identification and Characterization of a Ligand-independent Oligomerization Domain in the Extracellular Region of the CD95 Death Receptor
Papoff, G., Häusler, P., Eramo, A., Pagano, M. G., Leve, G. D., Signore, A., & Ruberti, G. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.53.38241 · Cited by 181 · see citing works
TNF Recruits TRADD to the Plasma Membrane But Not the trans -Golgi Network, the Principal Subcellular Location of TNF-R1
Jones, S. J., Ledgerwood, E. C., Prins, J. B., Galbraith, J., Johnson, D. R., Pober, J. S., & Bradley, J. R. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.162.2.1042 · Cited by 160 · see citing works
Overexpression of the p80 TNF receptor leads to TNF-dependent apoptosis, nuclear factor-kappa B activation, and c-Jun kinase activation.
Haridas, V., Darnay, B. G., Natarajan, K., Heller, R. A., & Aggarwal, B. B. (1998) · PubMed · Cited by 159 · see citing works
Recombinant 55-kDa tumor necrosis factor (TNF) receptor. Stoichiometry of binding to TNF alpha and TNF beta and inhibition of TNF activity.
Loetscher, H., Gentz, R., Zulauf, M., Lustig, A., Tabuchi, H., Schlaeǵer, E.-J., Brockhaus, M., Gallati, H., Manneberg, M., & Lesslauer, W. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)55273-x · Cited by 148 · see citing works
Structures of the extracellular domain of the type I tumor necrosis factor receptor
Naismith, J. H., Devine, T. Q., Kohno, T., & Sprang, S. R. (1996) · Structure · doi:10.1016/s0969-2126(96)00134-7 · Cited by 147 · see citing works
Measurement of Molecular Interactions in Living Cells by Fluorescence Resonance Energy Transfer Between Variants of the Green Fluorescent Protein
Siegel, R. M., Chan, F. K.-M., Zacharias, D. A., Swofford, R., Holmes, K. L., Tsien, R. Y., & Lenardo, M. J. (2000) · Science s STKE · doi:10.1126/stke.2000.38.pl1 · Cited by 145 · see citing works
Self-citation
Cooperation of Both TNF Receptors in Inducing Apoptosis: Involvement of the TNF Receptor-Associated Factor Binding Domain of the TNF Receptor 75
Declercq, W., Denecker, G., Fiers, W. C., & Vandenabeele, P. (1998) · The Journal of Immunology · doi:10.4049/jimmunol.161.1.390 · Cited by 145 · see citing works
Overexpression of the p80 TNF Receptor Leads to TNF-Dependent Apoptosis, Nuclear Factor-κB Activation, and c-Jun Kinase Activation
Haridas, V., Darnay, B. G., Natarajan, K., Heller, R. A., & Aggarwal, B. B. (1998) · The Journal of Immunology · doi:10.4049/jimmunol.160.7.3152 · Cited by 136 · see citing works
Fluorescence energy transfer measurements on cell surfaces: A critical comparison of steady‐state fluorimetric and flow cytometric methods
Szöllõsi, J., Trón, L., Damjanovich, S., et al. (1984) · Cytometry · doi:10.1002/cyto.990050216 · Cited by 130 · see citing works
Tumor necrosis factor receptor signaling. A dominant negative mutation suppresses the activation of the 55-kDa tumor necrosis factor receptor.
Tartaglia, L. A., & Goeddel, D. V. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42833-5 · Cited by 113 · see citing works
Identification of cysteine-rich domains of the type 1 tumor necrosis factor receptor involved in ligand binding.
Marsters, S. A., Frutkin, A. D., Simpson, N. J., FENDLY, B. M., & Ashkenazi, A. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42615-4 · Cited by 62 · see citing works
Mapping the Domain(s) Critical for the Binding of Human Tumor Necrosis Factor-α to Its Two Receptors
Chen, P. C.-H., DuBois, G. C., & Chen, M.-J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.6.2874 · Cited by 58 · see citing works
Fluorescence Resonance Energy Transfer Reveals Interleukin (IL)-1-dependent Aggregation of IL-1 Type I Receptors That Correlates with Receptor Activation
Guo, C., Dower, S., Holowka, D., & Baird, B. A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.46.27562 · Cited by 51 · see citing works
CD40: A Pivotal Receptor In the Determination of Life/Death Decisions in B Lymphocytes
Klaus, G. G. B., Choi, M. S. K., Lam, E. W. ‐., et al. (1997) · International Reviews of Immunology · doi:10.3109/08830189709068169 · Cited by 37 · see citing works
Differential expression and ligand binding properties of tumor necrosis factor receptor chimeric mutants
Hsu, K. C., & Chao, M. V. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85438-8 · Cited by 26 · see citing works
Conference
Wajant, H., Pfeffer, K., Pfizenmaier, K., et al. (1998) · Cytokine & Growth Factor Reviews · doi:10.1016/s1359-6101(98)00013-6 · Cited by 23 · see citing works
Mechanisms of tumor necrosis factor cytotoxicity and the cytotoxic signals transduced by the p75-tumor necrosis factor receptor.
Reid, T., Louie, P., & Heller, R. A. (1994) · PubMed · Cited by 21 · see citing works
Characterization of ligand binding by the human p55 tumour‐necrosis‐factor receptor
Corcoran, A. E., Barrett, K., Turner, M., et al. (1994) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1994.tb19059.x · Cited by 15 · see citing works
Post-transcriptional regulation of E2A proteins via lipopolysaccharide and CD40 signaling
Meyer, K. B., & Mufti, D. A. H. (2000) · European Journal of Immunology · doi:10.1002/1521-4141(200002)30:2 · Cited by 8 · see citing works
Book review
(1996) · Acta Paediatrica · doi:10.1111/j.1651-2227.1996.tb14158.x · Cited by 1 · see citing works

Flagged first, then by citations

Sorted by citations

Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018.
Galluzzi, L., Vitale, I., Aaronson, S. A., Abrams, J. M., Adam, D., Agostinis, P., Alnemri, E. S., Altucci, L., Amelio, I., Andrews, D. W., et al. (2018) · Cell Death & Differentiation · doi:10.1038/s41418-017-0012-4 · Cited by 6,680 · see citing works
Self-citation
The TNF and TNF Receptor Superfamilies
Locksley, R. M., Killeen, N., & Lenardo, M. J. (2001) · Cell · doi:10.1016/s0092-8674(01)00237-9 · Cited by 3,650 · see citing works
Self-citation
Principles of interleukin (IL)-6-type cytokine signalling and its regulation
HEINRICH, P. C., BEHRMANN, I., HAAN, S., HERMANNS, H. M., MÜLLER-NEWEN, G., & SCHAPER, F. (2003) · Biochemical Journal · doi:10.1042/bj20030407 · Cited by 3,272 · see citing works
Signalling pathways of the TNF superfamily: a double-edged sword
Aggarwal, B. B. (2003) · Nature Reviews Immunology · doi:10.1038/nri1184 · Cited by 2,793 · see citing works
Molecular mechanisms of necroptosis: an ordered cellular explosion
Vandenabeele, P., Galluzzi, L., Vanden Berghe, T., & Kroemer, G. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2970 · Cited by 2,382 · see citing works
TNF-mediated inflammatory disease
Bradley, Jr. (2008) · The Journal of Pathology · doi:10.1002/path.2287 · Cited by 2,094 · see citing works
IL-17 Signaling: The Yin and the Yang
Amatya, N., Garg, A. V., & Gaffen, S. L. (2017) · Trends in Immunology · doi:10.1016/j.it.2017.01.006 · Cited by 785 · see citing works
Neurotrophin Signaling Through the P75 Neurotrophin Receptor
Roux, P. (2002) · Progress in Neurobiology · doi:10.1016/s0301-0082(02)00016-3 · Cited by 717 · see citing works
TNF receptor subtype signalling: Differences and cellular consequences
MacEwan, D. J. (2002) · Cellular Signalling · doi:10.1016/s0898-6568(01)00262-5 · Cited by 610 · see citing works
RANK/RANKL: Regulators of Immune Responses and Bone Physiology
Leibbrandt, A., & Penninger, J. M. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1443.016 · Cited by 420 · see citing works
The many faces of tumor necrosis factor in stroke
Hallenbeck, J. M. (2002) · Nature Medicine · doi:10.1038/nm1202-1363 · Cited by 367 · see citing works
TNFα Transport across the Blood–Brain Barrier Is Abolished in Receptor Knockout Mice
Pan, W., & Kastin, A. J. (2002) · Experimental Neurology · doi:10.1006/exnr.2002.7871 · Cited by 210 · see citing works
Structural Basis and Functional Role of Intramembrane Trimerization of the Fas/CD95 Death Receptor
Fu, Q., Fu, T.-M., Cruz, A. C., Sengupta, P., Thomas, S. K., Wang, S., Siegel, R. M., Wu, H., & Chou, J. J. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.01.009 · Cited by 191 · see citing works
Self-citation
New knowledge on critical osteoclast formation and activation pathways from study of rare genetic diseases of osteoclasts: focus on the RANK/RANKL axis
Crockett, J. C., Mellis, D. J., Scott, D. I., & Helfrich, M. H. (2011) · Osteoporosis International · doi:10.1007/s00198-010-1272-8 · Cited by 143 · see citing works
Caspase-10 Negatively Regulates Caspase-8-Mediated Cell Death, Switching the Response to CD95L in Favor of NF-κB Activation and Cell Survival
Horn, S., Hughes, M. A., Schilling, R., Sticht, C., Tenev, T., Ploesser, M., Meier, P., Sprick, M. R., MacFarlane, M., & Leverkus, M. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.04.010 · Cited by 119 · see citing works
Intra- and Interdimeric Caspase-8 Self-Cleavage Controls Strength and Timing of CD95-Induced Apoptosis
Kallenberger, S. M., Beaudouin, J., Claus, J., Fischer, C., Sorger, P. K., Legewie, S., & Eils, R. (2014) · Science Signaling · doi:10.1126/scisignal.2004738 · Cited by 76 · see citing works

Influence of extracellular ion concentration on the intracellular accumulation of adriamycin.
Nishikawa, K., Asaumi, J. I., Kawasaki, S., et al. (1998) · PubMed
Unexpected Relationship of Extracellular ATP with Intracellular Ca Concentration in HepG2 Cells
Caner, A., Bıtgen, N., & Önal, M. G. (2019) · International Journal of Medical Research & Health Sciences
Interaction of extracellular calcium and magnesium in the regulation of cytosolic calcium and PTH release in dispersed bovine parathyroid cells
Shoback, D., Thatcher, J., & Brown, E. M. (1984) · Molecular and Cellular Endocrinology · doi:10.1016/0303-7207(84)90116-3 · Cited by 26 · see citing works
EXTRACELLULAR POTENTIALS FROM SINGLE SPINAL MOTONEURONS
Freygang, W. H., & Frank, K. (1959) · The Journal of General Physiology · doi:10.1085/jgp.42.4.749 · Cited by 113 · see citing works
Enhancement of intracellular calcium concentration by extracellular ATP and UTP in madin darby canine kidney cells
Paulmichl, M., & Lang, F. J. W. (1988) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(88)80751-4 · Cited by 36 · see citing works

Authors: Chan, F. K.-M., Chun, H. J., Zheng, L., Siegel, R. M., Bui, K. L., & Lenardo, M. J.
Affiliations: National Institutes of Health (US)
Corresponding author: Bui, Kimmie L.
Lenardo, Michael J.
ORCID: Chan, Francis Ka-Ming
Chun, Hyung J.
Zheng, Lixin
Siegel, Richard M.
Lenardo, Michael J.
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 2000-06-30
Volume: 288
Issue: 5475
Pages: 2351-2354
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.288.5475.2351
OpenAlex: W1985720487
Cited by: 856
References: 46
Citations by year: 2026: 16 · 2025: 15 · 2024: 23 · 2023: 22 · 2022: 26 · 2021: 29 · 2020: 29 · 2019: 23 · 2018: 25 · 2017: 29 · 2016: 19 · 2015: 29 · 2014: 33 · 2013: 34 · 2012: 32
FWCI: 22.62
Type: journal article
Language: en
Open access: closed
Locations: Science (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
Health Sciences › Medicine › Oncology › Cytokine Signaling Pathways and Interactions
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
Keywords: TNF receptor, TNF signaling, TRAIL receptor 1, CD40, receptor oligomerization, extracellular domain
MeSH terms: Binding Sites, Cross-Linking Reagents, Energy Transfer, Fluorescence, Humans, Ligands, Mutation, Protein Conformation, Recombinant Fusion Proteins, Succinimides, Tumor Cells, Cultured, Tumor Necrosis Factor-alpha, Signal Transduction, Antigens, CD, Apoptosis, Protein Structure, Tertiary, Receptors, Tumor Necrosis Factor, Dimerization, Amino Acid Substitution, Macromolecular Substances, Receptors, Tumor Necrosis Factor, Type I, Receptors, Tumor Necrosis Factor, Type II

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

A Domain in TNF Receptors That Mediates Ligand-Independent Receptor Assembly and Signaling

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Cites

Cited by

Related

Record

About these checks