Cited by 76

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Molecular insights into the multilayered regulation of ADAM17: The role of the extracellular region

Grötzinger, Joachim, Lorenzen, Inken, Düsterhöft, Stefan·2017·Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

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.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1016/j.bbamcr.2017.05.024

Cites

2 of 2 references verified0 citation errors · 0 not checkable

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.

A few free checks a day · papers already verified open instantly · results are public

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.

Citations

Cites

Flagged first, then by citations

Research works printed but not linked: 73

  1. Moss, 1997, Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-alpha, Nature, 385, 733, 10.1038/385733a0 · DOI · Paper page
  2. Chalaris, 2010, Critical role of the disintegrin metalloprotease ADAM17 for intestinal inflammation and regeneration in mice, J. Exp. Med., 207, 1617, 10.1084/jem.20092366 · DOI
  3. Blaydon, 2011, Inflammatory skin and bowel disease linked to ADAM17 deletion, N. Engl. J. Med., 365, 1502, 10.1056/NEJMoa1100721 · DOI
  4. Peschon, 1998, An essential role for ectodomain shedding in mammalian development, Science, 282, 1281, 10.1126/science.282.5392.1281 · DOI
  5. Horiuchi, 2007, Substrate selectivity of epidermal growth factor-receptor ligand sheddases and their regulation by phorbol esters and calcium influx, Mol. Biol. Cell, 18, 176, 10.1091/mbc.e06-01-0014 · DOI
  6. Reddy, 2000, Functional analysis of the domain structure of tumor necrosis factor-alpha converting enzyme, J. Biol. Chem., 275, 14608, 10.1074/jbc.275.19.14608 · DOI
  7. Müllberg, 1993, The soluble interleukin-6 receptor is generated by shedding, Eur. J. Immunol., 23, 473, 10.1002/eji.1830230226 · DOI
  8. Jones, 2011, Therapeutic strategies for the clinical blockade of IL-6/gp130 signaling, J. Clin. Invest., 121, 3375, 10.1172/JCI57158 · DOI
  9. Le Gall, 2010, ADAM17 is regulated by a rapid and reversible mechanism that controls access to its catalytic site, J. Cell Sci., 123, 3913, 10.1242/jcs.069997 · DOI
  10. Göoz, 2010, ADAM-17: the enzyme that does it all, Crit. Rev. Biochem. Mol. Biol., 45, 146, 10.3109/10409231003628015 · DOI · Paper page
  11. Düsterhöft, 2013, Membrane-proximal domain of a disintegrin and metalloprotease-17 represents the putative molecular switch of its shedding activity operated by protein-disulfide isomerase, J. Am. Chem. Soc., 135, 5776, 10.1021/ja400340u · DOI
  12. Düsterhöft, 2014, A disintegrin and metalloprotease 17 dynamic interaction sequence, the sweet tooth for the human interleukin 6 receptor, J. Biol. Chem., 289, 16336, 10.1074/jbc.M114.557322 · DOI
  13. Lorenzen, 2012, The membrane-proximal domain of A Disintegrin and Metalloprotease 17 (ADAM17) is responsible for recognition of the interleukin-6 receptor and interleukin-1 receptor II, FEBS Lett., 586, 1093, 10.1016/j.febslet.2012.03.012 · DOI
  14. Sommer, 2016, How membrane asymmetry regulates ADAM17 sheddase function, Cell Cycle, 15, 2995, 10.1080/15384101.2016.1211449 · DOI
  15. Milla, 1999, Specific sequence elements are required for the expression of functional tumor necrosis factor-alpha-converting enzyme (TACE), J. Biol. Chem., 274, 30563, 10.1074/jbc.274.43.30563 · DOI
  16. Wong, 2016, Harnessing the natural inhibitory domain to control TNFalpha Converting Enzyme (TACE) activity in vivo, Sci. Rep., 6, 35598, 10.1038/srep35598 · DOI
  17. Maskos, 1998, Crystal structure of the catalytic domain of human tumor necrosis factor-alpha-converting enzyme, Proc. Natl. Acad. Sci. U. S. A., 95, 3408, 10.1073/pnas.95.7.3408 · DOI
  18. Tucher, 2014, LC-MS based cleavage site profiling of the proteases ADAM10 and ADAM17 using proteome-derived peptide libraries, J. Proteome Res., 13, 2205, 10.1021/pr401135u · DOI
  19. Riethmüller, 2017, Proteolytic origin of the soluble human IL-6R in vivo and a decisive role of N-glycosylation, PLoS Biol., 15
  20. Murphy, 2011, Tissue inhibitors of metalloproteinases, Genome Biol., 12, 233, 10.1186/gb-2011-12-11-233 · DOI
  21. Wisniewska, 2008, Structural determinants of the ADAM inhibition by TIMP-3: crystal structure of the TACE-N-TIMP-3 complex, J. Mol. Biol., 381, 1307, 10.1016/j.jmb.2008.06.088 · DOI
  22. Lee, 2002, Engineering N-terminal domain of tissue inhibitor of metalloproteinase (TIMP)-3 to be a better inhibitor against tumour necrosis factor-alpha-converting enzyme, Biochem. J., 364, 227, 10.1042/bj3640227 · DOI
  23. Mavilio, 2016, A role for Timp3 in microbiota-driven hepatic steatosis and metabolic dysfunction, Cell Rep., 16, 731, 10.1016/j.celrep.2016.06.027 · DOI
  24. Janes, 2005, Adam meets Eph: an ADAM substrate recognition module acts as a molecular switch for ephrin cleavage in trans, Cell, 123, 291, 10.1016/j.cell.2005.08.014 · DOI
  25. Toquet, 2012, ADAM15 to alpha5beta1 integrin switch in colon carcinoma cells: a late event in cancer progression associated with tumor dedifferentiation and poor prognosis, Int. J. Cancer, 130, 278, 10.1002/ijc.25891 · DOI
  26. Lu, 2010, ADAM-15 disintegrin-like domain structure and function, Toxins (Basel), 2, 2411, 10.3390/toxins2102411 · DOI
  27. Takahashi, 2001, Sequence-specific interaction between the disintegrin domain of mouse ADAM 3 and murine eggs: role of beta1 integrin-associated proteins CD9, CD81, and CD98, Mol. Biol. Cell, 12, 809, 10.1091/mbc.12.4.809 · DOI
  28. Eto, 2000, RGD-independent binding of integrin alpha9beta1 to the ADAM-12 and -15 disintegrin domains mediates cell-cell interaction, J. Biol. Chem., 275, 34922, 10.1074/jbc.M001953200 · DOI
  29. Zigrino, 2011, The disintegrin-like and cysteine-rich domains of ADAM-9 mediate interactions between melanoma cells and fibroblasts, J. Biol. Chem., 286, 6801, 10.1074/jbc.M110.168617 · DOI
  30. Zigrino, 2007, Role of ADAM-9 disintegrin-cysteine-rich domains in human keratinocyte migration, J. Biol. Chem., 282, 30785, 10.1074/jbc.M701658200 · DOI
  31. Bridges, 2005, ADAM disintegrin-like domain recognition by the lymphocyte integrins alpha4beta1 and alpha4beta7, Biochem. J., 387, 101, 10.1042/BJ20041444 · DOI
  32. Huang, 2005, Selective modulation of integrin-mediated cell migration by distinct ADAM family members, Mol. Biol. Cell, 16, 4982, 10.1091/mbc.e05-03-0258 · DOI
  33. Bax, 2004, Integrin alpha5beta1 and ADAM-17 interact in vitro and co-localize in migrating HeLa cells, J. Biol. Chem., 279, 22377, 10.1074/jbc.M400180200 · DOI
  34. Göoz, 2012, A disintegrin and metalloenzyme (ADAM) 17 activation is regulated by alpha5beta1 integrin in kidney mesangial cells, PLoS One, 7, 10.1371/journal.pone.0033350 · DOI
  35. Trad, 2013, ADAM17-overexpressing breast cancer cells selectively targeted by antibody-toxin conjugates, Cancer Immunol. Immunother., 62, 411, 10.1007/s00262-012-1346-x · DOI
  36. Saha, 2010, Helicobacter pylori CagL activates ADAM17 to induce repression of the gastric H, K-ATPase alpha subunit, Gastroenterology, 139, 239, 10.1053/j.gastro.2010.03.036 · DOI
  37. Edwards, 2008, The ADAM metalloproteinases, Mol. Asp. Med., 29, 258, 10.1016/j.mam.2008.08.001 · DOI
  38. Willems, 2010, Thiol isomerases negatively regulate the cellular shedding activity of ADAM17, Biochem. J., 428, 439, 10.1042/BJ20100179 · DOI
  39. Bennett, 2000, Sulfhydryl regulation of L-selectin shedding: phenylarsine oxide promotes activation-independent L-selectin shedding from leukocytes, J. Immunol., 164, 4120, 10.4049/jimmunol.164.8.4120 · DOI
  40. Wang, 2009, Regulation of mature ADAM17 by redox agents for L-selectin shedding, J. Immunol., 182, 2449, 10.4049/jimmunol.0802770 · DOI
  41. Sommer, 2016, Phosphatidylserine exposure is required for ADAM17 sheddase function, Nat. Commun., 7, 11523, 10.1038/ncomms11523 · DOI
  42. Lemmon, 2008, Membrane recognition by phospholipid-binding domains, Nat. Rev. Mol. Cell Biol., 9, 99, 10.1038/nrm2328 · DOI · Paper page
  43. Leonard, 2005, Chaperone-like properties of the prodomain of TNFalpha-converting enzyme (TACE) and the functional role of its cysteine switch, Biochem. J., 387, 797, 10.1042/BJ20041727 · DOI
  44. Düsterhöft, 2015, Extracellular juxtamembrane segment of ADAM17 interacts with membranes and is essential for its shedding activity, Biochemistry, 54, 5791, 10.1021/acs.biochem.5b00497 · DOI
  45. Tellier, 2006, The shedding activity of ADAM17 is sequestered in lipid rafts, Exp. Cell Res., 312, 3969, 10.1016/j.yexcr.2006.08.027 · DOI
  46. Matthews, 2003, Cellular cholesterol depletion triggers shedding of the human interleukin-6 receptor by ADAM10 and ADAM17 (TACE), J. Biol. Chem., 278, 38829, 10.1074/jbc.M210584200 · DOI · Paper page
  47. Riethmüller, 2016, Cleavage site localization differentially controls interleukin-6 receptor proteolysis by ADAM10 and ADAM17, Sci. Rep., 6, 25550, 10.1038/srep25550 · DOI
  48. Lorenzen, 2011, Multimerisation of A disintegrin and metalloprotease protein-17 (ADAM17) is mediated by its EGF-like domain, Biochem. Biophys. Res. Commun., 10.1016/j.bbrc.2011.10.056 · DOI
  49. Rozanov, 2001, J. Biol. Chem., 276, 25705, 10.1074/jbc.M007921200 · DOI
  50. Tochowicz, 2011, The dimer interface of the membrane type 1 matrix metalloproteinase hemopexin domain: crystal structure and biological functions, J. Biol. Chem., 286, 7587, 10.1074/jbc.M110.178434 · DOI
  51. Xu, 2012, TACE activation by MAPK-mediated regulation of cell surface dimerization and TIMP3 association, Sci. Signal., 5, 10.1126/scisignal.2002689 · DOI
  52. Xu, 2010, Direct activation of TACE-mediated ectodomain shedding by p38 MAP kinase regulates EGF receptor-dependent cell proliferation, Mol. Cell, 37, 551, 10.1016/j.molcel.2010.01.034 · DOI
  53. Killock, 2010, The cytoplasmic domains of TNFalpha-converting enzyme (TACE/ADAM17) and L-selectin are regulated differently by p38 MAPK and PKC to promote ectodomain shedding, Biochem. J., 428, 293, 10.1042/BJ20091611 · DOI
  54. Kveiborg, 2011, PKCalpha and PKCdelta regulate ADAM17-mediated ectodomain shedding of heparin binding-EGF through separate pathways, PLoS One, 6, 10.1371/journal.pone.0017168 · DOI
  55. Dang, 2013, Regulated ADAM17-dependent EGF family ligand release by substrate-selecting signaling pathways, Proc. Natl. Acad. Sci. U. S. A., 110, 9776, 10.1073/pnas.1307478110 · DOI
  56. Adrain, 2012, Tumor necrosis factor signaling requires iRhom2 to promote trafficking and activation of TACE, Science, 335, 225, 10.1126/science.1214400 · DOI
  57. McIlwain, 2012, iRhom2 regulation of TACE controls TNF-mediated protection against Listeria and responses to LPS, Science, 335, 229, 10.1126/science.1214448 · DOI
  58. Siggs, 2012, iRhom2 is required for the secretion of mouse TNFalpha, Blood, 119, 5769, 10.1182/blood-2012-03-417949 · DOI
  59. Maretzky, 2013, iRhom2 controls the substrate selectivity of stimulated ADAM17-dependent ectodomain shedding, Proc. Natl. Acad. Sci. U. S. A., 110, 11433, 10.1073/pnas.1302553110 · DOI
  60. Grieve, 2017, Phosphorylation of iRhom2 at the plasma membrane controls mammalian TACE-dependent inflammatory and growth factor signalling, elife, 6, 10.7554/eLife.23968 · DOI
  61. Schwarz, 2014, Polo-like kinase 2, a novel ADAM17 signaling component, regulates tumor necrosis factor alpha ectodomain shedding, J. Biol. Chem., 289, 3080, 10.1074/jbc.M113.536847 · DOI
  62. Gechtman, 1999, The shedding of membrane-anchored heparin-binding epidermal-like growth factor is regulated by the Raf/mitogen-activated protein kinase cascade and by cell adhesion and spreading, J. Biol. Chem., 274, 28828, 10.1074/jbc.274.40.28828 · DOI
  63. Diaz-Rodriguez, 2002, Extracellular signal-regulated kinase phosphorylates tumor necrosis factor alpha-converting enzyme at threonine 735: a potential role in regulated shedding, Mol. Biol. Cell, 13, 2031, 10.1091/mbc.01-11-0561 · DOI
  64. Soond, 2005, ERK-mediated phosphorylation of Thr735 in TNFalpha-converting enzyme and its potential role in TACE protein trafficking, J. Cell Sci., 118, 2371, 10.1242/jcs.02357 · DOI
  65. Doedens, 2000, Stimulation-induced down-regulation of tumor necrosis factor-alpha converting enzyme, J. Biol. Chem., 275, 14598, 10.1074/jbc.275.19.14598 · DOI
  66. Endres, 2003, Tumor necrosis factor-alpha converting enzyme is processed by proprotein-convertases to its mature form which is degraded upon phorbol ester stimulation, Eur. J. Biochem., 270, 2386, 10.1046/j.1432-1033.2003.03606.x · DOI
  67. Dombernowsky, 2015, The sorting protein PACS-2 promotes ErbB signalling by regulating recycling of the metalloproteinase ADAM17, Nat. Commun., 6, 7518, 10.1038/ncomms8518 · DOI
  68. Lorenzen, 2016, Control of ADAM17 activity by regulation of its cellular localisation, Sci. Rep., 6, 35067, 10.1038/srep35067 · DOI
  69. Ostalecki, 2016, HIV Nef- and Notch1-dependent endocytosis of ADAM17 induces vesicular TNF secretion in chronic HIV infection, EBioMedicine, 13, 294, 10.1016/j.ebiom.2016.10.027 · DOI
  70. Percario, 2015, Nef, the shuttling molecular adaptor of HIV, influences the cytokine network, Cytokine Growth Factor Rev., 26, 159, 10.1016/j.cytogfr.2014.11.010 · DOI
  71. Lee, 2013, HIV Nef, paxillin, and Pak1/2 regulate activation and secretion of TACE/ADAM10 proteases, Mol. Cell, 49, 668, 10.1016/j.molcel.2012.12.004 · DOI
  72. Lee, 2016, HIV-Nef and ADAM17-containing plasma extracellular vesicles induce and correlate with immune pathogenesis in chronic HIV infection, EBioMedicine, 6, 103, 10.1016/j.ebiom.2016.03.004 · DOI
  73. Groth, 2016, Stimulated release and functional activity of surface expressed metalloproteinase ADAM17 in exosomes, Biochim. Biophys. Acta, 1863, 2795, 10.1016/j.bbamcr.2016.09.002 · DOI

Cited by

Sorted by citations

Metadata

Authors
Grötzinger, J., Lorenzen, I., & Düsterhöft, S.
Venue
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
Publisher
Elsevier BV
Published
2017-11
Volume
1864
Issue
11
Pages
2088-2095
ISSN
0167-4889
Cited by
76
References
2
Language
en
Funders
German Research Foundation (SFB877, DU 1582/1-1, 1710)

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