다음과 같은 기능을 한번의 로그인으로 사용 할 수 있습니다.
NTIS 바로가기
ACS biomaterials science & engineering, v.3 no.6, 2017년, pp.1136 - 1145
Anand, Bibin G. (Department of Bioscience and Bioengineering, Indian Institute of Technology Jodhpur, Rajasthan 342011,) , Shekhawat, Dolat S. (Department of Bioscience and Bioengineering, Indian Institute of Technology Jodhpur, Rajasthan 342011,) , Dubey, Kriti (Department of Bioscience and Bioengineering, Indian Institute of Technology Jodhpur, Rajasthan 342011,) , Kar, Karunakar (School of Life Sciences, Jawaharlal Nehru University, New Delhi 110067,)
AI-Helper
Because the process of insulin fibril assembly is linked to a multitude of medical problems, finding effective and biocompatible inhibitors against such an aggregation process could be beneficial. Targeting the aggregation-prone residues of insulin may perhaps work as an effective strategy to preven...
Aguzzi, Adriano, O'Connor, Tracy. Protein aggregation diseases: pathogenicity and therapeutic perspectives. Nature reviews. Drug discovery, vol.9, no.3, 237-248.
Greenwald, Jason, Riek, Roland. Biology of Amyloid: Structure, Function, and Regulation. Structure, vol.18, no.10, 1244-1260.
Chiti, Fabrizio, Dobson, Christopher M.. PROTEIN MISFOLDING, FUNCTIONAL AMYLOID, AND HUMAN DISEASE. Annual review of biochemistry, vol.75, 333-366.
Chatani, Eri, Imamura, Hiroshi, Yamamoto, Naoki, Kato, Minoru. Stepwise Organization of the β-Structure Identifies Key Regions Essential for the Propagation and Cytotoxicity of Insulin Amyloid Fibrils. The Journal of biological chemistry, vol.289, no.15, 10399-10410.
Wei, Yan, Chen, Lan, Chen, Ji, Ge, Lin, He, Rong Qiao. Rapid glycation with D-ribose induces globular amyloid-like aggregations of BSA with high cytotoxicity to SH-SY5Y cells. Bmc cell biology, vol.10, 10-10.
Wang, Feng, Hull, Rebecca L., Vidal, Josep, Cnop, Miriam, Kahn, Steven E.. Islet Amyloid Develops Diffusely Throughout the Pancreas Before Becoming Severe and Replacing Endocrine Cells. Diabetes, vol.50, no.11, 2514-2520.
Luo, Jinghui, Wärmländer, Sebastian K. T. S., Gräslund, Astrid, Abrahams, Jan Pieter. Reciprocal Molecular Interactions between the Aβ Peptide Linked to Alzheimer’s Disease and Insulin Linked to Diabetes Mellitus Type II. ACS chemical neuroscience, vol.7, no.3, 269-274.
Nielsen, L., Khurana, R., Coats, A., Frokjaer, S., Brange, J., Vyas, S., Uversky, V. N., Fink, A. L.. Effect of Environmental Factors on the Kinetics of Insulin Fibril Formation: Elucidation of the Molecular Mechanism. Biochemistry, vol.40, no.20, 6036-6046.
Brange, Jens, Havelund, Svend, Hougaard, Philip. Chemical Stability of Insulin. 2. Formation of Higher Molecular Weight Transformation Products During Storage of Pharmaceutical Preparations. Pharmaceutical research, vol.9, no.6, 727-734.
Ghosh, Ranendu, Sharma, Sunny, Chattopadhyay, Krishnananda. Effect of Arginine on Protein Aggregation Studied by Fluorescence Correlation Spectroscopy and Other Biophysical Methods. Biochemistry, vol.48, no.5, 1135-1143.
Kar, Karunakar, Kishore, Nand. Enhancement of thermal stability and inhibition of protein aggregation by osmolytic effect of hydroxyproline. Biopolymers, vol.87, no.5, 339-351.
Shiraki, K., Kudou, M., Fujiwara, S., Imanaka, T., Takagi, M.. Biophysical Effect of Amino Acids on the Prevention of Protein Aggregation. The Journal of biochemistry, vol.132, no.4, 591-595.
Rajasekhar, K., Suresh, S. N., Manjithaya, Ravi, Govindaraju, T.. Rationally Designed Peptidomimetic Modulators of Aβ Toxicity in Alzheimer's Disease. Scientific reports, vol.5, 8139-.
Viet, Man Hoang, Ngo, Son Tung, Lam, Nguyen Sy, Li, Mai Suan. Inhibition of Aggregation of Amyloid Peptides by Beta-Sheet Breaker Peptides and Their Binding Affinity. The journal of physical chemistry. B, Condensed matter, materials, surfaces, interfaces & biophysical, vol.115, no.22, 7433-7446.
Dubey, Kriti, Anand, Bibin G., Badhwar, Rahul, Bagler, Ganesh, Navya, P. N., Daima, Hemant Kumar, Kar, Karunakar. Tyrosine- and tryptophan-coated gold nanoparticles inhibit amyloid aggregation of insulin. Amino acids, vol.47, no.12, 2551-2560.
Álvarez, Yanina D., Fauerbach, Jonathan A., Pellegrotti, Jésica V., Jovin, Thomas M., Jares-Erijman, Elizabeth A., Stefani, Fernando D.. Influence of Gold Nanoparticles on the Kinetics of α-Synuclein Aggregation. Nano letters : a journal dedicated to nanoscience and nanotechnology, vol.13, no.12, 6156-6163.
Siposova, Katarina, Kubovcikova, Martina, Bednarikova, Zuzana, Koneracka, Martina, Zavisova, Vlasta, Antosova, Andrea, Kopcansky, Peter, Daxnerova, Zuzana, Gazova, Zuzana. Depolymerization of insulin amyloid fibrils by albumin-modified magnetic fluid. Nanotechnology, vol.23, no.5, 055101-.
Palmal, Sharbari, Maity, Amit Ranjan, Singh, Brijesh Kumar, Basu, Sreetama, Jana, Nihar R., Jana, Nikhil R.. Inhibition of Amyloid Fibril Growth and Dissolution of Amyloid Fibrils by Curcumin–Gold Nanoparticles. Chemistry : a European journal, vol.20, no.20, 6184-6191.
Cabaleiro-Lago, Celia, Quinlan-Pluck, Fiona, Lynch, Iseult, Dawson, Kenneth A., Linse, Sara. Dual Effect of Amino Modified Polystyrene Nanoparticles on Amyloid β Protein Fibrillation. ACS chemical neuroscience, vol.1, no.4, 279-287.
Cabaleiro-Lago, Celia, Quinlan-Pluck, Fiona, Lynch, Iseult, Lindman, Stina, Minogue, Aedin M., Thulin, Eva, Walsh, Dominic M., Dawson, Kenneth A., Linse, Sara. Inhibition of Amyloid β Protein Fibrillation by Polymeric Nanoparticles. Journal of the American Chemical Society, vol.130, no.46, 15437-15443.
Brambilla, Davide, Verpillot, Romain, Le Droumaguet, Benjamin, Nicolas, Julien, Taverna, Myriam, Kóňa, Juraj, Lettiero, Barbara, Hashemi, S. Hossein, De Kimpe, Line, Canovi, Mara, Gobbi, Marco, Nicolas, Valérie, Scheper, Wiep, Moghimi, S. Moein, Tvaroška, Igor, Couvreur, Patrick, Andrieux, Karine. PEGylated Nanoparticles Bind to and Alter Amyloid-Beta Peptide Conformation: Toward Engineering of Functional Nanomedicines for Alzheimer’s Disease. ACS nano, vol.6, no.7, 5897-5908.
Kim, Yuna, Park, Ji-Hyun, Lee, Hyojin, Nam, Jwa-Min. How Do the Size, Charge and Shape of Nanoparticles Affect Amyloid β Aggregation on Brain Lipid Bilayer?. Scientific reports, vol.6, 19548-.
Anand, Bibin G., Dubey, Kriti, Shekhawat, Dolat Singh, Kar, Karunakar. Capsaicin-Coated Silver Nanoparticles Inhibit Amyloid Fibril Formation of Serum Albumin. Biochemistry, vol.55, no.24, 3345-3348.
Chinta, Gopichand, Ramya Chandar Charles, Mariasoosai, Klopčič, Ivana, Sollner Dolenc, Marija, Periyasamy, Latha, Selvaraj Coumar, Mohane. In Silico and In Vitro Investigation of the Piperineʼs Male Contraceptive Effect: Docking and Molecular Dynamics Simulation Studies in Androgen-Binding Protein and Androgen Receptor. Planta medica, vol.81, no.10, 804-812.
Zsila, F., Hazai, E., Sawyer, L.. Binding of the Pepper Alkaloid Piperine to Bovine &bgr;-Lactoglobulin: Circular Dichroism Spectroscopy and Molecular Modeling Study. Journal of agricultural and food chemistry, vol.53, no.26, 10179-10185.
Haris, P., Mary, Varughese, Haridas, M., Sudarsanakumar, C.. Energetics, Thermodynamics, and Molecular Recognition of Piperine with DNA. Journal of chemical information and modeling, vol.55, no.12, 2644-2656.
Yeggoni, Daniel Pushparaju, Rachamallu, Aparna, Kallubai, Monika, Subramanyam, Rajagopal. Cytotoxicity and comparative binding mechanism of piperine with human serum albumin and α-1-acid glycoprotein. Journal of biomolecular structure & dynamics, vol.33, no.6, 1336-1351.
Ivanova, Magdalena I., Sievers, Stuart A., Sawaya, Michael R., Wall, Joseph S., Eisenberg, David. Molecular basis for insulin fibril assembly. Proceedings of the National Academy of Sciences of the United States of America, vol.106, no.45, 18990-18995.
Ivanova, Magdalena I., Thompson, Michael J., Eisenberg, David. A systematic screen of β 2 -microglobulin and insulin for amyloid-like segments. Proceedings of the National Academy of Sciences of the United States of America, vol.103, no.11, 4079-4082.
Perumal, Sathiamurthi, Dubey, Kriti, Badhwar, Rahul, George, Kodimattan Joseph, Sharma, Rakesh Kumar, Bagler, Ganesh, Madhan, Balaraman, Kar, Karunakar. Capsaicin inhibits collagen fibril formation and increases the stability of collagen fibers. European biophysics journal with biophysics letters, vol.44, no.1, 69-76.
Dubey, K., Kar, K.. Type I collagen prevents amyloid aggregation of hen egg white lysozyme. Biochemical and biophysical research communications, vol.448, no.4, 480-484.
Dubey, Kriti, Anand, Bibin G., Temgire, Mayur K., Kar, Karunakar. Evidence of Rapid Coaggregation of Globular Proteins during Amyloid Formation. Biochemistry, vol.53, no.51, 8001-8004.
Morozova-Roche, L.A., Zurdo, J., Spencer, A., Noppe, W., Receveur, V., Archer, D.B., Joniau, M., Dobson, C.M.. Amyloid Fibril Formation and Seeding by Wild-Type Human Lysozyme and Its Disease-Related Mutational Variants. Journal of structural biology, vol.130, no.2, 339-351.
Kar, Karunakar, Arduini, Irene, Drombosky, Kenneth W., van der Wel, Patrick C.A., Wetzel, Ronald. D-Polyglutamine Amyloid Recruits L-Polyglutamine Monomers and Kills Cells. Journal of molecular biology, vol.426, no.4, 816-829.
Dubey, Kriti, Anand, Bibin G., Shekhawat, Dolat Singh, Kar, Karunakar. Eugenol prevents amyloid formation of proteins and inhibits amyloid-induced hemolysis. Scientific reports, vol.7, 40744-.
Mattson, Mark P, Begley, James G, Mark, Robert J, Furukawa, Katsutoshi. Aβ25–35 induces rapid lysis of red blood cells: contrast with Aβ1–42 and examination of underlying mechanisms. Brain research, vol.771, no.1, 147-153.
Pechkova, Eugenia, Bragazzi, Nicola Luigi, Bozdaganyan, Marine, Belmonte, Luca, Nicolini, Claudio. A Review of the Strategies for Obtaining High-Quality Crystals Utilizing Nanotechnologies and Microgravity. Critical reviews in eukaryotic gene expression, vol.24, no.4, 325-339.
Brooks, B. R., Brooks III, C. L., Mackerell Jr., A. D., Nilsson, L., Petrella, R. J., Roux, B., Won, Y., Archontis, G., Bartels, C., Boresch, S., Caflisch, A., Caves, L., Cui, Q., Dinner, A. R., Feig, M., Fischer, S., Gao, J., Hodoscek, M., Im, W., Kuczera, K., Lazaridis, T., Ma, J., Ovchinnikov, V., Paci, E., Pastor, R. W., Post, C. B., Pu, J. Z., Schaefer, M., Tidor, B., Venable, R. M., Woodcock, H. L., Wu, X., Yang, W., York, D. M., Karplus, M.. CHARMM: The biomolecular simulation program. Journal of computational chemistry, vol.30, no.10, 1545-1614.
Wu, Guosheng, Robertson, Daniel H., Brooks III, Charles L., Vieth, Michal. Detailed analysis of grid-based molecular docking: A case study of CDOCKER—A CHARMm-based MD docking algorithm. Journal of computational chemistry, vol.24, no.13, 1549-1562.
Schulz, H., Baranska, M.. Identification and quantification of valuable plant substances by IR and Raman spectroscopy. Vibrational spectroscopy : an international journal devoted to applications of infrared and Raman spectroscopy, vol.43, no.1, 13-25.
Lee, Jiyong, Culyba, Elizabeth K., Powers, Evan T., Kelly, Jeffery W.. Amyloid-β Forms Fibrils by Nucleated Conformational Conversion of Oligomers. Nature chemical biology, vol.7, no.9, 602-609.
Erlkamp, Mirko, Grobelny, Sebastian, Faraone, Antonio, Czeslik, Claus, Winter, Roland. Solvent Effects on the Dynamics of Amyloidogenic Insulin Revealed by Neutron Spin Echo Spectroscopy. The journal of physical chemistry. B, Condensed matter, materials, surfaces, interfaces & biophysical, vol.118, no.12, 3310-3316.
Librizzi, Fabio, Carrotta, Rita, Spigolon, Dario, Bulone, Donatella, San Biagio, Pier Luigi. α-Casein Inhibits Insulin Amyloid Formation by Preventing the Onset of Secondary Nucleation Processes. The journal of physical chemistry letters, vol.5, no.17, 3043-3048.
Mishra, Narendra Kumar, Krishna Deepak, R. N. V., Sankararamakrishnan, Ramasubbu, Verma, Sandeep. Controlling in Vitro Insulin Amyloidosis with Stable Peptide Conjugates: A Combined Experimental and Computational Study. The journal of physical chemistry. B, Condensed matter, materials, surfaces, interfaces & biophysical, vol.119, no.50, 15395-15406.
Dutta, Colina, Yang, Mu, Long, Fei, Shahbazian-Yassar, Reza, Tiwari, Ashutosh. Preformed Seeds Modulate Native Insulin Aggregation Kinetics. The journal of physical chemistry. B, Condensed matter, materials, surfaces, interfaces & biophysical, vol.119, no.49, 15089-15099.
Soldi, G., Plakoutsi, G., Taddei, N., Chiti, F.. Stabilization of a Native Protein Mediated by Ligand Binding Inhibits Amyloid Formation Independently of the Aggregation Pathway. Journal of medicinal chemistry, vol.49, no.20, 6057-6064.
Cejas, Mabel A., Kinney, William A., Chen, Cailin, Vinter, Jeremy G., Almond Jr., Harold R., Balss, Karin M., Maryanoff, Cynthia A., Schmidt, Ute, Breslav, Michael, Mahan, Andrew, Lacy, Eilyn, Maryanoff, Bruce E.. Thrombogenic collagen-mimetic peptides: Self-assembly of triple helix-based fibrils driven by hydrophobic interactions. Proceedings of the National Academy of Sciences of the United States of America, vol.105, no.25, 8513-8518.
Kar, Karunakar, Ibrar, Sajjad, Nanda, Vikas, Getz, Todd M., Kunapuli, Satya P., Brodsky, Barbara. Aromatic Interactions Promote Self-Association of Collagen Triple-Helical Peptides to Higher-Order Structures. Biochemistry, vol.48, no.33, 7959-7968.
Kar, Karunakar, Amin, Priyal, Bryan, Michael A., Persikov, Anton V., Mohs, Angela, Wang, Yuh-Hwa, Brodsky, Barbara. Self-association of Collagen Triple Helic Peptides into Higher Order Structures. The Journal of biological chemistry, vol.281, no.44, 33283-33290.
Blood Savage B. 2704 94 1999 10.1182/blood.V94.8.2704.420k41_2704_2715
Porat, Yair, Abramowitz, Adel, Gazit, Ehud. Inhibition of Amyloid Fibril Formation by Polyphenols: Structural Similarity and Aromatic Interactions as a Common Inhibition Mechanism. Chemical biology & drug design, vol.67, no.1, 27-37.
Gong, Hao, He, Zihao, Peng, Anlin, Zhang, Xin, Cheng, Biao, Sun, Yue, Zheng, Ling, Huang, Kun. Effects of several quinones on insulin aggregation. Scientific reports, vol.4, 5648-.
Cheng, B., Gong, H., Xiao, H., Petersen, R.B., Zheng, L., Huang, K.. Inhibiting toxic aggregation of amyloidogenic proteins: A therapeutic strategy for protein misfolding diseases. Biochimica et biophysica acta, General subjects, vol.1830, no.10, 4860-4871.
*원문 PDF 파일 및 링크정보가 존재하지 않을 경우 KISTI DDS 시스템에서 제공하는 원문복사서비스를 사용할 수 있습니다.
Copyright KISTI. All Rights Reserved.
※ AI-Helper는 부적절한 답변을 할 수 있습니다.