The DOI matches its Crossref record; 86 of the 87 references it cites were found in a registry or an index.
Roles of PLODs in Collagen Synthesis and Cancer Progression
Open accessAbstract
genes. Expression of PLODs is regulated by multiple cytokines, transcription factors and microRNAs. Dysregulation of PLODs promotes cancer progression and metastasis, suggesting that targeting PLODs is potential strategy for cancer treatment. Here, we summarize the recent progress in the investigation of function and regulation of PLODs in normal tissue development and disease progression, especially in cancer.
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.
Integrity signals
Registry
Cites
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.
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
2 retracted
Gilkes, D. M., Bajpai, S. K., Chaturvedi, P., Wirtz, D., & Semenza, G. L. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.442939 · Cited by 473
RetractedProcollagen lysyl hydroxylase 2 is essential for hypoxia-induced breast cancer metastasis
Gilkes, D. M., Bajpai, S., Wong, C. C., Chaturvedi, P., Hubbi, M. E., Wirtz, D., & Semenza, G. L. (2013) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-12-0629 · Cited by 252
RetractedMolecular Mechanisms of Stress-Responsive Changes in Collagen and Elastin Networks in Skin
Aziz, J., Shezali, H., Radzi, Z., Yahya, N. A., Abu Kassim, N. H., Czernuszka, J., & Rahman, M. T. (2016) · Skin Pharmacology and Physiology · doi:10.1159/000447017 · Cited by 7,323
Matrix Crosslinking Forces Tumor Progression by Enhancing Integrin Signaling
Levental, K. R., Yu, H., Kass, L., Lakins, J. N., Egeblad, M., Erler, J. T., Fong, S. F. T., Csiszar, K., Giaccia, A., Weninger, W., et al. (2009) · Cell · doi:10.1016/j.cell.2009.10.027 · Cited by 4,101
Tumour-educated macrophages promote tumour progression and metastasis
Pollard, J. W. (2004) · Nature reviews. Cancer · doi:10.1038/nrc1256 · Cited by 3,414
Collagen reorganization at the tumor-stromal interface facilitates local invasion
Provenzano, P. P., Eliceiri, K. W., Campbell, J. M., Inman, D. R., White, J. G., & Keely, P. J. (2006) · BMC Medicine · doi:10.1186/1741-7015-4-38 · Cited by 1,804
Collagen density promotes mammary tumor initiation and progression
Provenzano, P. P., Inman, D. R., Eliceiri, K. W., Knittel, J. G., Yan, L., Rueden, C., White, J. G., & Keely, P. J. (2008) · BMC Medicine · doi:10.1186/1741-7015-6-11 · Cited by 1,394
Aligned Collagen Is a Prognostic Signature for Survival in Human Breast Carcinoma
Conklin, M. W., Eickhoff, J. C., Riching, K. M., Pehlke, C. A., Eliceiri, K. W., Provenzano, P. P., Friedl, A., & Keely, P. J. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2010.11.076 · Cited by 1,321
Dynamic interplay between the collagen scaffold and tumor evolution
Egeblad, M., Rasch, M. G., & Weaver, V. M. (2010) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2010.08.015 · Cited by 931
Saito, M., & Marumo, K. (2009) · Osteoporosis International · doi:10.1007/s00198-009-1066-z · Cited by 914
Xiong, G., Deng, L., Zhu, J., Rychahou, P. G., & Xu, R. (2014) · BMC Cancer · doi:10.1186/1471-2407-14-1 · Cited by 759
Self-citationLysine post-translational modifications of collagen
Yamauchi, M., & Sricholpech, M. (2012) · Essays in Biochemistry · doi:10.1042/bse0520113 · Cited by 628
Basement Membrane Proteins: Structure, Assembly, and Cellular Interactions
Mats Paulsson, M. (1992) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409239209082560 · Cited by 621
The collagen family members as cell adhesion proteins
Heino, J. (2007) · BioEssays · doi:10.1002/bies.20636 · Cited by 439
Cheon, D., Tong, Y., Sim, M., Dering, J., Berel, D., Cui, X., Lester, J., Beach, J. A., Tighiouart, M., Walts, A. E., et al. (2013) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-13-1256 · Cited by 374
Transmembrane collagen receptors
Leitinger, B. (2011) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-092910-154013 · Cited by 354
Collagen Hydroxylases and the Protein Disulfide Isomerase Subunit of Prolyl 4‐Hydroxylases
Kivirikko, K. I., & Pihlajaniemi, T. A. (1998) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470123188.ch9 · Cited by 318
Hypoxia-Dependent Modification of Collagen Networks Promotes Sarcoma Metastasis
Eisinger‐Mathason, T. S. K., Zhang, M., Qiu, Q., Skuli, N., Nakazawa, M. S., Karakasheva, T. A., Mucaj, V., Shay, J. E. S., Stangenberg, L., Sadri, N., et al. (2013) · Cancer Discovery · doi:10.1158/2159-8290.cd-13-0118 · Cited by 279
Albaugh, V. L., Mukherjee, K., & Barbul, A. (2017) · Journal of Nutrition · doi:10.3945/jn.117.256404 · Cited by 269
Collagen: structure, function, and metabolism in normal and fibrotic tissues.
Nimni, M. (1983) · Seminars in Arthritis & Rheumatism · doi:10.1016/0049-0172(83)90024-0 · Cited by 262
Selective Binding of Collagen Subtypes by Integrin α1I, α2I, and α10I Domains
Tulla, M., Pentikäinen, O. T., Viitasalo, T., Käpylä, J., Impola, U., Nykvist, P., Nissinen, L. M., Johnson, M. S., & Heino, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104058200 · Cited by 257
Tiger, C., Fougerousse, F., Grundström, G., Velling, T., & Gullberg, D. (2001) · Developmental Biology · doi:10.1006/dbio.2001.0363 · Cited by 235
Cancer-Associated Fibroblasts Induce a Collagen Cross-link Switch in Tumor Stroma
Paňková, D., Chen, Y., Terajima, M., Schliekelman, M. J., Baird, B. N., Fahrenholtz, M. M., Sun, L., Gill, B. J., Vadakkan, T. J., Kim, M. P., et al. (2015) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-15-0307 · Cited by 233
Camper, L., Hellman, U., & Lundgren-Åkerlund, E. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.32.20383 · Cited by 228
Molecular Analysis of Collagen Binding by the Human Discoidin Domain Receptors, DDR1 and DDR2
Leitinger, B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301370200 · Cited by 219
Tumor Cell–Driven Extracellular Matrix Remodeling Drives Haptotaxis during Metastatic Progression
Oudin, M. J., Jonas, O. H., Kosciuk, T., Broye, L. C., Guido, B. C., Wyckoff, J., Riquelme, D. N., Lamar, J. M., Asokan, S. B., Whittaker, C. A., et al. (2016) · Cancer Discovery · doi:10.1158/2159-8290.cd-15-1183 · Cited by 207
Lysyl hydroxylase 2 induces a collagen cross-link switch in tumor stroma
Chen, Y., Terajima, M., Yang, Y., Sun, L., Ahn, Y., Paňková, D., Puperi, D. S., Watanabe, T., Kim, M. P., Blackmon, S. H., et al. (2015) · Journal of Clinical Investigation · doi:10.1172/jci74725 · Cited by 186
Identification and validation of genes involved in cervical tumourigenesis
Rajkumar, T., Sabitha, K., Vijayalakshmi, N., Shirley, S., Bose, M. V., Gopisetty, G., & Selvaluxmy, G. (2011) · BMC Cancer · doi:10.1186/1471-2407-11-80 · Cited by 183
Miyamoto, K., Seki, N., Matsushita, R., Yonemori, M., Yoshino, H., Nakagawa, M., & Enokida, H. (2016) · British Journal of Cancer · doi:10.1038/bjc.2016.179 · Cited by 167
Hautala, T., Byers, M. G., Eddy, R. L., Shows, T. B., Kivirikko, K. I., & Myllylä, R. (1992) · Genomics · doi:10.1016/0888-7543(92)90202-4 · Cited by 139
Lysyl Hydroxylase 3 Is a Multifunctional Protein Possessing Collagen Glucosyltransferase Activity
Heikkinen, J., Risteli, M., Wang, C., Latvala, J., Rossi, M., Valtavaara, M., & Myllylä, R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m006203200 · Cited by 139
Chaperone Hsp47 Drives Malignant Growth and Invasion by Modulating an ECM Gene Network
Zhu, J., Xiong, G., Fu, H., Evers, B. M., Zhou, B. P., & Xu, R. (2015) · Cancer Research · doi:10.1158/0008-5472.can-14-1027 · Cited by 137
Self-citationA Connective Tissue Disorder Caused by Mutations of the Lysyl Hydroxylase 3 Gene
Salo, A. M., Cox, H., Farndon, P. A., Moss, C., Grindulis, H., Risteli, M., Robins, S. P., & Myllylä, R. (2008) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2008.09.004 · Cited by 135
Valtavaara, M., Szpirer, C., Szpirer, J., & Myllylä, R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.21.12881 · Cited by 130
Function of cancer cell-derived extracellular matrix in tumor progression
Xiong, G., & Xu, R. (2016) · Journal of Cancer Metastasis and Treatment · doi:10.20517/2394-4722.2016.08 · Cited by 129
Self-citationDecarboxylation of alpha-ketoglutarate coupled to collagen proline hydroxylase.
Rhoads, R. E., & Udenfriend, S. (1968) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.60.4.1473 · Cited by 128
Hollern, D. P., Honeysett, J., Cardiff, R. D., & Andrechek, E. R. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.00737-14 · Cited by 124
Patino, M. G., Neiders, M. E., Andreana, S., Noble, B. K., & Cohen, R. E. (2002) · Implant Dentistry · doi:10.1097/00008505-200207000-00014 · Cited by 123
Shen, Q., Eun, J. W., Lee, K., Kim, H. S., Yang, H. D., Kim, S. Y., Lee, E. K., Kim, T., Kang, K., Kim, S., et al. (2017) · Hepatology · doi:10.1002/hep.29606 · Cited by 120
Premature aggregation of type IV collagen and early lethality in lysyl hydroxylase 3 null mice
Rautavuoma, K., Takaluoma, K., Sormunen, R. T., Myllyharju, J., Kivirikko, K. I., & Soininen, R. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404966101 · Cited by 116
Song, Y., Zheng, S., Wang, J., Long, H., Fang, L., Wang, G., Li, Z., Que, T., Liu, Y., Li, Y., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.16710 · Cited by 110
Rohrbach, M., Vandersteen, A., Yiş, U., Serdaroglu, G., Ataman, E., Chopra, M., Garcia, S., Jones, K., Kariminejad, A., Kraenzlin, M., et al. (2011) · Orphanet Journal of Rare Diseases · doi:10.1186/1750-1172-6-46 · Cited by 106
Rygiel, T. P., Stolte, E. H., Ruiter, T. E.-D., van de Weijer, M. L., & Meyaard, L. (2011) · Molecular Immunology · doi:10.1016/j.molimm.2011.09.006 · Cited by 104
Xu, F., Zhang, J., Hu, G., Liu, L., & Liang, W. (2017) · Cancer Cell International · doi:10.1186/s12935-017-0420-z · Cited by 102
Kurozumi, A., Kato, M., Goto, Y., Matsushita, R., Nishikawa, R., Okato, A., FUKUMOTO, I., Ichikawa, T., & Seki, N. (2016) · International Journal of Oncology · doi:10.3892/ijo.2016.3440 · Cited by 100
Age-related variations in hydroxylation of lysine and proline in collagen
Barnes, M. J., Constable, B. J., Morton, L. F., & Royce, P. M. (1974) · Biochemical Journal · doi:10.1042/bj1390461 · Cited by 97
PLOD2 regulated by transcription factor FOXA1 promotes metastasis in NSCLC
Du, H., Chen, Y., Hou, X., Huang, Y., Wei, X., Yu, X., Feng, S. L., Wu, Y., Zhan, M., Shi, X., et al. (2017) · Cell Death and Disease · doi:10.1038/cddis.2017.553 · Cited by 97
Hausmann, E. (1967) · Biochimica et Biophysica Acta (BBA) - Protein Structure · doi:10.1016/0005-2795(67)90566-1 · Cited by 95
Sada, M., Ohuchida, K., Horioka, K., Okumura, T., Moriyama, T., Miyasaka, Y., Ohtsuka, T., Mizumoto, K., Oda, Y., & Nakamura, M. (2016) · Cancer Letters · doi:10.1016/j.canlet.2016.01.016 · Cited by 94
Yamada, Y., Ando, F., & Shimokata, H. (2007) · International Journal of Molecular Medicine · doi:10.3892/ijmm.19.5.791 · Cited by 89
Noda, T., Yamamoto, H., Takemasa, I., Yamada, D., Uemura, M., Wada, H., Kobayashi, S., Marubashi, S., Eguchi, H., Tanemura, M., et al. (2011) · Liver International · doi:10.1111/j.1478-3231.2011.02619.x · Cited by 89
Pitx2 Regulates Procollagen Lysyl Hydroxylase (Plod) Gene Expression
Hjalt, T. Å. H., Amendt, B. A., & Murray, J. C. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.152.3.545 · Cited by 88
Secretion and Assembly of Type IV and VI Collagens Depend on Glycosylation of Hydroxylysines
Sipilä, L., Ruotsalainen, H. J., Sormunen, R. T., Baker, N. L., Lamandé, S. R., Vapola, M. H., Wang, C., Sado, Y., Aszódi, A., & Myllylä, R. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704198200 · Cited by 86
Gistelinck, C., Witten, P. E., Huysseune, A., Symoens, S., Malfait, F., Larionova, D., Simoens, P., Dierick, M., Hoorebeke, L. V., Paepe, A. D., et al. (2016) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.2977 · Cited by 83
Lysyl Hydroxylase 2 Is Secreted by Tumor Cells and Can Modify Collagen in the Extracellular Space
Chen, Y., Guo, H., Terajima, M., Banerjee, P., Liu, X., Jiang, Y. L., Momin, A. A., Katayama, H., Hanash, S., Burns, A. R., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.759803 · Cited by 79
Giunta, C., Randolph, A. E., & Steinmann, B. U. (2005) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2005.04.014 · Cited by 78
Hamaia, S. W., Pugh, N., Raynal, N., Némoz, B., Stone, R., Gullberg, D., Bihan, D. G., & Farndale, R. W. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.353144 · Cited by 74
Sricholpech, M., Perdivara, I., Nagaoka, H., Yokoyama, M., Tomer, K. B., & Yamauchi, M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.178509 · Cited by 72
Pousi, B., Hautala, T., Heikkinen, J., PAJUNEN, L., Kivirikko, K. I., & Myllylä, R. (1994) · PubMed Central · Cited by 71
Remst, D. F. G., Davidson, E. N. B., Vitters, E. L., Bank, R. A., van den Berg, W. B., & van der Kraan, P. M. (2013) · Cell and Tissue Research · doi:10.1007/s00441-013-1740-5 · Cited by 69
Gjaltema, R. A. F., de Rond, S., Rots, M. G., & Bank, R. A. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.634311 · Cited by 66
Hydroxylysine-linked glycosides of human complement subcomponent C1q and various collagens
Shinkai, H., & Yonemasu, K. (1979) · Biochemical Journal · doi:10.1042/bj1770847 · Cited by 59
Liefhebber, J. M. P., Punt, S., Spaan, W. J. M., & van Leeuwen, H. C. (2010) · BMC Cell Biology · doi:10.1186/1471-2121-11-33 · Cited by 47
Novel signatures of cancer‐associated fibroblasts
Bozóky, B., Savchenko, A., Csermely, P., Korcsmáros, T., Dúl, Z., Pontén, F., Székely, L., & Klein, G. (2013) · International Journal of Cancer · doi:10.1002/ijc.28035 · Cited by 46
N-Glycoprotein Analysis Discovers New Up-Regulated Glycoproteins in Colorectal Cancer Tissue
Nicastri, A., Gaspari, M., Sacco, R., Elia, L., Gabriele, C., Romano, R., Rizzuto, A., & Cuda, G. (2014) · Journal of Proteome Research · doi:10.1021/pr500647y · Cited by 45
Sun, L., Wang, D., Li, X., Zhang, L., Zhang, H., & Zhang, Y. (2016) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2016.03.053 · Cited by 40
Carafoli, F., Hamaia, S. W., Bihan, D. G., Hohenester, E., & Farndale, R. W. (2013) · PLoS ONE · doi:10.1371/journal.pone.0069833 · Cited by 37
Chong, M. S., Goh, L. K., Lim, W. S., Chan, M., Tay, L. B. G., Chen, G., Feng, L., Ng, T. P., Tan, C. H., & Lee, T.-S. W. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-121621 · Cited by 32
Amodio, G., Sasso, E., DˈAmbrosio, C., Scaloni, A., Moltedo, O., Franceschelli, S., Zambrano, N., & Remondelli, P. (2016) · Cell Biology and Toxicology · doi:10.1007/s10565-016-9335-z · Cited by 30
Association of ECRG4 with PLK1, CDK4, PLOD1 and PLOD2 in esophageal squamous cell carcinoma.
Li, L., Wang, W., Li, X., & Gao, T. (2017) · PubMed Central · Cited by 30
Mia, M. M., & Bank, R. A. (2015) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.12661 · Cited by 29
Localization of the gene encoding a novel isoform of lysyl hydroxylase
Szpirer, C., Szpirer, J., Rivière, M., Vanvooren, P., Valtavaara, M., & Myllylä, R. (1997) · Mammalian Genome · doi:10.1007/s003359900549 · Cited by 28
Knippenberg, M., Helder, M. N., Zandieh‐Doulabi, B., Bank, R. A., Wuisman, P. I. J. M., & Klein‐Nulend, J. (2009) · Tissue Engineering Part A · doi:10.1089/ten.tea.2007.0184 · Cited by 28
Elsemman, I. E., Mardinoğlu, A., Shoaie, S., Soliman, T. H. A., & Nielsen, J. (2016) · Molecular BioSystems · doi:10.1039/c5mb00827a · Cited by 26
Abdalla, E. M., Rohrbach, M., Bürer, C., KRAENZLIN, M. E., El-Tayeby, H. M., El-Belbesy, M., Nabil, A., & Giunta, C. (2014) · European Journal of Pediatrics · doi:10.1007/s00431-014-2429-9 · Cited by 25
Watt, S. A., Dayal, J. H. S., Wright, S. C., Riddle, M. J., Pourreyron, C., McMillan, J. R., Kimble, R. M., di Prisco, M., Gärtner, U., Warbrick, E., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0137639 · Cited by 25
The Role of Leukocyte-Associated Ig-like Receptor-1 in Suppressing Collagen-Induced Arthritis
Kim, S., Easterling, E. R., Price, L., Smith, S. L., Coligan, J. E., Park, J. J., Brand, D. D., Rosloniec, E. F., Stuart, J. M., Kang, A. H., et al. (2017) · The Journal of Immunology · doi:10.4049/jimmunol.1700271 · Cited by 24
Ah-Kim, H., Zhang, X., Islam, S., Sofi, J. I., Glickberg, Y., Malemud, C. J., Moskowitz, R. W., & Haqqi, T. M. (2000) · Cytokine · doi:10.1006/cyto.1999.0539 · Cited by 20
Pousi, B., Hautala, T., Heikkinen, J., PAJUNEN, L., Kivirikko, K. I., & Myllalä, R. (1994) · Matrix Biology · doi:10.1016/0945-053x(94)90130-9 · Cited by 17
Tasker, P. N., Macdonald, H., Fraser, W. D., Reid, D. M., Ralston, S. H., & Albagha, O. (2006) · Osteoporosis International · doi:10.1007/s00198-006-0129-7 · Cited by 17
Belangero, P. S., Leal, M. F., Cohen, C., de Figueiredo, E. A., Smith, M. D. A. C., Andreoli, C. V., Pochini, A. D. C., Ejnisman, B., & Cohen, M. (2015) · Journal of Orthopaedic Research® · doi:10.1002/jor.22984 · Cited by 16
Novel lysyl hydroxylase isoforms
Valtavaara, M. (1999) · Cited by 12
Neyazi, B., Tanrikulu, L., Wilkens, L., Hartmann, C. J., Stein, K. P., Dumitru, C. A., & Sandalcioglu, I. E. (2017) · World Neurosurgery · doi:10.1016/j.wneu.2017.02.116 · Cited by 12
The Extracellular Matrix Signature in Vein Graft Disease
Kahle, B. K., Schmidtke, C., Hunzelmann, N., Bartels, C., Sievers, H. H., Steenbock, H., Reinhardt, D. P., & Brinckmann, J. (2015) · Canadian Journal of Cardiology · doi:10.1016/j.cjca.2015.11.014 · Cited by 10
van Dijk, F. S., Mancini, G. M. S., Maugeri, A., & Cobben, J. M. (2017) · European Journal of Medical Genetics · doi:10.1016/j.ejmg.2017.07.011 · Cited by 10
Kyphoscolitic type of Ehlers-Danlos syndrome with prenatal stroke
Zahed, M., Tosello, B., Coze, S., & Gire, C. (2017) · Indian Pediatrics · doi:10.1007/s13312-017-1054-x · Cited by 9
Flagged first, then by citations
1 of the 87 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Concepts of extracellular matrix remodelling in tumour progression and metastasis
Winkler, J., Abisoye-Ogunniyan, A., Metcalf, K. J., & Werb, Z. (2020) · Nature Communications · doi:10.1038/s41467-020-18794-x · Cited by 2,296
Cox, T. R. (2021) · Nature reviews. Cancer · doi:10.1038/s41568-020-00329-7 · Cited by 1,015
Vitamin C-Sources, Physiological Role, Kinetics, Deficiency, Use, Toxicity, and Determination
Doseděl, M., Jirkovský, E., Macáková, K., Krčmová, L., Javorská, L., Pourová, J., Mercolini, L., Remião, F., Nováková, L., Mladěnka, P., et al. (2021) · Nutrients · doi:10.3390/nu13020615 · Cited by 553
The Extracellular Matrix: Its Composition, Function, Remodeling, and Role in Tumorigenesis
Dzobo, K., & Dandara, C. (2023) · Biomimetics · doi:10.3390/biomimetics8020146 · Cited by 228
He, J., Wei, X., Li, S., Liu, Y., Hu, H., Li, Z., Kuang, X.-H., Wang, L., Shi, X., Yuan, S., et al. (2018) · Cell Communication and Signaling · doi:10.1186/s12964-018-0309-z · Cited by 128
Metadata
- Authors
- Qi, Y., & Xu, R.
- Affiliations
- University of Kentucky (US)
- Corresponding author
- Xu, Ren
- ORCID
- Xu, Ren
- Venue
- Frontiers in Cell and Developmental Biology
- Publisher
- Frontiers Media SA
- Published
- 2018-06-28
- Volume
- 6
- Pages
- 66-66
- ISSN
- 2296-634X (ISSN-L)
- PMC
- PMC6031748
- OpenAlex
- W2808438085
- Cited by
- 248
- References
- 87
- Citations by year
- 2026: 20 · 2025: 31 · 2024: 28 · 2023: 26 · 2022: 42 · 2021: 38 · 2020: 48 · 2019: 13 · 2018: 1
- FWCI
- 2.67
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Frontiers in Cell and Developmental Biology (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- UKnowledge (University of Kentucky) (submittedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Institutes of Health (1R01CA207772, 1R01CA215095, 1R21CA209045)
- U.S. Department of Defense (W81XWH-15-1-0052)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › TGF-β signaling in diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Keywords
- collagen synthesis, tumor progression, metastasis, gene expression regulation, cytokines, transcription factors, microRNA, histogenesis, cancer therapy targets
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