Статті в журналах з теми "Macromolecular crowding agents"
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Ознайомтеся з топ-38 статей у журналах для дослідження на тему "Macromolecular crowding agents".
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De Pieri, Andrea, Shubhasmin Rana, Stefanie Korntner, and Dimitrios I. Zeugolis. "Seaweed polysaccharides as macromolecular crowding agents." International Journal of Biological Macromolecules 164 (December 2020): 434–46. http://dx.doi.org/10.1016/j.ijbiomac.2020.07.087.
Повний текст джерелаLee, Hong Bok, Anh Cong, Hannah Leopold, Megan Currie, Arnold J. Boersma, Erin D. Sheets, and Ahmed A. Heikal. "Rotational and translational diffusion of size-dependent fluorescent probes in homogeneous and heterogeneous environments." Physical Chemistry Chemical Physics 20, no. 37 (2018): 24045–57. http://dx.doi.org/10.1039/c8cp03873b.
Повний текст джерелаStepanenko, Olesya V., Olga V. Stepanenko, Irina M. Kuznetsova, and Konstantin K. Turoverov. "The unfolding of iRFP713 in a crowded milieu." PeerJ 7 (April 8, 2019): e6707. http://dx.doi.org/10.7717/peerj.6707.
Повний текст джерелаdel Álamo, Marta, Germán Rivas, and Mauricio G. Mateu. "Effect of Macromolecular Crowding Agents on Human Immunodeficiency Virus Type 1 Capsid Protein Assembly In Vitro." Journal of Virology 79, no. 22 (November 15, 2005): 14271–81. http://dx.doi.org/10.1128/jvi.79.22.14271-14281.2005.
Повний текст джерелаGnutt, David, and Simon Ebbinghaus. "The macromolecular crowding effect – from in vitro into the cell." Biological Chemistry 397, no. 1 (January 1, 2016): 37–44. http://dx.doi.org/10.1515/hsz-2015-0161.
Повний текст джерелаVweza, Alick-O., Chul-Gyu Song, and Kil-To Chong. "Liquid–Liquid Phase Separation in the Presence of Macromolecular Crowding and State-Dependent Kinetics." International Journal of Molecular Sciences 22, no. 13 (June 22, 2021): 6675. http://dx.doi.org/10.3390/ijms22136675.
Повний текст джерелаZhou, Huan-Xiang. "Effect of mixed macromolecular crowding agents on protein folding." Proteins: Structure, Function, and Bioinformatics 72, no. 4 (May 27, 2008): 1109–13. http://dx.doi.org/10.1002/prot.22111.
Повний текст джерелаBiswas, Saikat, and Pramit K. Chowdhury. "Unusual domain movement in a multidomain protein in the presence of macromolecular crowders." Physical Chemistry Chemical Physics 17, no. 30 (2015): 19820–33. http://dx.doi.org/10.1039/c5cp02674a.
Повний текст джерелаZhang, Chen, Fang Li, Si-Xi Wang, Zhao-Sheng Liu, and Haji Akber Aisa. "Molecularly imprinted polymers prepared using a porogenic solvent of an ionic liquid and a macromolecular crowding agent and their application in purification of oleanic acid." Analytical Methods 7, no. 24 (2015): 10256–65. http://dx.doi.org/10.1039/c5ay01960e.
Повний текст джерелаKoch, Leon, Roland Pollak, Simon Ebbinghaus, and Klaus Huber. "A Comparative Study on Cyanine Dyestuffs as Sensor Candidates for Macromolecular Crowding In Vitro and In Vivo." Biosensors 13, no. 7 (July 8, 2023): 720. http://dx.doi.org/10.3390/bios13070720.
Повний текст джерелаChristopoulou, Natalia-Maria, Despina P. Kalogianni, and Theodore K. Christopoulos. "Macromolecular crowding agents enhance the sensitivity of lateral flow immunoassays." Biosensors and Bioelectronics 218 (December 2022): 114737. http://dx.doi.org/10.1016/j.bios.2022.114737.
Повний текст джерелаRosin, Christopher, Paul Hendrik Schummel, and Roland Winter. "Cosolvent and crowding effects on the polymerization kinetics of actin." Physical Chemistry Chemical Physics 17, no. 13 (2015): 8330–37. http://dx.doi.org/10.1039/c4cp04431b.
Повний текст джерелаLin, Szu-Ning, Gijs J. L. Wuite, and Remus T. Dame. "Effect of Different Crowding Agents on the Architectural Properties of the Bacterial Nucleoid-Associated Protein HU." International Journal of Molecular Sciences 21, no. 24 (December 15, 2020): 9553. http://dx.doi.org/10.3390/ijms21249553.
Повний текст джерелаSu, Wan-Chih, Douglas L. Gettel, Morgan Chabanon, Padmini Rangamani, and Atul N. Parikh. "Pulsatile Gating of Giant Vesicles Containing Macromolecular Crowding Agents Induced by Colligative Nonideality." Journal of the American Chemical Society 140, no. 2 (January 5, 2018): 691–99. http://dx.doi.org/10.1021/jacs.7b10192.
Повний текст джерелаChristiansen, Alexander, Qian Wang, Margaret S. Cheung, and Pernilla Wittung-Stafshede. "Effects of macromolecular crowding agents on protein folding in vitro and in silico." Biophysical Reviews 5, no. 2 (February 19, 2013): 137–45. http://dx.doi.org/10.1007/s12551-013-0108-0.
Повний текст джерелаRowe, Ian, Andriy Anishkin, Kishore Kamaraju, Kenjiro Yoshimura, and Sergei Sukharev. "The cytoplasmic cage domain of the mechanosensitive channel MscS is a sensor of macromolecular crowding." Journal of General Physiology 143, no. 5 (April 28, 2014): 543–57. http://dx.doi.org/10.1085/jgp.201311114.
Повний текст джерелаMukherjee, Sanjib K., Saurabh Gautam, Saikat Biswas, Jayanta Kundu, and Pramit K. Chowdhury. "Do Macromolecular Crowding Agents Exert Only an Excluded Volume Effect? A Protein Solvation Study." Journal of Physical Chemistry B 119, no. 44 (October 23, 2015): 14145–56. http://dx.doi.org/10.1021/acs.jpcb.5b09446.
Повний текст джерелаDey, Pinki, and Arnab Bhattacherjee. "Disparity in anomalous diffusion of proteins searching for their target DNA sites in a crowded medium is controlled by the size, shape and mobility of macromolecular crowders." Soft Matter 15, no. 9 (2019): 1960–69. http://dx.doi.org/10.1039/c8sm01933a.
Повний текст джерелаFerreira, L. A., V. N. Uversky, and B. Y. Zaslavsky. "Role of solvent properties of water in crowding effects induced by macromolecular agents and osmolytes." Molecular BioSystems 13, no. 12 (2017): 2551–63. http://dx.doi.org/10.1039/c7mb00436b.
Повний текст джерелаShahid, Sumra, Faizan Ahmad, Md Imtaiyaz Hassan, and Asimul Islam. "Mixture of Macromolecular Crowding Agents Has a Non-additive Effect on the Stability of Proteins." Applied Biochemistry and Biotechnology 188, no. 4 (February 9, 2019): 927–41. http://dx.doi.org/10.1007/s12010-019-02972-9.
Повний текст джерелаPaudel, Bishnu P., Erica Fiorini, Richard Börner, Roland K. O. Sigel, and David S. Rueda. "Optimal molecular crowding accelerates group II intron folding and maximizes catalysis." Proceedings of the National Academy of Sciences 115, no. 47 (November 5, 2018): 11917–22. http://dx.doi.org/10.1073/pnas.1806685115.
Повний текст джерелаRusinga, Farai I., and David D. Weis. "Automated Strong Cation-Exchange Cleanup To Remove Macromolecular Crowding Agents for Protein Hydrogen Exchange Mass Spectrometry." Analytical Chemistry 89, no. 2 (December 23, 2016): 1275–82. http://dx.doi.org/10.1021/acs.analchem.6b04057.
Повний текст джерелаLi, Quan-Fu, Yan-Mei Zhan, Yong-Gang Zhong, Bo Zhang, and Chang-Qing Ge. "Macromolecular Crowding Agents-Assisted Imprinted Polymers For Analysis Of Glycocholic Acid In Human Plasma And Urine." Biomedical Chromatography 30, no. 11 (May 20, 2016): 1706–13. http://dx.doi.org/10.1002/bmc.3737.
Повний текст джерелаShahid, Sumra, Ikramul Hasan, Faizan Ahmad, Md Imtaiyaz Hassan, and Asimul Islam. "Carbohydrate-Based Macromolecular Crowding-Induced Stabilization of Proteins: Towards Understanding the Significance of the Size of the Crowder." Biomolecules 9, no. 9 (September 12, 2019): 477. http://dx.doi.org/10.3390/biom9090477.
Повний текст джерелаAumiller, William M., Bradley W. Davis, Emmanuel Hatzakis, and Christine D. Keating. "Interactions of Macromolecular Crowding Agents and Cosolutes with Small-Molecule Substrates: Effect on Horseradish Peroxidase Activity with Two Different Substrates." Journal of Physical Chemistry B 118, no. 36 (August 26, 2014): 10624–32. http://dx.doi.org/10.1021/jp506594f.
Повний текст джерелаAmzallag, Emmanuel, and Eran Hornstein. "Crosstalk between Biomolecular Condensates and Proteostasis." Cells 11, no. 15 (August 4, 2022): 2415. http://dx.doi.org/10.3390/cells11152415.
Повний текст джерелаCaterino, Tamara L., and Jeffrey J. Hayes. "Structure of the H1 C-terminal domain and function in chromatin condensationThis paper is one of a selection of papers published in a Special Issue entitled 31st Annual International Asilomar Chromatin and Chromosomes Conference, and has undergone the Journal’s usual peer review process." Biochemistry and Cell Biology 89, no. 1 (February 2011): 35–44. http://dx.doi.org/10.1139/o10-024.
Повний текст джерелаChang, Jui-Yoa, Bao-Yun Lu, and Por-Hsiung Lai. "Oxidative folding of hirudin in human serum." Biochemical Journal 394, no. 1 (January 27, 2006): 249–57. http://dx.doi.org/10.1042/bj20051660.
Повний текст джерелаShahid, Sumra, Faizan Ahmad, Md Imtaiyaz Hassan, and Asimul Islam. "Relationship between protein stability and functional activity in the presence of macromolecular crowding agents alone and in mixture: An insight into stability-activity trade-off." Archives of Biochemistry and Biophysics 584 (October 2015): 42–50. http://dx.doi.org/10.1016/j.abb.2015.08.015.
Повний текст джерелаVogel, Kristina, Thorsten Greinert, Monique Reichard, Christoph Held, Hauke Harms, and Thomas Maskow. "Thermodynamics and Kinetics of Glycolytic Reactions. Part II: Influence of Cytosolic Conditions on Thermodynamic State Variables and Kinetic Parameters." International Journal of Molecular Sciences 21, no. 21 (October 25, 2020): 7921. http://dx.doi.org/10.3390/ijms21217921.
Повний текст джерелаWerner, Tony E. R., Istvan Horvath, and Pernilla Wittung-Stafshede. "Response to crowded conditions reveals compact nucleus for amyloid formation of folded protein." QRB Discovery 2 (2021). http://dx.doi.org/10.1017/qrd.2020.17.
Повний текст джерелаOkamoto, Debora N., Lilian C. G. Oliveira, Marcia Y. Kondo, Maria H. S. Cezari, Zoltán Szeltner, Tünde Juhász, Maria A. Juliano, László Polgár, Luiz Juliano, and Iuri E. Gouvea. "Increase of SARS-CoV 3CL peptidase activity due to macromolecular crowding effects in the milieu composition." Biological Chemistry 391, no. 12 (December 1, 2010). http://dx.doi.org/10.1515/bc.2010.145.
Повний текст джерелаLecinski, Sarah, Jack W. Shepherd, Kate Bunting, Lara Dresser, Steven D. Quinn, Chris MacDonald, and Mark C. Leake. "Correlating viscosity and molecular crowding with fluorescent nanobeads and molecular probes: in vitro and in vivo." Interface Focus 12, no. 6 (October 14, 2022). http://dx.doi.org/10.1098/rsfs.2022.0042.
Повний текст джерелаLouisthelmy, Rebecca, Brycen M. Burke, and R. Chase Cornelison. "Brain cancer cell-derived matrices and effects on astrocyte migration." Cells Tissues Organs, February 15, 2022. http://dx.doi.org/10.1159/000522609.
Повний текст джерелаHagedoorn, Peter-Leon. "Isothermal Titration Calorimetry in Biocatalysis." Frontiers in Catalysis 2 (May 10, 2022). http://dx.doi.org/10.3389/fctls.2022.906668.
Повний текст джерелаSiraj, Seerat, Daraksha Yameen, Anas Shamsi, Faizya Khan, Asimul Islam, and Mohammad Mahfuzul Haque. "Interaction of Thioflavin T (ThT) and 8-anilino-1-naphthalene sulfonic acid (ANS) with macromolecular crowding agents and their monomers: Biophysical analysis using in vitro and computational approaches." Journal of Molecular Liquids, January 2023, 121270. http://dx.doi.org/10.1016/j.molliq.2023.121270.
Повний текст джерелаBonucci, Alessio, Martina Palomino-Schätzlein, Paula Malo de Molina, Arantxa Arbe, Roberta Pierattelli, Bruno Rizzuti, Juan L. Iovanna, and José L. Neira. "Crowding Effects on the Structure and Dynamics of the Intrinsically Disordered Nuclear Chromatin Protein NUPR1." Frontiers in Molecular Biosciences 8 (July 5, 2021). http://dx.doi.org/10.3389/fmolb.2021.684622.
Повний текст джерелаKöhn, Birgit, and Michael Kovermann. "All atom insights into the impact of crowded environments on protein stability by NMR spectroscopy." Nature Communications 11, no. 1 (November 13, 2020). http://dx.doi.org/10.1038/s41467-020-19616-w.
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