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Crystal structures of VAP1 reveal ADAMs' MDC domain architecture and its unique C‐shaped scaffold
Open accessAbstract
ADAMs (a disintegrin and metalloproteinase) are sheddases possessing extracellular metalloproteinase/disintegrin/cysteine-rich (MDC) domains. ADAMs uniquely display both proteolytic and adhesive activities on the cell surface, however, most of their physiological targets and adhesion mechanisms remain unclear. Here for the first time, we reveal the ADAMs' MDC architecture and a potential target-binding site by solving crystal structures of VAP1, a snake venom homolog of mammalian ADAMs. The D-domain protrudes from the M-domain opposing the catalytic site and constituting a C-shaped arm with cores of Ca2+ ions. The disintegrin-loop, supposed to interact with integrins, is packed by the C-domain and inaccessible for protein binding. Instead, the hyper-variable region (HVR) in the C-domain, which has a novel fold stabilized by the strictly conserved disulfide bridges, constitutes a potential protein-protein adhesive interface. The HVR is located at the distal end of the arm and faces toward the catalytic site. The C-shaped structure implies interplay between the ADAMs' proteolytic and adhesive domains and suggests a molecular mechanism for ADAMs' target recognition for shedding.
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“Based on the model, known mutations that cause disease (magenta spheres in Fig. 3A) could act by hindering catalysis (R26K, R32Q, and L50P, near active site) or produce steric clashes (G154R) (19) in the hydrophobic core.”
From Accurate prediction of protein structures and interactions using a 3-track network (2021) · cites this paper as [19]
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Citations
Cites
The CCP4 suite: programs for protein crystallography
Number Collaborative Computational Project (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,317
Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse‐Kunstleve, R. W., Jiang, J., Kuszewski, J. J., Nilges, M., Pannu, N., et al. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998003254 · Cited by 15,723
A metalloproteinase disintegrin that releases tumour-necrosis factor-α from cells
Black, R. A., Rauch, C. T., Kozlosky, C. J., Peschon, J. J., Slack, J. L., Wolfson, M. F., Castner, B. J., Stocking, K. L., Reddy, P., Srinivasan, S., et al. (1997) · Nature · doi:10.1038/385729a0 · Cited by 3,149
Automated protein model building combined with iterative structure refinement.
Perrakis, A., Morris, R. J., & Lamzin, V. S. (1999) · Nature Structural Biology · doi:10.1038/8263 · Cited by 2,423
Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-α
Moss, M. L., Jin, S.-L. C., Milla, M. E., Burkhart, W., Carter, H. L., Chen, W.-J., Clay, W. C., Didsbury, J. R., Hassler, D., Hoffman, C. R., et al. (1997) · Nature · doi:10.1038/385733a0 · Cited by 1,378
ADAMs: key components in EGFR signalling and development
Blobel, C. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1548 · Cited by 1,112
The ADAMs family of metalloproteases: multidomain proteins with multiple functionsPreprint
Seals, D. F., & Courtneidge, S. A. (2003) · Genes & Development · doi:10.1101/gad.1039703 · Cited by 1,101
Association of the ADAM33 gene with asthma and bronchial hyperresponsiveness
Eerdewegh, P. V., Little, R. D., Dupuis, J., Mastro, R. G. D., Falls, K., Simon, J. S., Torrey, D., Pandit, S., McKenny, J., Braunschweiger, K. I., et al. (2002) · Nature · doi:10.1038/nature00878 · Cited by 1,082
Bode, W., Gomis‐Rüth, F. X., & Stöckler, W. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80312-i · Cited by 762
A potential fusion peptide and an integrin ligand domain in a protein active in sperm–egg fusion
Blobel, C., Wolfsberg, T. G., Turck, C. W., Myles, D. G., Primakoff, P., & White, J. M. (1992) · Nature · doi:10.1038/356248a0 · Cited by 672
Cited by
Sorted by citations
Items 101–200 of 201
Zhu, Z., Gao, Y., Zhu, Z., Yu, Y., Zhang, X., Zang, J., Teng, M., & Niu, L. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.06.004 · Cited by 24
“2); this is in the distal portion of the C-shape and has been designated as the hypervariable region (HVR) in the VAP1 and VAP2B structures [11,12].”
BackgroundRole of ADAM and ADAMTS disintegrin and metalloproteinases in normal pregnancy and preeclampsia
Qu, H., & Khalil, R. A. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.115266 · Cited by 24
Leonardi, A., Sajevic, T., Kovačič, L., Pungerčar, J., Balija, M. L., Halassy, B., Bakija, A. T., & Križaj, I. (2013) · Toxicon · doi:10.1016/j.toxicon.2013.11.009 · Cited by 23
ADAM-15 Disintegrin-Like Domain Structure and Function
Lu, D., Scully, M. F., Kakkar, V. V., & Lu, X. (2010) · Toxins · doi:10.3390/toxins2102411 · Cited by 25
“In the study of metalloproteinase domain-containing proteins including the active sequence in terms of structure and function, the crystal structure of the entire ectodomain of mature ADAM-22 [62] reported following the crystallographic studies of two PIII SVMP proteins, VAP1 (vascular apoptosisinducing protein-1) and…”
Seo, T., Sakon, T., Nakazawa, S., Nishioka, A., Watanabe, K., Matsumoto, K., Akasaka, M., Shioi, N., Sawada, H., & Araki, S. (2017) · FEBS Journal · doi:10.1111/febs.14066 · Cited by 25
Self-citationOyama, E., & Takahashi, H. (2017) · Molecules · doi:10.3390/molecules22081305 · Cited by 23
“It is suggested that the HVR segment might be an additional protein-binding site [3,27,28].”
BackgroundPinyachat, A., Rojnuckarin, P., Muanpasitporn, C., Singhamatr, P., & Nuchprayoon, S. (2011) · Toxicon · doi:10.1016/j.toxicon.2011.02.011 · Cited by 22
Imoto, I., Saitō, M., Suga, K., Kohmoto, T., Otsu, M., Horiuchi, K., Nakayama, H., Higashiyama, S., Sugimoto, M., Sasaki, A., et al. (2021) · Scientific Reports · doi:10.1038/s41598-021-89063-0 · Cited by 22
A model for COVID-19-induced dysregulation of ACE2 shedding by ADAM17
Healy, E. F., & Lilic, M. (2021) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2021.08.040 · Cited by 22
“While the MPD of ADAM10 has disulfide linkages (C594eC639 and C632eC645) aligned to those found in the inactive state of ADAM17, two of the disulfide linkages in the crystal structure of VAP1, C556eC598 and C592eC603 show no such alignment, suggesting a closed state in the former and an open, or active, conformation f…”
InfluentialInhibitory monoclonal antibody targeting ADAM17 expressed on cancer cells
Saha, N., Xu, K. Y., Zhu, Z., Tzvetkova‐Robev, D., Kalidindi, T. M., Xu, Y., Himanen, J. P., de Stanchina, E., Pillarsetty, N., Dimitrov, D. S., et al. (2021) · Translational Oncology · doi:10.1016/j.tranon.2021.101265 · Cited by 22
Hemorrhagic activity of the vascular apoptosis-inducing proteins VAP1 and VAP2 from Crotalus atrox
Kikushima, E., Nakamura, S., Oshima, Y., Shibuya, T., Miao, J. Y., Hayashi, H., Nikai, T., & Araki, S. (2008) · Toxicon · doi:10.1016/j.toxicon.2008.06.027 · Cited by 22
Self-citationCarbajo, R. J., Sanz, L., Pérez, A., & Calvete, J. J. (2014) · FEBS Journal · doi:10.1111/febs.13138 · Cited by 20
ADAM10 Is Involved in Cell Junction Assembly in Early Porcine Embryo Development
Kwon, J., Jeong, S.-M., Choi, I., & Kim, N. (2016) · PLoS ONE · doi:10.1371/journal.pone.0152921 · Cited by 20
Moiseeva, N., Bau, R., Swenson, S. D., Markland, F. S., Choe, J., Liu, Z., & Allaire, M. (2008) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444908002370 · Cited by 20
“…1996; Guo et al., 2001; Moreno-Murciano et al., 2003; Fujii et al., 2003; Shin et al., 2003; Bilgrami et al., 2004, 2005; Monleón et al., 2005; Janes et al., 2005; Takeda et al., 2006; Igarashi et al., 2007) revealed a remarkable similarity and a fold having an elongated overall shape.”
Morine, N., Matsuda, S., Terada, K., Eto, A., Ishida, I., & Oku, H. (2007) · Toxicon · doi:10.1016/j.toxicon.2007.10.009 · Cited by 19
Masuda, S., Maeda, H., Miao, J. Y., Hayashi, H., & Araki, S. (2007) · Endothelium · doi:10.1080/10623320701346882 · Cited by 19
Self-citationEngmark, M., Lomonte, B., Gutiérrez, J. M., Laustsen, A. H., Masi, F. D., Andersen, M. R., & Lund, O. (2017) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0005768 · Cited by 18
“adamanteus homology model based on RCSB entry 2ERQ [41].”
MethodYang, H., & Khalil, R. A. (2022) · Advances in pharmacology · doi:10.1016/bs.apha.2021.11.002 · Cited by 18
Bass, R., & Edwards, D. R. (2010) · Biochemical Journal · doi:10.1042/bj20100568 · Cited by 18
Kahveci-Türköz, S., Bläsius, K., Wozniak, J., Rinkens, C., Seifert, A., Kasparek, P., Ohm, H., Oltzen, S., Nieszporek, M., Schwarz, N., et al. (2023) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-023-04783-y · Cited by 17
Song, J., Xu, X., Zhang, Y., Guo, M., Yan, X., Wang, S., & Gao, S. (2012) · Biochimie · doi:10.1016/j.biochi.2012.10.013 · Cited by 17
“Partial sequence of the protein obtained by LC-MS/MS analysis reveals a sequence similarity with other members of PIIIc SVMPs, VAP1 from the Crotalus atrox venom [29] and TSV-DM from the Trimeresurus stejnegeri venom [30] (Fig.”
BackgroundSnake Venom Metalloproteinases
Escalante, T., Rucavado, A., Gutiérrez, M. D. C., & José (2009) · CRC Press eBooks · doi:10.1201/9781420008661.ch5 · Cited by 17
Martin, A. C. B. M., Cardoso, A. C. F., Selistre-de-Araújo, H. S., & Cominetti, M. R. (2015) · Cell Adhesion & Migration · doi:10.4161/19336918.2014.994917 · Cited by 16
“The disease incidence has increased in the past 2 decades, probably due the improvements in early detection and/or treatment, and also an increased public awareness.(11) Because of the high prostate cancer incidence, the development of new therapeutic tools should be created to combat this disease.”
BackgroundShioi, N., Ogawa, E., Mizukami, Y., Abe, S., Hayashi, R., & Terada, S. (2012) · The Journal of Biochemistry · doi:10.1093/jb/mvs127 · Cited by 16
“Each P-III SVMP has a distinct HVR sequence, which results in distinct surface features.”
BackgroundInfluentialSharma, D., & Singh, N. K. (2021) · Reviews of physiology, biochemistry and pharmacology · doi:10.1007/112_2021_67 · Cited by 16
Healy, E. F. (2022) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2022.01.038 · Cited by 14
“We have previously described the use of homology modeling, using vascular apoptosis-inducing protein-1 (VAP1) [34] as a template, to generate a structure of the ADAM17 ectodomain [11].”
Jangprasert, P., & Rojnuckarin, P. (2014) · Toxicon · doi:10.1016/j.toxicon.2013.12.005 · Cited by 14
Shioi, N., Nishijima, A., & Terada, S. (2015) · The Journal of Biochemistry · doi:10.1093/jb/mvv017 · Cited by 14
Structural, Functional and Therapeutic Aspects of Snake Venom Metalloproteinases
Chellapandi, P. (2014) · Mini-Reviews in Organic Chemistry · doi:10.2174/1570193x1101140402100707 · Cited by 14
Urra, F. A., Pulgar, R., Gutiérrez, R., Christian Hodar, Q., Cambiazo, V., & Labra, A. (2015) · Toxicon · doi:10.1016/j.toxicon.2015.09.032 · Cited by 14
Liu, L., Tian, E., Quan, S., Su, C., Zhou, J., Hu, S., Bian, N., Du, S., & Li, J. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1640090 · Cited by 13
“…DD is thought to be a scaffold for the extracellular structural domain of ADAM17, maintaining the rigidity of the C-type structure of the extracellular structural domain by connecting the catalytic structure to the near-membrane protein structural domains (Janes et al., 2005; Takeda et al., 2006).”
Mackessy, S. P., & Mackessy, S. P. (2016) · CRC Press eBooks · doi:10.1201/9781420008661-24 · Cited by 12
Jeong, Y., Ock, S., Yoo, J. G., Yu, D., & Choi, I. (2019) · Molecular Reproduction and Development · doi:10.1002/mrd.23250 · Cited by 12
The role of ADAM17 during liver damage
Al-Salihi, M. A., Bornikoel, A., Zhuang, Y., Stachura, P., Scheller, J., Lang, K. S., & Lang, P. A. (2021) · Biological Chemistry · doi:10.1515/hsz-2021-0149 · Cited by 11
Igarashi, T., Oishi, Y., Araki, S., Mori, H., & Takeda, S. (2006) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309106022548 · Cited by 11
“…asymmetric unit for each crystal form was obtained by a preliminary molecular-replacement method using MOLREP from the CCP4 suite (Collaborative Computational Project, Number 4, 1994) and the metalloproteinase (M) and cysteine-rich (C) domains of VAP1 (Takeda et al., 2006) as the starting models.”
BackgroundMethodInfluentialSelf-citationADAMs family in kidney physiology and pathology
Zhu, H., Wang, J., Nie, W., Armando, I., & Han, F. (2021) · EBioMedicine · doi:10.1016/j.ebiom.2021.103628 · Cited by 10
“This region may be involved in modulating subcellular localization and protein-protein interactions [5].”
Tavares, N. A. C., Correia, J. M., Guarnieri, M. C., Lima‐Filho, J. L., Prieto-da-Silva, A. R. B., & Rádis‐Baptista, G. (2008) · Toxicon · doi:10.1016/j.toxicon.2008.08.022 · Cited by 10
Sánchez, E. F., de Alvarenga, V. G., de Oliveira, L. S., Oliveira, D. L., Estevão-Costa, M. I., Flores-Ortiz, R., & Eble, J. A. (2021) · Biochimie · doi:10.1016/j.biochi.2021.01.016 · Cited by 10
Structural Aspects of the Factor X Activator RVV-X from Russell’s Viper Venom
Takeda, S. (2010) · Springer eBooks · doi:10.1007/978-90-481-9295-3_27 · Cited by 10
Self-citationAkiyama, M. (2010) · Japanese Journal of Thrombosis and Hemostasis · doi:10.2491/jjsth.21.319 · Cited by 10
Dagda, R. K., Gasanov, S. E., Zhang, B., Welch, W., & Rael, E. D. (2014) · Journal of Biological Physics · doi:10.1007/s10867-014-9347-y · Cited by 10
Natural Inhibitors of Snake Venom Metalloproteinases
Shioi, N., Koh, C. Y., & Kini, R. M. (2020) · Australian Journal of Chemistry · doi:10.1071/ch19414 · Cited by 9
Bastos, V. A., Gomes‐Neto, F., da Rocha, S. B., Teixeira‐Ferreira, A., Perales, J., Neves‐Ferreira, A. G. C., & Valente, R. H. (2020) · Journal of Proteomics · doi:10.1016/j.jprot.2020.103761 · Cited by 9
Natural Inhibitors of Snake Venom Metallopeptidases
Neves‐Ferreira, A. G. C., Valente, R. H., Domont, G. B., & Perales, J. (2017) · Toxinology · doi:10.1007/978-94-007-6452-1_19 · Cited by 9
Dagda, R. K., Gasanov, S. E., Zhang, B., Welch, W., & Rael, E. D. (2014) · Journal of Biological Physics · doi:10.1007/s10867-013-9339-3 · Cited by 9
Mori, E., Fukuda, H., Imajoh‐Ohmi, S., Mori, T., & Takasaki, S. (2011) · Journal of Reproduction and Development · doi:10.1262/jrd.11-108n · Cited by 9
“On the other hand, crystal structural studies suggested that the hypervariable region in the cysteine-rich domain would serve as an adhesive site [40, 41].”
BackgroundNeila‐Montero, M., Alvarez, M., Riesco, M. F., Montes‐Garrido, R., Palacin-Martinez, C., Silva‐Rodríguez, A., Martín‐Cano, F. E., Peña, F. J., de Paz, P., Anel, L., et al. (2023) · Theriogenology · doi:10.1016/j.theriogenology.2023.05.030 · Cited by 7
Ameh, I., Chia, M. A., Cataldi, T. R., Labate, C. A., Ebiloma, G. U., Yusuf, P. O., Shuaibu, M. N., & Balogun, E. O. (2023) · Toxicon · doi:10.1016/j.toxicon.2023.107138 · Cited by 7
Schluga, P. H. D. C., Larangote, D., de Melo, A. M., Lobermayer, G. K., Torrejón, D., de Oliveira, L. S., de Alvarenga, V. G., Vivas-Ruiz, D. E., Veiga, S. S., Sánchez, E. F., et al. (2024) · Toxins · doi:10.3390/toxins16110486 · Cited by 6
A Novel Class of Human ADAM8 Inhibitory Antibodies for Treatment of Triple-Negative Breast Cancer
Mineva, N. D., Pianetti, S., Das, S. G., Srinivasan, S. S., Billiald, N. M., & Sonenshein, G. E. (2024) · Pharmaceutics · doi:10.3390/pharmaceutics16040536 · Cited by 6
“The positions of the ADP2 and ADP13 critical and secondary binding residues, within the C-shaped structure of the ADAM8 ectodomain, are indicated in an ADAM8 crystal structure model based on the structure of vascular apoptosis-inducing protein-1 (PDB: 2ERP, [21]) (Figure 5B,C).”
BackgroundInfluentialThe distinct N-terminomes of Bothrops jararaca newborn and adult venoms
Andrade-Silva, D., Nishiyama, M. Y., Stuginski, D. R., Zelanis, A., & Serrano, S. M. T. (2021) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2021.140643 · Cited by 6
ADAM10: Function insights, disease implications, and promise of therapeutic targeting
Zhang, W., Xu, Y., & Fu, J. (2025) · Drug Discovery Today · doi:10.1016/j.drudis.2025.104414 · Cited by 6
VAP 1—Snake Venom Homolog of Mammalian ADAMs
Takeda, S. (2011) · Encyclopedia of Inorganic and Bioinorganic Chemistry · doi:10.1002/9781119951438.eibc0660 · Cited by 5
Self-citationExpression, purification and insights into structure and folding of the ADAM22 pro domain
Sørensen, H. P., Jacobsen, J., Nielbo, S., Poulsen, F. M., & Wewer, U. M. (2008) · Protein Expression and Purification · doi:10.1016/j.pep.2008.05.020 · Cited by 4
Snake Venomics and Disintegrins
Calvete, J. J., Sanz, L., & Juárez, P. (2009) · CRC Press eBooks · doi:10.1201/9781420008661.ch17 · Cited by 4
Snake Venom and Haemostasis – An Overview
Rojnuckarin, P. (2008) · European Oncology & Haematology · doi:10.17925/eoh.2008.02.1.7 · Cited by 4
de Alvarenga, V. G., de Oliveira, L. S., dos Santos, G. O., Vivas-Ruiz, D. E., Borges, M. H., de Souza, R. C. G., Eble, J. A., Moura-da-Silva, A. M., & Sánchez, E. F. (2023) · Toxicon · doi:10.1016/j.toxicon.2023.107097 · Cited by 3
Structure-Function Relationship of Modular Domains of P-III Class Snake Venom Metalloproteinases
Takeda, S. (2014) · Springer eBooks · doi:10.1007/978-94-007-6649-5_45-2 · Cited by 3
“3d) (Takeda et al. 2006).”
BackgroundInfluentialSelf-citationGarcía‐Robles, I., Ochoa‐Campuzano, C., Sanchez, J. J., Contreras, E., Real, M. D., & Rausell, C. (2012) · Toxicon · doi:10.1016/j.toxicon.2012.07.012 · Cited by 3
Nagase, H., & Murphy, G. (2013) · Springer eBooks · doi:10.1007/978-3-7091-0885-7_13 · Cited by 4
“The Ch subdomain has a core of α/β-fold structure consisting of two antiparallel β strands packed against two of the three α helices and five disulfide bonds (Takeda et al. 2006).”
BackgroundInfluentialSnake Venom Metalloproteinases
Serrano, S. M. T., & Fox, J. W. (2009) · CRC Press eBooks · doi:10.1201/9781420008661.sec2 · Cited by 3
ADAM Proteases in Physiology and Pathophysiology: Cleave to Function in Health or to Cause Disease
Grötzinger, J., & Rose‐John, S. (2013) · Springer eBooks · doi:10.1007/978-3-7091-0885-7_9 · Cited by 3
ADAMs and ADAMTs Selective Synthetic Inhibitors
Rossello, A., Nuti, E., & Maresca, A. (2009) · Wiley eBooks · doi:10.1002/9780470508169.ch26 · Cited by 3
VAP 1—Snake Venom Homolog of Mammalian ADAMs
Takeda, S. (2004) · Handbook of Metalloproteins · doi:10.1002/0470028637.met234 · Cited by 3
Self-citationNatural Inhibitors of Snake Venom Metallopeptidases
Neves‐Ferreira, A. G. C., Valente, R. H., Domont, G. B., & Perales, J. (2015) · Springer eBooks · doi:10.1007/978-94-007-6726-3_19-1 · Cited by 2
Rami, A., Damizadeh, B., Behdani, M., & Kazemi‐Lomedasht, F. (2024) · Protein and Peptide Letters · doi:10.2174/0109298665321842240819073453 · Cited by 2
Espín-Angulo, J., & Vela, D. (2025) · Toxins · doi:10.3390/toxins17060262 · Cited by 2
“Several SVMP-III proteins described in the literature, such as AaHIV from Agkistrodon acutus [109], bothropasin from Bothrops jararaca [118], VAP1 from Crotalus atrox [113], and VaH3 from Vipera ammodytes ammodytes [114], exhibit a conserved motif similar to those found in our models.”
Endothelial Cell Toxicity of Vascular Apoptosis-Inducing Proteins from Hemorrhagic Snake Venom
Araki, S. (2017) · Springer eBooks · doi:10.1007/978-94-007-6410-1_5 · Cited by 2
“There are also many monomer-type VAPs such as VAP2, agkistin, jararhagin, and VLH2, although some VAPs like VAP2 are observed as a dimer without a sulfhydryl connection in crystal (Masuda et al. 1998; Igarashi et al. 2007) (Fig.”
BackgroundInfluentialSelf-citationSnake Venom Proteinases as Toxins and Tools
Suvilesh, K. N., Urs, A. N. N., Savitha, M. N., Gowda, M. D. M., & Vishwanath, B. S. (2017) · Springer eBooks · doi:10.1007/978-981-10-2513-6_23 · Cited by 2
Structure-Function Relationship of Modular Domains of P-III Class Snake Venom Metalloproteinases
Takeda, S. (2016) · Springer eBooks · doi:10.1007/978-94-007-6416-3_45 · Cited by 2
Self-citationSnake Venoms and Other Toxic Components Affecting Thrombosis and Hemostasis
Yamazaki, Y., & Morita, T. (2009) · Springer eBooks · doi:10.1007/978-4-431-78847-8_32 · Cited by 2
Sehara‐Fujisawa, A. (2025) · Handbook of Proteolytic Enzymes · doi:10.1016/b978-0-443-28849-4.00190-9 · Cited by 1
Moura-da-Silva, A. M., & Paine, M. J. I. (2012) · Handbook of Proteolytic Enzymes · doi:10.1016/b978-0-12-382219-2.00210-6 · Cited by 1
Contribution of ADAMs and ADAMTSs to Tumor Expansion and Metastasis
Torres‐Collado, A. X., & Iruela‐Arispe, M. L. (2009) · Springer eBooks · doi:10.1007/978-1-4419-0711-0_13 · Cited by 1
“While in snake venom proteases this domain binds to integrins through an RGD motif (Perutelli 1995), in adamalysins the disintegrin domain is frequently folded and not available for binding to cells (Takeda et al. 2006), but in some cases, other regions of the molecule might contain RGD repeats and interact with integ…”
BackgroundKveiborg, M., Fröhlich, C., Albrechtsen, R., & Wewer, U. M. (2012) · Handbook of Proteolytic Enzymes · doi:10.1016/b978-0-12-382219-2.00252-0 · Cited by 1
Microsporidia Spore Adherence and Host Cell Infection In Vitro
Leonard, C. A. (2013) · Digital Commons - East Tennessee State University (East Tennessee State University) · doi:10.13140/rg.2.1.2879.4647 · Cited by 1
Variable expressions of ADAM family genes in tissues and cancer cells
Kleino, I. (2007) · Tampere University Institutional Repository (Tampere University)
Gómez, P. J. (2007) · Repository of Digital Objects for Teaching Research and Culture (University of Valencia)
Takeda, S. (2009) · Japanese Journal of Thrombosis and Hemostasis · doi:10.2491/jjsth.20.307
Self-citationSehara‐Fujisawa, A. (2012) · Handbook of Proteolytic Enzymes · doi:10.1016/b978-0-12-382219-2.00255-6
Menezes, M. C., Oliveira, A. K., & Serrano, S. M. T. (2012) · Handbook of Proteolytic Enzymes · doi:10.1016/b978-0-12-382219-2.00214-3
Vascular Apoptosis-Inducing Protein 1
Araki, S. (2012) · Handbook of Proteolytic Enzymes · doi:10.1016/b978-0-12-382219-2.00228-3
Self-citationADAM8 as a drug target in pancreatic cancer
Schlomann, U., Koller, G., Conrad, C., Ferdous, T., Golfi, P., Garcia, A. M., Höfling, S., Parsons, M., Costa, P., Soper, R., et al. (2014) · RePEc: Research Papers in Economics
Investigation of ADAM17 and ADAMTS-1, -4 and -5 in liver carcinoma.
Turner, S. (2009) · SHURA (Sheffield Hallam University Research Archive) (Sheffield Hallam University)
Zigrino, P., & Mauch, C. (2012) · Handbook of Proteolytic Enzymes · doi:10.1016/b978-0-12-382219-2.00250-7
Mochizuki, S., & Okada, Y. (2012) · Handbook of Proteolytic Enzymes · doi:10.1016/b978-0-12-382219-2.00256-8
Endothelial Cell Toxicity of Vascular Apoptosis-Inducing Proteins from Hemorrhagic Snake Venom
Araki, S. (2016) · Springer eBooks · doi:10.1007/978-94-007-6648-8_5-1
Self-citationKveiborg, M., & Albrechtsen, R. (2025) · Handbook of Proteolytic Enzymes · doi:10.1016/b978-0-443-28849-4.00186-7
Mochizuki, S., & Okada, Y. (2025) · Handbook of Proteolytic Enzymes · doi:10.1016/b978-0-443-28849-4.00191-0
Moura-da-Silva, A. M. (2025) · Handbook of Proteolytic Enzymes · doi:10.1016/b978-0-443-28849-4.00162-4
Menezes, M. C., Oliveira, A. K., & Serrano, S. M. T. (2025) · Handbook of Proteolytic Enzymes · doi:10.1016/b978-0-443-28849-4.00166-1
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Self-citationSam, R., Lopes, C., Marques, O., Carvalho, C., & Nuvor, S. V. (2017) · Journal of Cancer and Tumor International · doi:10.9734/jcti/2017/35955
Micro-environnement et cancer : rôle des adamalysines dans la progression tumorale
Dekky, B. (2018) · theses.fr (ABES) · doi:10.70675/30190222z7377z44fdzbbc4zd0a03a82efd6
Metadata
- Authors
- Takeda, S., Igarashi, T., Mori, H., & Araki, S.
- Affiliations
- SPring-8 (JP)
- National Cerebral and Cardiovascular Center (JP)
- Nagoya University (JP)
- Corresponding author
- Takeda, Soichi
- ORCID
- Takeda, Soichi
- Venue
- The EMBO Journal
- Published
- 2006-05-11
- Volume
- 25
- Issue
- 11
- Pages
- 2388-2396
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC1478178
- OpenAlex
- W2000001290
- Cited by
- 202
- References
- 45
- Citations by year
- 2025: 10 · 2024: 4 · 2023: 4 · 2022: 4 · 2021: 9 · 2020: 4 · 2019: 5 · 2018: 2 · 2017: 11 · 2016: 12 · 2015: 7 · 2014: 14 · 2013: 9 · 2012: 17
- FWCI
- 8.36
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Takeda Science Foundation
- Senri Life Science Foundation
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Health Sciences › Medicine › Hematology › Blood Coagulation and Thrombosis Mechanisms
- Keywords
- ADAMS, snake venom proteins, disintegrins, metalloproteinases, hypervariable region, disulfide bonds, calcium ions, extracellular matrix, crystal structure
- MeSH terms
- Amino Acid Sequence, Animals, Crotalid Venoms, Humans, Metalloendopeptidases, Models, Molecular, Molecular Sequence Data, Sequence Alignment, Protein Structure, Tertiary, Crystallography, X-Ray, Apoptosis Regulatory Proteins, ADAM Proteins
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