BPG is committed to discovery and dissemination of knowledge
Cited by in F6Publishing
For: Jones JC, Rustagi S, Dempsey PJ. ADAM Proteases and Gastrointestinal Function. Annu Rev Physiol 2016;78:243-76. [PMID: 26667078 DOI: 10.1146/annurev-physiol-021014-071720] [Cited by in Crossref: 35] [Cited by in F6Publishing: 33] [Article Influence: 5.0] [Reference Citation Analysis]
Number Citing Articles
1 Tanzer MC, Frauenstein A, Stafford CA, Phulphagar K, Mann M, Meissner F. Quantitative and Dynamic Catalogs of Proteins Released during Apoptotic and Necroptotic Cell Death. Cell Reports 2020;30:1260-1270.e5. [DOI: 10.1016/j.celrep.2019.12.079] [Cited by in Crossref: 14] [Cited by in F6Publishing: 10] [Article Influence: 7.0] [Reference Citation Analysis]
2 Wu B, Cui J, Yang XM, Liu ZY, Song F, Li L, Jiang JL, Chen ZN. Cytoplasmic fragment of CD147 generated by regulated intramembrane proteolysis contributes to HCC by promoting autophagy. Cell Death Dis. 2017;8:e2925. [PMID: 28703811 DOI: 10.1038/cddis.2017.251] [Cited by in Crossref: 19] [Cited by in F6Publishing: 20] [Article Influence: 3.8] [Reference Citation Analysis]
3 Hsia HE, Tüshaus J, Feng X, Hofmann LI, Wefers B, Marciano DK, Wurst W, Lichtenthaler SF. Endoglycan (PODXL2) is proteolytically processed by ADAM10 (a disintegrin and metalloprotease 10) and controls neurite branching in primary neurons. FASEB J 2021;35:e21813. [PMID: 34390512 DOI: 10.1096/fj.202100475R] [Reference Citation Analysis]
4 Jones JC, Brindley CD, Elder NH, Myers MG Jr, Rajala MW, Dekaney CM, McNamee EN, Frey MR, Shroyer NF, Dempsey PJ. Cellular Plasticity of Defa4Cre-Expressing Paneth Cells in Response to Notch Activation and Intestinal Injury. Cell Mol Gastroenterol Hepatol 2019;7:533-54. [PMID: 30827941 DOI: 10.1016/j.jcmgh.2018.11.004] [Cited by in Crossref: 36] [Cited by in F6Publishing: 35] [Article Influence: 9.0] [Reference Citation Analysis]
5 Zhu G, Liu J, Wang Y, Jia N, Wang W, Zhang J, Liang Y, Tian H, Zhang J. ADAM17 Mediates Hypoxia-Induced Keratinocyte Migration via the p38/MAPK Pathway. Biomed Res Int 2021;2021:8328216. [PMID: 34746310 DOI: 10.1155/2021/8328216] [Reference Citation Analysis]
6 Tüshaus J, Müller SA, Shrouder J, Arends M, Simons M, Plesnila N, Blobel CP, Lichtenthaler SF. The pseudoprotease iRhom1 controls ectodomain shedding of membrane proteins in the nervous system. FASEB J 2021;35:e21962. [PMID: 34613632 DOI: 10.1096/fj.202100936R] [Reference Citation Analysis]
7 Gao S, Wu F, Chen X, Yang Y, Zhu Y, Xiao L, Shang J, Bao X, Luo Y, Chen H, Liu Q. Sex-Biased Gene Expression of Mesobuthus martensii Collected from Gansu Province, China, Reveals Their Different Therapeutic Potentials. Evid Based Complement Alternat Med 2021;2021:1967158. [PMID: 34462639 DOI: 10.1155/2021/1967158] [Reference Citation Analysis]
8 Heidmann O, Béguin A, Paternina J, Berthier R, Deloger M, Bawa O, Heidmann T. HEMO, an ancestral endogenous retroviral envelope protein shed in the blood of pregnant women and expressed in pluripotent stem cells and tumors. Proc Natl Acad Sci U S A 2017;114:E6642-51. [PMID: 28739914 DOI: 10.1073/pnas.1702204114] [Cited by in Crossref: 32] [Cited by in F6Publishing: 25] [Article Influence: 6.4] [Reference Citation Analysis]
9 Mandal P, Feng Y, Lyons JD, Berger SB, Otani S, DeLaney A, Tharp GK, Maner-Smith K, Burd EM, Schaeffer M, Hoffman S, Capriotti C, Roback L, Young CB, Liang Z, Ortlund EA, DiPaolo NC, Bosinger S, Bertin J, Gough PJ, Brodsky IE, Coopersmith CM, Shayakhmetov DM, Mocarski ES. Caspase-8 Collaborates with Caspase-11 to Drive Tissue Damage and Execution of Endotoxic Shock. Immunity 2018;49:42-55.e6. [PMID: 30021146 DOI: 10.1016/j.immuni.2018.06.011] [Cited by in Crossref: 56] [Cited by in F6Publishing: 55] [Article Influence: 18.7] [Reference Citation Analysis]
10 Seegar TCM, Killingsworth LB, Saha N, Meyer PA, Patra D, Zimmerman B, Janes PW, Rubinstein E, Nikolov DB, Skiniotis G, Kruse AC, Blacklow SC. Structural Basis for Regulated Proteolysis by the α-Secretase ADAM10. Cell 2017;171:1638-1648.e7. [PMID: 29224781 DOI: 10.1016/j.cell.2017.11.014] [Cited by in Crossref: 66] [Cited by in F6Publishing: 60] [Article Influence: 13.2] [Reference Citation Analysis]
11 Sikora-skrabaka M, Walkiewicz K, Nowakowska-zajdel E. Adamalizyny jako potencjalne biomarkery w wybranych nowotworach złośliwych przewodu pokarmowego. Postępy Higieny i Medycyny Doświadczalnej 2021;75:674-82. [DOI: 10.2478/ahem-2021-0020] [Reference Citation Analysis]
12 Wichert R, Ermund A, Schmidt S, Schweinlin M, Ksiazek M, Arnold P, Knittler K, Wilkens F, Potempa B, Rabe B, Stirnberg M, Lucius R, Bartsch JW, Nikolaus S, Falk-Paulsen M, Rosenstiel P, Metzger M, Rose-John S, Potempa J, Hansson GC, Dempsey PJ, Becker-Pauly C. Mucus Detachment by Host Metalloprotease Meprin β Requires Shedding of Its Inactive Pro-form, which Is Abrogated by the Pathogenic Protease RgpB. Cell Rep 2017;21:2090-103. [PMID: 29166602 DOI: 10.1016/j.celrep.2017.10.087] [Cited by in Crossref: 19] [Cited by in F6Publishing: 19] [Article Influence: 4.8] [Reference Citation Analysis]
13 Duhachek-Muggy S, Qi Y, Wise R, Alyahya L, Li H, Hodge J, Zolkiewska A. Metalloprotease-disintegrin ADAM12 actively promotes the stem cell-like phenotype in claudin-low breast cancer. Mol Cancer 2017;16:32. [PMID: 28148288 DOI: 10.1186/s12943-017-0599-6] [Cited by in Crossref: 25] [Cited by in F6Publishing: 26] [Article Influence: 5.0] [Reference Citation Analysis]
14 Brummer T, Pigoni M, Rossello A, Wang H, Noy PJ, Tomlinson MG, Blobel CP, Lichtenthaler SF. The metalloprotease ADAM10 (a disintegrin and metalloprotease 10) undergoes rapid, postlysis autocatalytic degradation. FASEB J 2018;32:3560-73. [PMID: 29430990 DOI: 10.1096/fj.201700823RR] [Cited by in Crossref: 15] [Cited by in F6Publishing: 11] [Article Influence: 3.8] [Reference Citation Analysis]
15 Tan Y, Fu R, Liu J, Wu Y, Wang B, Jiang N, Nie P, Cao H, Yang Z, Fang B. ADAM10 is essential for cranial neural crest-derived maxillofacial bone development. Biochem Biophys Res Commun 2016;475:308-14. [PMID: 27221046 DOI: 10.1016/j.bbrc.2016.05.101] [Cited by in Crossref: 7] [Cited by in F6Publishing: 6] [Article Influence: 1.2] [Reference Citation Analysis]
16 von Hoven G, Rivas A, Neukirch C, Klein S, Hamm C, Qin Q, Meyenburg M, Füser S, Saftig P, Hellmann N, Postina R, Husmann M. Dissecting the role of ADAM10 as a mediator of Staphylococcus aureus α-toxin action. Biochemical Journal 2016;473:1929-40. [DOI: 10.1042/bcj20160062] [Cited by in Crossref: 23] [Cited by in F6Publishing: 14] [Article Influence: 3.8] [Reference Citation Analysis]
17 Frick A, Khare V, Jimenez K, Dammann K, Lang M, Krnjic A, Gmainer C, Baumgartner M, Mesteri I, Gasche C. A Novel PAK1-Notch1 Axis Regulates Crypt Homeostasis in Intestinal Inflammation. Cell Mol Gastroenterol Hepatol 2021;11:892-907.e1. [PMID: 33189893 DOI: 10.1016/j.jcmgh.2020.11.001] [Reference Citation Analysis]
18 Sun L, Chen B, Wu J, Jiang C, Fan Z, Feng Y, Xu Y. Epigenetic Regulation of a Disintegrin and Metalloproteinase (ADAM) Transcription in Colorectal Cancer Cells: Involvement of β-Catenin, BRG1, and KDM4. Front Cell Dev Biol 2020;8:581692. [PMID: 33043016 DOI: 10.3389/fcell.2020.581692] [Cited by in Crossref: 18] [Cited by in F6Publishing: 18] [Article Influence: 9.0] [Reference Citation Analysis]
19 Mullooly M, McGowan PM, Crown J, Duffy MJ. The ADAMs family of proteases as targets for the treatment of cancer. Cancer Biol Ther 2016;17:870-80. [PMID: 27115328 DOI: 10.1080/15384047.2016.1177684] [Cited by in Crossref: 48] [Cited by in F6Publishing: 49] [Article Influence: 8.0] [Reference Citation Analysis]
20 Mitsuyama K, Tsuruta K, Takedatsu H, Yoshioka S, Morita M, Niwa M, Matsumoto S. Clinical Features and Pathogenic Mechanisms of Gastrointestinal Injury in COVID-19. J Clin Med. 2020;9:3630. [PMID: 33187280 DOI: 10.3390/jcm9113630] [Cited by in Crossref: 3] [Cited by in F6Publishing: 4] [Article Influence: 1.5] [Reference Citation Analysis]
21 Adu-Amankwaah J, Adzika GK, Adekunle AO, Ndzie Noah ML, Mprah R, Bushi A, Akhter N, Huang F, Xu Y, Adzraku SY, Nadeem I, Sun H. ADAM17, A Key Player of Cardiac Inflammation and Fibrosis in Heart Failure Development During Chronic Catecholamine Stress. Front Cell Dev Biol 2021;9:732952. [PMID: 34966735 DOI: 10.3389/fcell.2021.732952] [Reference Citation Analysis]
22 Villalba-Rodríguez AM, Martínez-González S, Sosa-Hernández JE, Parra-Saldívar R, Bilal M, Iqbal HMN. Nanoclay/Polymer-Based Hydrogels and Enzyme-Loaded Nanostructures for Wound Healing Applications. Gels 2021;7:59. [PMID: 34068868 DOI: 10.3390/gels7020059] [Reference Citation Analysis]
23 Zhu H, Wang J, Nie W, Armando I, Han F. ADAMs family in kidney physiology and pathology. EBioMedicine 2021;72:103628. [PMID: 34653870 DOI: 10.1016/j.ebiom.2021.103628] [Reference Citation Analysis]
24 Dixit G, Schanz W, Pappas BA, Maretzky T. Members of the Fibroblast Growth Factor Receptor Superfamily Are Proteolytically Cleaved by Two Differently Activated Metalloproteases. Int J Mol Sci 2021;22:3165. [PMID: 33804608 DOI: 10.3390/ijms22063165] [Cited by in Crossref: 3] [Cited by in F6Publishing: 3] [Article Influence: 3.0] [Reference Citation Analysis]
25 Schmidt-Arras D, Rose-John S. Regulation of Fibrotic Processes in the Liver by ADAM Proteases. Cells 2019;8:E1226. [PMID: 31601007 DOI: 10.3390/cells8101226] [Cited by in Crossref: 5] [Cited by in F6Publishing: 5] [Article Influence: 1.7] [Reference Citation Analysis]
26 Dreymueller D, Ludwig A. Considerations on inhibition approaches for proinflammatory functions of ADAM proteases. Platelets 2017;28:354-61. [PMID: 27460023 DOI: 10.1080/09537104.2016.1203396] [Cited by in Crossref: 16] [Cited by in F6Publishing: 16] [Article Influence: 2.7] [Reference Citation Analysis]
27 Ouyang S, Jia B, Xie W, Yang J, Lv Y. Mechanism underlying the regulation of sortilin expression and its trafficking function. J Cell Physiol 2020;235:8958-71. [PMID: 32474917 DOI: 10.1002/jcp.29818] [Cited by in Crossref: 3] [Article Influence: 1.5] [Reference Citation Analysis]
28 Dempsey PJ. Role of ADAM10 in intestinal crypt homeostasis and tumorigenesis. Biochim Biophys Acta Mol Cell Res 2017;1864:2228-39. [PMID: 28739265 DOI: 10.1016/j.bbamcr.2017.07.011] [Cited by in Crossref: 11] [Cited by in F6Publishing: 12] [Article Influence: 2.2] [Reference Citation Analysis]
29 Shen S, Ke Y, Dang E, Fang H, Chang Y, Zhang J, Zhu Z, Shao S, Qiao P, Zhang T, Qiao H, Wang G. Semaphorin 4D from CD15+ Granulocytes via ADAM10-Induced Cleavage Contributes to Antibody Production in Bullous Pemphigoid. J Invest Dermatol 2018;138:588-97. [PMID: 29054606 DOI: 10.1016/j.jid.2017.09.037] [Cited by in Crossref: 6] [Cited by in F6Publishing: 6] [Article Influence: 1.2] [Reference Citation Analysis]
30 Dong W, Liu L, Dou Y, Xu M, Liu T, Wang S, Zhang Y, Deng B, Wang B, Cao H. Deoxycholic acid activates epidermal growth factor receptor and promotes intestinal carcinogenesis by ADAM17-dependent ligand release. J Cell Mol Med 2018;22:4263-73. [PMID: 29956475 DOI: 10.1111/jcmm.13709] [Cited by in Crossref: 10] [Cited by in F6Publishing: 11] [Article Influence: 2.5] [Reference Citation Analysis]
31 Posselt G, Crabtree JE, Wessler S. Proteolysis in Helicobacter pylori-Induced Gastric Cancer. Toxins (Basel) 2017;9:E134. [PMID: 28398251 DOI: 10.3390/toxins9040134] [Cited by in Crossref: 13] [Cited by in F6Publishing: 14] [Article Influence: 2.6] [Reference Citation Analysis]
32 Lokau J, Agthe M, Flynn CM, Garbers C. Proteolytic control of Interleukin-11 and Interleukin-6 biology. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 2017;1864:2105-17. [DOI: 10.1016/j.bbamcr.2017.06.008] [Cited by in Crossref: 18] [Cited by in F6Publishing: 19] [Article Influence: 3.6] [Reference Citation Analysis]
33 Kishida K, Pearce SC, Yu S, Gao N, Ferraris RP. Nutrient sensing by absorptive and secretory progenies of small intestinal stem cells. Am J Physiol Gastrointest Liver Physiol 2017;312:G592-605. [PMID: 28336548 DOI: 10.1152/ajpgi.00416.2016] [Cited by in Crossref: 21] [Cited by in F6Publishing: 17] [Article Influence: 4.2] [Reference Citation Analysis]
34 Zunke F, Rose-john S. The shedding protease ADAM17: Physiology and pathophysiology. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 2017;1864:2059-70. [DOI: 10.1016/j.bbamcr.2017.07.001] [Cited by in Crossref: 127] [Cited by in F6Publishing: 117] [Article Influence: 25.4] [Reference Citation Analysis]
35 Fu J, Li L, Yang X, Yang R, Amjad N, Liu L, Tan C, Chen H, Wang X. Transactivated Epidermal Growth Factor Receptor Recruitment of α-actinin-4 From F-actin Contributes to Invasion of Brain Microvascular Endothelial Cells by Meningitic Escherichia coli. Front Cell Infect Microbiol 2018;8:448. [PMID: 30687645 DOI: 10.3389/fcimb.2018.00448] [Cited by in Crossref: 4] [Cited by in F6Publishing: 7] [Article Influence: 1.3] [Reference Citation Analysis]
36 Wang G, Huang Y, Hu T, Zhang B, Tang Z, Yao R, Huang Y, Fan X, Ni X. Contribution of placental 11β-HSD2 to the pathogenesis of preeclampsia. FASEB J 2020;34:15379-99. [PMID: 32978833 DOI: 10.1096/fj.202001003RR] [Cited by in Crossref: 1] [Article Influence: 0.5] [Reference Citation Analysis]
37 Begum Y, Pandit A, Swarnakar S. Insights Into the Regulation of Gynecological Inflammation-Mediated Malignancy by Metalloproteinases. Front Cell Dev Biol 2021;9:780510. [PMID: 34912809 DOI: 10.3389/fcell.2021.780510] [Reference Citation Analysis]
38 Mishra HK, Ma J, Walcheck B. Ectodomain Shedding by ADAM17: Its Role in Neutrophil Recruitment and the Impairment of This Process during Sepsis. Front Cell Infect Microbiol 2017;7:138. [PMID: 28487846 DOI: 10.3389/fcimb.2017.00138] [Cited by in Crossref: 28] [Cited by in F6Publishing: 23] [Article Influence: 5.6] [Reference Citation Analysis]
39 Heib M, Rose-John S, Adam D. Necroptosis, ADAM proteases and intestinal (dys)function. Int Rev Cell Mol Biol 2020;353:83-152. [PMID: 32381179 DOI: 10.1016/bs.ircmb.2020.02.001] [Cited by in Crossref: 2] [Cited by in F6Publishing: 2] [Article Influence: 1.0] [Reference Citation Analysis]