Structure, Stability and Folding of the Collagen Triple Helix
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
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?
Collagen is non-labile relative to many other vertebrate proteins because of its decay resistance, partly due to its triple helical quaternary structure and high concentration of thermally stable amino acids.
“Collagen is also non-labile relative to many other vertebrate proteins because of its decay resistance, partly due to its triple helical quaternary structure and high concentration of thermally stable amino acids (Engel and Bächinger, 2005; Persikov et al., 2005; Sansom et al., 2010; Wang et al., 2012)”
From Cretaceous dinosaur bone contains recent organic material and provides an environment conducive to microbial communities (2019) · cites this paper as Engel and Bächinger, 2005
Cites
Principles of protein structure
Schulz, G., & Schirmer, R. H. (1980) · Journal of Steroid Biochemistry · doi:10.1016/0022-4731(80)90019-9 · Cited by 1,058 · see citing works
The structure and action of proteins
Dickerson, R. E., & Geis, I. (1969) · Andalas University Repository (Andalas University) · Cited by 733 · see citing works
Ricard‐Blum, S., Dublet, B., & REST, M. V. D. (2000) · doi:10.1093/oso/9780198505457.001.0001 · Cited by 56 · see citing works
Analysis of the helix–coil transition in (Pro‐Pro‐Gly)n by the All‐or‐none model
Gō, N., & Suezaki, Y. (1973) · Biopolymers · doi:10.1002/bip.1973.360120818 · Cited by 23 · see citing works
The stereoelectronic basis of collagen stability
Raines, R. T., Bretscher, L. E., Holmgren, S. K., & Taylor, K. M. (2006) · Kluwer Academic Publishers eBooks · doi:10.1007/0-306-46881-6_139 · Cited by 1 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
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 · see citing works
Amirrah, I. N., Lokanathan, Y., Zulkiflee, I., Wee, M. F. M. R., Motta, A., & Fauzi, M. B. (2022) · Biomedicines · doi:10.3390/biomedicines10092307 · Cited by 426 · see citing works
Utech, S., & Boccaccini, A. R. (2015) · Journal of Materials Science · doi:10.1007/s10853-015-9382-5 · Cited by 362 · see citing works
Multicomponent peptide assemblies
Raymond, D. M., & Nilsson, B. L. (2018) · Chemical Society Reviews · doi:10.1039/c8cs00115d · Cited by 348 · see citing works
In Situ Imaging of Tissue Remodeling with Collagen Hybridizing Peptides
Hwang, J., Huang, Y., Burwell, T. J., Peterson, N. C., Connor, J., Weiss, S. J., Yu, S. M., & Li, Y. (2017) · ACS Nano · doi:10.1021/acsnano.7b03150 · Cited by 208 · see citing works
Targeting collagen strands by photo-triggered triple-helix hybridization
Li, Y., Foss, C. A., Summerfield, D. D., Doyle, J. J., Torok, C. M., Dietz, H. C., Pomper, M. G., & Yu, S. M. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1209721109 · Cited by 191 · see citing works
Zhang, X., Xu, S., Shen, L., & Li, G. (2020) · Journal of Leather Science and Engineering · doi:10.1186/s42825-020-00033-0 · Cited by 184 · see citing works
Jellyfish collagen scaffolds for cartilage tissue engineering
Hoyer, B., Bernhardt, A., Lode, A., Heinemann, S., Sewing, J., Klinger, M. H. F., Notbohm, H., & Gelinsky, M. (2013) · Acta Biomaterialia · doi:10.1016/j.actbio.2013.10.022 · Cited by 179 · see citing works
Type 1 collagen: Synthesis, structure and key functions in bone mineralization
Vimalraj, S., Sekaran, S., Dhanasekaran, A., & Warrier, S. R. (2024) · Differentiation · doi:10.1016/j.diff.2024.100757 · Cited by 172 · see citing works
Nanostructure of electrospun collagen: Do electrospun collagen fibers form native structures?
Sizeland, K. H., Hofman, K., Hallett, I. C., Martin, D. E., Potgieter, J., Kirby, N. M., Hawley, A. M., Mudie, S., Ryan, T. M., Haverkamp, R., et al. (2018) · Materialia · doi:10.1016/j.mtla.2018.10.001 · Cited by 147 · see citing works
Hwang, J., San, B. H., Turner, N. J., White, L. J., Faulk, D. M., Badylak, S. F., Li, Y., & Yu, S. M. (2017) · Acta Biomaterialia · doi:10.1016/j.actbio.2017.01.079 · Cited by 146 · see citing works
Boran, G., & Regenstein, J. M. (2010) · Advances in food and nutrition research · doi:10.1016/s1043-4526(10)60005-8 · Cited by 145 · see citing works
Kuemin, M., Schweizer, S., Ochsenfeld, C., & Wennemers, H. (2009) · Journal of the American Chemical Society · doi:10.1021/ja906466q · Cited by 131 · see citing works
Rocha‐Mendoza, I., Yankelevich, D. R., Wang, M., Reiser, K. M., Frank, C. W., & Knoesen, A. (2007) · Biophysical Journal · doi:10.1529/biophysj.107.111047 · Cited by 130 · see citing works
Temperature induced denaturation of collagen in acidic solution
Mu, C., Li, D., Lin, W. J., Ding, Y., & Zhang, G. (2007) · Biopolymers · doi:10.1002/bip.20742 · Cited by 129 · see citing works
Electrostatic Interactions Modulate the Conformation of Collagen I
Freudenberg, U., Behrens, S. H., Welzel, P. B., Müller, M., Grimmer, M., Salchert, K., Taeger, T., Schmidt, K., Pompe, W., & Werner, C. (2007) · Biophysical Journal · doi:10.1529/biophysj.106.094284 · Cited by 121 · see citing works
Collagens, Suprastructures, and Collagen Fibril Assembly
Birk, D. E., & Brückner, P. (2010) · Springer eBooks · doi:10.1007/978-3-642-16555-9_3 · Cited by 114 · see citing works
Targeting and mimicking collagens via triple helical peptide assembly
Li, Y., & Yu, S. M. (2013) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2013.10.018 · Cited by 111 · see citing works
Panwar, P., Lamour, G., Mackenzie, N. C. W., Yang, H., Ko, F. C., Li, H., & Brömme, D. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.644310 · Cited by 111 · see citing works
Ultrasonic irradiation in the enzymatic extraction of collagen
Li, D., Mu, C., Cai, S., & Lin, W. J. (2009) · Ultrasonics Sonochemistry · doi:10.1016/j.ultsonch.2009.02.004 · Cited by 109 · see citing works
Collagen cryogel cross-linked by naturally derived dialdehyde carboxymethyl cellulose
Tan, H., Wu, B., Li, C., Mu, C., Li, H., & Lin, W. J. (2015) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2015.04.029 · Cited by 109 · see citing works
Functionalizable Collagen Model Peptides
Erdmann, R. S., & Wennemers, H. (2010) · Journal of the American Chemical Society · doi:10.1021/ja103392t · Cited by 107 · see citing works
Tziveleka, L., Ioannou, E., Tsiourvas, D., Berillis, P., Foufa, E., & Roussis, V. (2017) · Marine Drugs · doi:10.3390/md15060152 · Cited by 105 · see citing works
Native collagen hydrogel nanofibres with anisotropic structure using core-shell electrospinning
Wakuda, Y., Nishimoto, S., Suye, S., & Fujita, S. (2018) · Scientific Reports · doi:10.1038/s41598-018-24700-9 · Cited by 103 · see citing works
Collagen and Its Derivatives Serving Biomedical Purposes: A Review
Wosicka-Frąckowiak, H., Poniedziałek, K., Woźny, S., Kuprianowicz, M., Nyga, M., Jadach, B., & Milanowski, B. (2024) · Polymers · doi:10.3390/polym16182668 · Cited by 101 · see citing works
Direct Detection of Collagenous Proteins by Fluorescently Labeled Collagen Mimetic Peptides
Li, Y., Ho, D., Meng, H., Chan, T. R., An, B., Yu, H., Brodsky, B., Jun, A. S., & Yu, S. M. (2012) · Bioconjugate Chemistry · doi:10.1021/bc3005842 · Cited by 101 · see citing works
Schroeter, E. R., DeHart, C. J., Cleland, T. P., Zheng, W., Thomas, P. M., Kelleher, N. L., Bern, M. W., & Schweitzer, M. H. (2017) · Journal of Proteome Research · doi:10.1021/acs.jproteome.6b00873 · Cited by 99 · see citing works
PEG-Based Hydrogels with Collagen Mimetic Peptide-Mediated and Tunable Physical Cross-Links
Stahl, P. J., Romano, N. H., Wirtz, D., & Yu, S. M. (2010) · Biomacromolecules · doi:10.1021/bm100465q · Cited by 98 · see citing works
Boyatzis, S. C., Velivasaki, G., & Malea, E. (2016) · Heritage Science · doi:10.1186/s40494-016-0083-4 · Cited by 95 · see citing works
Lim, N. S. J., Hamed, Z., Yeow, C., Chan, C. K., & Huang, Z. (2011) · Journal of Biomedical Optics · doi:10.1117/1.3528006 · Cited by 95 · see citing works
Erdmann, R. S., & Wennemers, H. (2011) · Angewandte Chemie International Edition · doi:10.1002/anie.201008118 · Cited by 90 · see citing works
Simon, P., Grüner, D., Worch, H., Pompe, W., Lichte, H., Khassawna, T. E., Heiß, C., Wenisch, S., & Kniep, R. (2018) · Scientific Reports · doi:10.1038/s41598-018-31983-5 · Cited by 89 · see citing works
Krishna, O. D., & Kiick, K. L. (2009) · Biomacromolecules · doi:10.1021/bm900551c · Cited by 89 · see citing works
Desorption of nutrients and flavor compounds formation during the cooking of bone soup
Meng, Q., Zhou, J., Gao, D., Xu, E., Guo, M., & Liu, D. (2021) · Food Control · doi:10.1016/j.foodcont.2021.108408 · Cited by 88 · see citing works
4‐Chloroprolines: Synthesis, conformational analysis, and effect on the collagen triple helix
Shoulders, M. D., Guzei, I. A., & Raines, R. T. (2007) · Biopolymers · doi:10.1002/bip.20864 · Cited by 85 · see citing works
Erdmann, R. S., & Wennemers, H. (2012) · Journal of the American Chemical Society · doi:10.1021/ja3066418 · Cited by 85 · see citing works
Use of Collagen in Cosmetic Products
Jadach, B., Mielcarek, Z., & Osmałek, T. Z. (2024) · Current Issues in Molecular Biology · doi:10.3390/cimb46030132 · Cited by 84 · see citing works
Dewle, A., Pathak, N., Rakshasmare, P., & Srivastava, A. (2020) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.9b01225 · Cited by 83 · see citing works
Self-complementary peptides for the formation of collagen-like triple helical supramolecules
Koide, T., Homma, D. L., Asada, S., & Kitagawa, K. (2005) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2005.08.041 · Cited by 79 · see citing works
Parallel and Antiparallel Triple Helices of Naphthyridine Oligoamides
Ferrand, Y., Kendhale, A. M., Garric, J., Kauffmann, B., & Huc, I. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.200906401 · Cited by 79 · see citing works
Electrostatic effects in collagen fibril formation
Morozova, S., & Muthukumar, M. (2018) · The Journal of Chemical Physics · doi:10.1063/1.5036526 · Cited by 77 · see citing works
Petrenko, I., Summers, A. P., Simon, P., Żółtowska‐Aksamitowska, S., Motylenko, M., Schimpf, C., Rafaja, D., Roth, F., Kummer, K., Brendler, E., et al. (2019) · Science Advances · doi:10.1126/sciadv.aax2805 · Cited by 76 · see citing works
Chaperoning osteogenesis: new protein-folding disease paradigms
Makareeva, E., Aviles, N. A., & Leikin, S. (2010) · Trends in Cell Biology · doi:10.1016/j.tcb.2010.11.007 · Cited by 75 · see citing works
Effects of various salts on structural polymorphism of reconstituted type I collagen fibrils
Li, Y., & Douglas, E. P. (2013) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2013.07.037 · Cited by 73 · see citing works
Spatio-Temporal Modification of Collagen Scaffolds Mediated by Triple Helical Propensity
Wang, A. Y., Foss, C. A., Leong, S., Mo, X., Pomper, M. G., & Yu, S. M. (2008) · Biomacromolecules · doi:10.1021/bm701378k · Cited by 71 · see citing works
The Aberrance of the 4S Diastereomer of 4-Hydroxyproline
Shoulders, M. D., Kotch, F. W., Choudhary, A., Guzei, I. A., & Raines, R. T. (2010) · Journal of the American Chemical Society · doi:10.1021/ja103082y · Cited by 71 · see citing works
Cross-Linked Collagen Triple Helices by Oxime Ligation
Hentzen, N. B., Smeenk, L. E. J., Witek, J., Riniker, S., & Wennemers, H. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b07498 · Cited by 70 · see citing works
Xu, Y., & Kirchner, M. (2021) · Bioengineering · doi:10.3390/bioengineering8010005 · Cited by 69 · see citing works
Collagen Formation and Structure
Bächinger, H. P., Mizuno, K., Vranka, J. A., & Boudko, S. P. (2010) · Elsevier eBooks · doi:10.1016/b978-008045382-8.00698-5 · Cited by 69 · see citing works
Self-citationSaitta, E. T., Liang, R., Lau, M. C., Brown, C. M., Longrich, N. R., Kaye, T. G., Novak, B. J., Salzberg, S. L., Norell, M. A., Abbott, G. D., et al. (2019) · eLife · doi:10.7554/elife.46205 · Cited by 67 · see citing works
The Chemistry and Biology of Collagen Hybridization
Li, X., Zhang, Q., Yu, S. M., & Li, Y. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.3c00713 · Cited by 67 · see citing works
Gao, D., Cheng, Y., Wang, P., Li, F., Wu, Y., Lyu, B., Ma, J., & Qin, J. (2020) · Journal of Cleaner Production · doi:10.1016/j.jclepro.2020.120546 · Cited by 67 · see citing works
Collagen based polyurethanes—A review of recent advances and perspective
Zuber, M., Zia, F., Zia, K. M., Tabasum, S., Salman, M., & Sultan, N. (2015) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2015.07.001 · Cited by 67 · see citing works
Kinetic Hysteresis in Collagen Folding
Mizuno, K., Boudko, S. P., Engel, J., & Bächinger, H. P. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2010.03.019 · Cited by 66 · see citing works
Self-citationDSC investigation of bovine hide collagen at varying degrees of crosslinking and humidities
Schröpfer, M., & Meyer, M. (2017) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2017.04.124 · Cited by 66 · see citing works
Wiss, K. T., Krishna, O. D., Roth, P. J., Kiick, K. L., & Théato, P. (2009) · Macromolecules · doi:10.1021/ma900417n · Cited by 65 · see citing works
FTIR spectro-imaging of collagens for characterization and grading of gliomas
Noreen, R., Moenner, M., Hwu, Y., & Petibois, C. (2012) · Biotechnology Advances · doi:10.1016/j.biotechadv.2012.03.009 · Cited by 65 · see citing works
Joy, J. M., Amruth, P., Akshay, P., Paul, P. T., Rosemol Jacob, M., & Mathew, S. (2024) · Foods · doi:10.3390/foods13172793 · Cited by 64 · see citing works
Hsu, W., Chen, Y.-L., & Horng, J. (2012) · Langmuir · doi:10.1021/la204351w · Cited by 64 · see citing works
Intrinsic disorder of the extracellular matrix
Peysselon, F., Xue, B., Uversky, V. N., & Ricard‐Blum, S. (2011) · Molecular BioSystems · doi:10.1039/c1mb05316g · Cited by 60 · see citing works
Bachmann, A., Kiefhaber, T., Boudko, S. P., Engel, J., & Bächinger, H. P. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0505141102 · Cited by 60 · see citing works
Self-citationRegion‐specific role of water in collagen unwinding and assembly
Ravikumar, K. M., & Hwang, W. (2008) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22026 · Cited by 59 · see citing works
A Collagen Peptide‐Based Physical Hydrogel for Cell Encapsulation
Pérez, C. M. R., Panitch, A., & Chmielewski, J. A. (2011) · Macromolecular Bioscience · doi:10.1002/mabi.201100230 · Cited by 59 · see citing works
General Solution for Stabilizing Triple Helical Collagen
Zhang, Y., Herling, M. R., & Chenoweth, D. M. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b03823 · Cited by 57 · see citing works
The characterization of acid and pepsin soluble collagen from ovine bones (Ujumuqin sheep)
Gao, L., Wang, Z., Zheng, L., Zhang, C., & Zhang, D. (2018) · Journal of Integrative Agriculture · doi:10.1016/s2095-3119(17)61751-9 · Cited by 54 · see citing works
Roulet, M., Ruggiero, F., Karsenty, G., & Guellec, D. L. (2006) · Cell and Tissue Research · doi:10.1007/s00441-006-0294-1 · Cited by 53 · see citing works
Hydrophobic Moieties Bestow Fast-Folding and Hyperstability on Collagen Triple Helices
Egli, J., Siebler, C., Köhler, M., Zenobi, R., & Wennemers, H. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.8b13871 · Cited by 53 · see citing works
Egli, J., Esposito, C., Müri, M., Riniker, S., & Wennemers, H. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.1c01512 · Cited by 52 · see citing works
Amino and carboxyl plasma functionalization of collagen films for tissue engineering applications
Taraballi, F., Zanini, S., Lupo, C., Panseri, S., Cunha, C., ̃Riccardi, C., Marcacci, M., Campione, M., & Cipolla, L. (2012) · Journal of Colloid and Interface Science · doi:10.1016/j.jcis.2012.11.041 · Cited by 50 · see citing works
Interplay between Covalent and Physical Interactions within Environment Sensitive Hydrogels
Jeong, K. J., & Panitch, A. (2009) · Biomacromolecules · doi:10.1021/bm801270k · Cited by 50 · see citing works
Collagen Structure, Folding and Function
Makareeva, E., & Leikin, S. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-397165-4.00007-1 · Cited by 48 · see citing works
Collagen and collagen mimetic peptide conjugates in polymer science
He, L., & Théato, P. (2013) · European Polymer Journal · doi:10.1016/j.eurpolymj.2013.05.033 · Cited by 45 · see citing works
Ishikawa, Y., Boudko, S. P., & Bächinger, H. P. (2015) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.12.024 · Cited by 45 · see citing works
Self-citationModulating Extracellular Matrix at Interfaces of Polymeric Materials
Werner, C., Pompe, W., & Salchert, K. (2006) · Advances in polymer science · doi:10.1007/12_089 · Cited by 45 · see citing works
Zhao, H.-F., Feng, L., Jiang, W., Liu, Y., Jiang, J., Wu, P., Zhao, J., Kuang, S., Tang, L. Y., Tang, W., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0142915 · Cited by 44 · see citing works
Role of side chains in collagen triple helix stabilization and partner recognition
Berisio, R., Simone, A. D., Ruggiero, A., Improta, R., & Vitagliano, L. (2008) · Journal of Peptide Science · doi:10.1002/psc.1082 · Cited by 43 · see citing works
Shi, J., Wang, C., Ngai, T., & Lin, W. J. (2018) · Langmuir · doi:10.1021/acs.langmuir.8b00923 · Cited by 42 · see citing works
Morphological transformations in a dually thermoresponsive coil–rod–coil bioconjugate
Krishna, O. D., Wiss, K. T., Luo, T., Pochan, D. J., Théato, P., & Kiick, K. L. (2012) · Soft Matter · doi:10.1039/c2sm07025a · Cited by 41 · see citing works
Assessing Collagen D-Band Periodicity with Atomic Force Microscopy
Stylianou, A. (2022) · Materials · doi:10.3390/ma15041608 · Cited by 40 · see citing works
Differential Unfolding of α1 and α2 Chains in Type I Collagen and Collagenolysis
Nerenberg, P. S., & Stultz, C. M. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.07.009 · Cited by 40 · see citing works
Kuemin, M., Engel, J., & Wennemers, H. (2010) · Journal of Peptide Science · doi:10.1002/psc.1245 · Cited by 40 · see citing works
Self-citationErdmann, R. S., & Wennemers, H. (2012) · Organic & Biomolecular Chemistry · doi:10.1039/c2ob06720j · Cited by 39 · see citing works
Optimization of a Multi-Step Procedure for Isolation of Chicken Bone Collagen
Cansu, Ü., & Boran, G. (2015) · Korean Journal for Food Science of Animal Resources · doi:10.5851/kosfa.2015.35.4.431 · Cited by 38 · see citing works
pH‐Responsive Aminoproline‐Containing Collagen Triple Helices
Egli, J., Siebler, C., Maryasin, B., Erdmann, R. S., Bergande, C., Ochsenfeld, C., & Wennemers, H. (2017) · Chemistry - A European Journal · doi:10.1002/chem.201701134 · Cited by 35 · see citing works
Kusebauch, U., Cadamuro, S. A., Musiol, H., Moroder, L., & Renner, C. (2007) · Chemistry - A European Journal · doi:10.1002/chem.200601162 · Cited by 35 · see citing works
Protein adsorption can be reversibly switched on and off on mixed PEO/PAA brushes
Delcroix, M., Laurent, S., Huet, G., & Dupont-Gillain, C. C. (2014) · Acta Biomaterialia · doi:10.1016/j.actbio.2014.09.010 · Cited by 34 · see citing works
New cellulose-collagen-alginate materials incorporated with quercetin, anthocyanins and lipoic acid
Anghel, N., Dinu, M. V., Zaltariov, M., Pamfil, D., & Spiridon, I. (2021) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2021.03.120 · Cited by 34 · see citing works
Arya, S., Hadjievangelou, N., Lei, S., Kudo, H., Goldin, R. D., Darzi, A. W., Elson, D. S., & Hanna, G. B. (2013) · Surgical Endoscopy · doi:10.1007/s00464-013-2935-2 · Cited by 33 · see citing works
Direct Radiation Effects on the Structure and Stability of Collagen and Other Proteins
Lalande, M., Schwob, L., Vizcaino, V., Chirot, F., Dugourd, P., Schlathölter, T., & Poully, J. (2019) · ChemBioChem · doi:10.1002/cbic.201900202 · Cited by 33 · see citing works
Dara, P. K., Raghavankutty, M., Sebastian, N., Chatterjee, N. S., Mathew, S., RAVISHANKAR, C. N., & Anandan, R. (2020) · Journal of Aquatic Food Product Technology · doi:10.1080/10498850.2020.1749745 · Cited by 33 · see citing works
Natural polymer-based hydrogels: versatile biomaterials for biomedical applications
Angaria, N., Saini, S., Hussain, M. S., Sharma, S., Singh, G., Khurana, N., & Kumar, R. (2024) · International Journal of Polymeric Materials · doi:10.1080/00914037.2023.2301645 · Cited by 32 · see citing works
Huster, D. (2008) · Annual reports on NMR spectroscopy · doi:10.1016/s0066-4103(08)00004-5 · Cited by 32 · see citing works
Templated Collagen “Double Helices” Maintain Their Structure
Tanrikulu, I. C., Westler, W. M., Ellison, A. J., Markley, J. L., & Raines, R. T. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.9b07583 · Cited by 32 · see citing works
Value Addition to Leather Industry Wastes and By-Products: Hydrolyzed Collagen and Collagen Peptides
Yorgancıoğlu, A., Başaran, B., & Sancaklı, A. (2020) · IntechOpen eBooks · doi:10.5772/intechopen.92699 · Cited by 32 · see citing works
A Single Stereodynamic Center Modulates the Rate of Self‐Assembly in a Biomolecular System
Zhang, Y., Malamakal, R. M., & Chenoweth, D. M. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201504459 · Cited by 31 · see citing works
Stabilization and Anomalous Hydration of Collagen Fibril under Heating
Gevorkian, S. G., ALLAHVERDYAN, A. E., Gevorgyan, D. S., Simonian, A. L., & Hu, C. (2013) · PLoS ONE · doi:10.1371/journal.pone.0078526 · Cited by 31 · see citing works
Synthesis and solid state NMR characterization of novel peptide/silica hybrid materials
Werner, M., Heil, A., Rothermel, N., Breitzke, H., Groszewicz, P. B., Thankamony, A. S. L., Gutmann, T., & Buntkowsky, G. (2015) · Solid State Nuclear Magnetic Resonance · doi:10.1016/j.ssnmr.2015.09.008 · Cited by 29 · see citing works
Punitha, V., Raman, S. S., Parthasarathi, R., Subramanian, V., Rao, J. R., Nair, B. U., & Ramasami, T. (2009) · The Journal of Physical Chemistry B · doi:10.1021/jp808690m · Cited by 29 · see citing works
Impacts of fullerene derivatives on regulating the structure and assembly of collagen molecules
Yin, X., Zhao, L., Kang, S.-G., Pan, J. L., Song, Y. L., Zhang, M., Xing, G., Wang, F., Li, J., Zhou, R., et al. (2013) · Nanoscale · doi:10.1039/c3nr01469j · Cited by 28 · see citing works
Zhao, Q., Jia, T., Cao, Q. C., Tian, F., & Ying, W. T. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19061699 · Cited by 28 · see citing works
- Authors
- Engel, J., & Bächinger, H. P.
- Affiliations
- University of Basel (CH)
- Oregon Health & Science University (US)
- Corresponding author
- Engel, Jürgen
- Venue
- Topics in Current Chemistry
- Publisher
- Springer Berlin Heidelberg
- Published
- 2005-04-12
- Pages
- 7-33
- ISSN
- 0340-1022 (ISSN-L)
- 1436-5049
- OpenAlex
- W2561310140
- Cited by
- 254
- References
- 5
- Citations by year
- 2026: 7 · 2025: 17 · 2024: 18 · 2023: 8 · 2022: 12 · 2021: 14 · 2020: 11 · 2019: 11 · 2018: 14 · 2017: 11 · 2016: 13 · 2015: 19 · 2014: 6 · 2013: 14 · 2012: 14
- FWCI
- 10.40
- Type
- book chapter
- Language
- en
- Open access
- closed
- Locations
- Topics in current chemistry (publishedVersion)
- Topics
- Physical Sciences › Materials Science › Biomaterials › Collagen: Extraction and Characterization
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Connective tissue disorders research
- Keywords
- collagen triple helix, triple helix stability, protein folding, proline, hydroxyproline, cis-trans isomerization, trimerization domain, oligomerization domain, model peptides, collagen mutations
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