The DOI matches its Crossref record.
COLLAGENS: Molecular Biology, Diseases, and Potentials for Therapy
Abstract
The collagen superfamily of proteins now contains at least 19 proteins formally defined as collagens and an additional ten proteins that have collagen-like domains. The most abundant collagens form extracellular fibrils or network-like structures, but the others fulfill a variety of biological functions. Some of the eight highly specific post-translational enzymes involved in collagen biosynthesis have recently been cloned. Over 400 mutations in 6 different collagens cause a variety of human diseases that include osteogenesis imperfecta, chondrodysplasias, some forms of osteoporosis, some forms of osteoarthritis, and the renal disease known as the Alport syndrome. Many of the disease phenotypes have been produced in transgenic mice with mutated collagen genes. There has been increasing interest in the possibility that the unique post-translational enzymes involved in collagen biosynthesis offer attractive targets for specifically inhibiting excessive fibrotic reactions in a number of diseases. A number of experiments suggest it may be possible to inhibit collagen synthesis with oligo-nucleotides or antisense genes.
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
Cited by
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
Wound healing: an overview of acute, fibrotic and delayed healing
Diegelmann, R. (2004) · Frontiers in Bioscience · doi:10.2741/1184 · Cited by 2,147
Vitamin C as an Antioxidant: Evaluation of Its Role in Disease Prevention
Padayatty, S. J., Katz, A., Wang, Y., Eck, P., Kwon, O., Lee, J.-H., Chen, S., Corpe, C., Dutta, A., Dutta, S. K., et al. (2003) · Journal of the American College of Nutrition · doi:10.1080/07315724.2003.10719272 · Cited by 1,949
The Discoidin Domain Receptor Tyrosine Kinases Are Activated by Collagen
Vogel, W., Gish, G. D., Alves, F., & Pawson, T. (1997) · Molecular Cell · doi:10.1016/s1097-2765(00)80003-9 · Cited by 1,002
Vitamin C: The known and the unknown and Goldilocks
Padayatty, S., & Levine, M. (2016) · Oral Diseases · doi:10.1111/odi.12446 · Cited by 753
Khoshnoodi, J., Pedchenko, V., & Hudson, B. G. (2008) · Microscopy Research and Technique · doi:10.1002/jemt.20564 · Cited by 668
Processing of collagen based biomaterials and the resulting materials properties
Meyer, M. (2019) · BioMedical Engineering OnLine · doi:10.1186/s12938-019-0647-0 · Cited by 539
Hierarchical Structures of Bone and Bioinspired Bone Tissue Engineering
Liu, Y., Luo, D., & Wang, T. (2016) · Small · doi:10.1002/smll.201600626 · Cited by 482
Clinical and molecular genetics of Stickler syndrome
Snead, M. P., & Yates, J. R. W. (1999) · Journal of Medical Genetics · doi:10.1136/jmg.36.5.353 · Cited by 448
The application of recombinant human collagen in tissue engineering
Yang, C., Hillas, P. J., B??ez, J. A., Nokelainen, M., Balan, J., Tang, J., Spiro, R., & Polarek, J. W. (2004) · BioDrugs · doi:10.2165/00063030-200418020-00004 · Cited by 385
Nutritional Deficiencies in Morbidly Obese Patients: A New Form of Malnutrition?: Part A: Vitamins
Kaidar-Person, O., Person, B., Szomstein, S., & Rosenthal, R. J. (2008) · Obesity Surgery · doi:10.1007/s11695-007-9349-y · Cited by 325
Kuo, D. S., Labelle-Dumais, C., & Gould, D. B. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds346 · Cited by 320
Singh, B., Fleury, C., Jalalvand, F., & Riesbeck, K. (2012) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2012.00340.x · Cited by 302
Loenarz, C., & Schofield, C. J. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.07.002 · Cited by 274
Collagen synthesis in atherosclerosis: too much and not enough
Rekhter, M. (1999) · Cardiovascular Research · doi:10.1016/s0008-6363(98)00321-6 · Cited by 280
Disuse of the musculo-skeletal system in space and on earth
Narici, M. V., & de Boer, M. D. (2011) · European Journal of Applied Physiology · doi:10.1007/s00421-010-1556-x · Cited by 270
Medicinal plants and their components for wound healing applications
Sharma, A., Khanna, S., Kaur, G., & Singh, I. (2021) · Future Journal of Pharmaceutical Sciences · doi:10.1186/s43094-021-00202-w · Cited by 245
The impact of aging on cardiac extracellular matrix
Meschiari, C. A., Ero, O. K., Pan, H., Finkel, T., & Lindsey, M. L. (2017) · GeroScience · doi:10.1007/s11357-017-9959-9 · Cited by 237
Dietary vitamin C in human health
Granger, M., & Eck, P. (2018) · Advances in food and nutrition research · doi:10.1016/bs.afnr.2017.11.006 · Cited by 217
Stabilization of short collagen-like triple helices by protein engineering
Frank, S., Kammerer, R. A., Mechling, D., Schulthess, T., Landwehr, R., Bann, J., Guo, Y., Lustig, A., Bächinger, H. P., & Engel, J. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4644 · Cited by 213
Matrix metalloproteinase collagenolysis in health and disease
Amar, S., Smith, L., & Fields, G. B. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.04.015 · Cited by 194
Hypoxic Induction of Prolyl 4-Hydroxylase α(I) in Cultured Cells
Takahashi, Y., Takahashi, S., Shiga, Y., Yoshimi, T., & Miura, T. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.19.14139 · Cited by 174
Tendon properties in relation to muscular activity and physical training
Magnusson, S. P., Hansen, P., & Kjær, M. (2003) · Scandinavian Journal of Medicine & Science in Sports · doi:10.1034/j.1600-0838.2003.00308.x · Cited by 166
Emerging materials for hemostasis
Li, X.-F., Lu, P., Jia, H.-R., Li, G., Zhu, B., Wang, X., & Wu, F.-G. (2023) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2022.214823 · Cited by 164
Takamizawa, S., Maehata, Y., Imai, K., Senoo, H., Sato, S., & Hata, R. (2004) · Cell Biology International · doi:10.1016/j.cellbi.2004.01.010 · Cited by 155
Collagen–Alginate Composite Hydrogel: Application in Tissue Engineering and Biomedical Sciences
Hu, T., & Lo, A. C. Y. (2021) · Polymers · doi:10.3390/polym13111852 · Cited by 155
Clinical pharmacology and therapeutic use of antioxidant vitamins
Rodrigo, R., Guichard, C., & Charles, R. (2007) · Fundamental & Clinical Pharmacology · doi:10.1111/j.1472-8206.2006.00466.x · Cited by 124
Russek, L. N. (1999) · Physical Therapy · doi:10.1093/ptj/79.6.591 · Cited by 115
Zoppi, N., Gardella, R., De Paepe, A., Barlati, S., & Colombi, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312609200 · Cited by 107
Genetic Link Between Obesity and MMP14-Dependent Adipogenic Collagen Turnover
Chun, T.-H., Inoue, M., Morisaki, H., Yamanaka, I., Miyamoto, Y., Okamura, T., Sato-Kusubata, K., & Weiss, S. J. (2010) · Diabetes · doi:10.2337/db10-0073 · Cited by 97
The effect of mangiferin on skin: Penetration, permeation and inhibition of ECM enzymes
Ochocka, R., Hering, A., Stefanowicz–Hajduk, J., Cal, K., & Barańska, H. (2017) · PLOS ONE · doi:10.1371/journal.pone.0181542 · Cited by 56
Forlino, A., Tani, C., Rossi, A., Lupi, A., Campari, E., Gualeni, B., Bianchi, L., Armini, A., Cetta, G., Bini, L., et al. (2007) · PROTEOMICS · doi:10.1002/pmic.200600919 · Cited by 54
COL1A2 is a TBX3 target that mediates its impact on fibrosarcoma and chondrosarcoma cell migration
Omar, R., Cooper, A., Maranyane, H. M., Zerbini, L., & Prince, S. (2019) · Cancer Letters · doi:10.1016/j.canlet.2019.06.004 · Cited by 21
Metadata
- Authors
- Prockop, D. J., & Kivirikko, K. I.
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 1995-06
- Volume
- 64
- Issue
- 1
- Pages
- 403-434
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W2097707959
- Cited by
- 1,623
- References
- 0
- FWCI
- 40.97
- Type
- journal article
- Language
- en
- Open access
- closed
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
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.