Статті в журналах з теми "Proteolytic assemblies"
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Ознайомтеся з топ-50 статей у журналах для дослідження на тему "Proteolytic assemblies".
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Walz, J., A. J. Koster, T. Tamura, and W. Baumeister. "Macromolecular Assemblies Designed for Controlled Proteolysis." Microscopy and Microanalysis 4, S2 (July 1998): 980–81. http://dx.doi.org/10.1017/s1431927600025022.
Повний текст джерелаKoppen, Mirko, Metodi D. Metodiev, Giorgio Casari, Elena I. Rugarli, and Thomas Langer. "Variable and Tissue-Specific Subunit Composition of Mitochondrial m-AAA Protease Complexes Linked to Hereditary Spastic Paraplegia." Molecular and Cellular Biology 27, no. 2 (November 13, 2006): 758–67. http://dx.doi.org/10.1128/mcb.01470-06.
Повний текст джерелаAweida, Dina, and Shenhav Cohen. "Breakdown of Filamentous Myofibrils by the UPS–Step by Step." Biomolecules 11, no. 1 (January 15, 2021): 110. http://dx.doi.org/10.3390/biom11010110.
Повний текст джерелаYang, Dongsik, Hongjian He, and Bing Xu. "Enzyme-instructed morphological transition of the supramolecular assemblies of branched peptides." Beilstein Journal of Organic Chemistry 16 (November 4, 2020): 2709–18. http://dx.doi.org/10.3762/bjoc.16.221.
Повний текст джерелаOláh, Judit, Attila Lehotzky, Tibor Szénási, and Judit Ovádi. "Anti-Aggregative Effect of the Antioxidant DJ-1 on the TPPP/p25-Derived Pathological Associations of Alpha-Synuclein." Cells 10, no. 11 (October 27, 2021): 2909. http://dx.doi.org/10.3390/cells10112909.
Повний текст джерелаUskoković, V., M.-K. Kim, W. Li, and S. Habelitz. "Enzymatic processing of amelogenin during continuous crystallization of apatite." Journal of Materials Research 23, no. 12 (December 2008): 3184–95. http://dx.doi.org/10.1557/jmr.2008.0387.
Повний текст джерелаYang, Jin-Kyoung, Seon-Yeong Kwak, Su-Ji Jeon, Eunjin Lee, Jong-Min Ju, Hye-In Kim, Yoon-Sik Lee, and Jong-Ho Kim. "Proteolytic disassembly of peptide-mediated graphene oxide assemblies for turn-on fluorescence sensing of proteases." Nanoscale 8, no. 24 (2016): 12272–81. http://dx.doi.org/10.1039/c6nr02815b.
Повний текст джерелаErk, Inge, Jean-Claude Huet, Mariela Duarte, Stéphane Duquerroy, Felix Rey, Jean Cohen, and Jean Lepault. "A Zinc Ion Controls Assembly and Stability of the Major Capsid Protein of Rotavirus." Journal of Virology 77, no. 6 (March 15, 2003): 3595–601. http://dx.doi.org/10.1128/jvi.77.6.3595-3601.2003.
Повний текст джерелаHarkness, Robert W., Yuki Toyama, Zev A. Ripstein, Huaying Zhao, Alexander I. M. Sever, Qing Luan, Jacob P. Brady, Patricia L. Clark, Peter Schuck, and Lewis E. Kay. "Competing stress-dependent oligomerization pathways regulate self-assembly of the periplasmic protease-chaperone DegP." Proceedings of the National Academy of Sciences 118, no. 32 (August 6, 2021): e2109732118. http://dx.doi.org/10.1073/pnas.2109732118.
Повний текст джерелаTamara, Sem, Vojtech Franc, and Albert J. R. Heck. "A wealth of genotype-specific proteoforms fine-tunes hemoglobin scavenging by haptoglobin." Proceedings of the National Academy of Sciences 117, no. 27 (June 19, 2020): 15554–64. http://dx.doi.org/10.1073/pnas.2002483117.
Повний текст джерелаOsman, Christof, Claudia Wilmes, Takashi Tatsuta, and Thomas Langer. "Prohibitins Interact Genetically with Atp23, a Novel Processing Peptidase and Chaperone for the F1FO-ATP Synthase." Molecular Biology of the Cell 18, no. 2 (February 2007): 627–35. http://dx.doi.org/10.1091/mbc.e06-09-0839.
Повний текст джерелаEhses, Sarah, Ines Raschke, Giuseppe Mancuso, Andrea Bernacchia, Stefan Geimer, Daniel Tondera, Jean-Claude Martinou, Benedikt Westermann, Elena I. Rugarli, and Thomas Langer. "Regulation of OPA1 processing and mitochondrial fusion by m-AAA protease isoenzymes and OMA1." Journal of Cell Biology 187, no. 7 (December 28, 2009): 1023–36. http://dx.doi.org/10.1083/jcb.200906084.
Повний текст джерелаGres, Anna, Karen Kirby, Atsuko Hachiya, Eleftherios Michailidis, Owen Pornillos, Wataru Sugiura, KyeongEun Lee, Vineet KewalRamani, John Tanner, and Stefan Sarafianos. "Native Hexameric Full-Length HIV-1 Capsid: Crystal Structure and Drug Targeting." Acta Crystallographica Section A Foundations and Advances 70, a1 (August 5, 2014): C696. http://dx.doi.org/10.1107/s2053273314093036.
Повний текст джерелаBaier, Kerstin, Heike Lehmann, Dirk Paul Stephan, and Wolfgang Lockau. "NblA is essential for phycobilisome degradation in Anabaena sp. strain PCC 7120 but not for development of functional heterocysts." Microbiology 150, no. 8 (August 1, 2004): 2739–49. http://dx.doi.org/10.1099/mic.0.27153-0.
Повний текст джерелаYewdell, J., C. Lapham, I. Bacik, T. Spies, and J. Bennink. "MHC-encoded proteasome subunits LMP2 and LMP7 are not required for efficient antigen presentation." Journal of Immunology 152, no. 3 (February 1, 1994): 1163–70. http://dx.doi.org/10.4049/jimmunol.152.3.1163.
Повний текст джерелаSchur, Florian K. M., Robert A. Dick, Wim J. H. Hagen, Volker M. Vogt, and John A. G. Briggs. "The Structure of Immature Virus-Like Rous Sarcoma Virus Gag Particles Reveals a Structural Role for the p10 Domain in Assembly." Journal of Virology 89, no. 20 (July 29, 2015): 10294–302. http://dx.doi.org/10.1128/jvi.01502-15.
Повний текст джерелаYuan, Dan, Xuewen Du, Junfeng Shi, Ning Zhou, Abdulgader Ahmed Baoum, Khalid Omar Al Footy, Khadija Omar Badahdah, and Bing Xu. "Synthesis and evaluation of the biostability and cell compatibility of novel conjugates of nucleobase, peptidic epitope, and saccharide." Beilstein Journal of Organic Chemistry 11 (August 3, 2015): 1352–59. http://dx.doi.org/10.3762/bjoc.11.145.
Повний текст джерелаWainwright, S. Mark, Ben R. Hopkins, Cláudia C. Mendes, Aashika Sekar, Benjamin Kroeger, Josephine E. E. U. Hellberg, Shih-Jung Fan, et al. "Drosophila Sex Peptide controls the assembly of lipid microcarriers in seminal fluid." Proceedings of the National Academy of Sciences 118, no. 5 (January 25, 2021): e2019622118. http://dx.doi.org/10.1073/pnas.2019622118.
Повний текст джерелаBuhimschi, Irina A., Unzila A. Nayeri, Guomao Zhao, Lydia L. Shook, Anna Pensalfini, Edmund F. Funai, Ira M. Bernstein, Charles G. Glabe, and Catalin S. Buhimschi. "Protein misfolding, congophilia, oligomerization, and defective amyloid processing in preeclampsia." Science Translational Medicine 6, no. 245 (July 16, 2014): 245ra92. http://dx.doi.org/10.1126/scitranslmed.3008808.
Повний текст джерелаde Sousa, J. P., R. G. Carvalho, L. F. Barbosa-Martins, R. J. S. Torquato, K. C. U. Mugnol, F. D. Nascimento, I. L. S. Tersariol, and R. M. Puppin-Rontani. "The Self-Assembling Peptide P11-4 Prevents Collagen Proteolysis in Dentin." Journal of Dental Research 98, no. 3 (January 5, 2019): 347–54. http://dx.doi.org/10.1177/0022034518817351.
Повний текст джерелаClapp, Aaron R., Ellen R. Goldman, H. Tetsuo Uyeda, Eddie L. Chang, Jessica L. Whitley, and Igor L. Medintz. "Monitoring of Enzymatic Proteolysis Using Self-Assembled Quantum Dot-Protein Substrate Sensors." Journal of Sensors 2008 (2008): 1–10. http://dx.doi.org/10.1155/2008/797436.
Повний текст джерелаDU, Jinping, Barbara H. KNOWLES, Jade LI, and David J. ELLAR. "Biochemical characterization of Bacillus thuringiensis cytolytic toxins in association with a phospholipid bilayer." Biochemical Journal 338, no. 1 (February 8, 1999): 185–93. http://dx.doi.org/10.1042/bj3380185.
Повний текст джерелаWoodward, Cora L., Sarah N. Cheng, and Grant J. Jensen. "Electron Cryotomography Studies of Maturing HIV-1 Particles Reveal the Assembly Pathway of the Viral Core." Journal of Virology 89, no. 2 (November 12, 2014): 1267–77. http://dx.doi.org/10.1128/jvi.02997-14.
Повний текст джерелаWileman, T., LP Kane, J. Young, GR Carson, and C. Terhorst. "Associations between subunit ectodomains promote T cell antigen receptor assembly and protect against degradation in the ER." Journal of Cell Biology 122, no. 1 (July 1, 1993): 67–78. http://dx.doi.org/10.1083/jcb.122.1.67.
Повний текст джерелаKnorpp, C., C. Szigyarto, and E. Glaser. "Evidence for a novel ATP-dependent membrane-associated protease in spinach leaf mitochondria." Biochemical Journal 310, no. 2 (September 1, 1995): 527–31. http://dx.doi.org/10.1042/bj3100527.
Повний текст джерелаQu, Kun, Bärbel Glass, Michal Doležal, Florian K. M. Schur, Brice Murciano, Alan Rein, Michaela Rumlová, Tomáš Ruml, Hans-Georg Kräusslich, and John A. G. Briggs. "Structure and architecture of immature and mature murine leukemia virus capsids." Proceedings of the National Academy of Sciences 115, no. 50 (November 26, 2018): E11751—E11760. http://dx.doi.org/10.1073/pnas.1811580115.
Повний текст джерелаUskoković, Vuk. "Prospects and Pits on the Path of Biomimetics: The Case of Tooth Enamel." Journal of Biomimetics, Biomaterials and Tissue Engineering 8 (November 2010): 45–78. http://dx.doi.org/10.4028/www.scientific.net/jbbte.8.45.
Повний текст джерелаFerch, Uta, Bernhard Kloo, Andreas Gewies, Vera Pfaender, Michael Düwel, Christian Peschel, Daniel Krappmann, and Jürgen Ruland. "Inhibition of MALT1 Protease Activity Is Selectively Toxic for Activated B CellÃ,–Like Diffuse Large B Cell Lymphoma Cells." Blood 114, no. 22 (November 20, 2009): 1271. http://dx.doi.org/10.1182/blood.v114.22.1271.1271.
Повний текст джерелаNa, Mahesheema, Joesph R. Wiencek, Jamila Hirbawi, and Michael Kalafatis. "Cleavage At Arg1018 During Thrombin-Mediated Activation of Coagulation Factor V Is Dispensable." Blood 118, no. 21 (November 18, 2011): 1186. http://dx.doi.org/10.1182/blood.v118.21.1186.1186.
Повний текст джерелаSelvaraj, Bethilda Anne, Abdul Razak Mariatulqabtiah, Kok Lian Ho, Chyan Leong Ng, Chean Yeah Yong, and Wen Siang Tan. "Regulation of Proteolytic Activity to Improve the Recovery of Macrobrachium rosenbergii Nodavirus Capsid Protein." International Journal of Molecular Sciences 22, no. 16 (August 13, 2021): 8725. http://dx.doi.org/10.3390/ijms22168725.
Повний текст джерелаSerrano, L., F. Wandosell, J. de la Torre, and J. Avila. "Effect of specific proteolytic cleavages on tubulin polymer formation." Biochemical Journal 252, no. 3 (June 15, 1988): 683–91. http://dx.doi.org/10.1042/bj2520683.
Повний текст джерелаKelly, Jeffery W., and William E. Balch. "Amyloid as a natural product." Journal of Cell Biology 161, no. 3 (May 12, 2003): 461–62. http://dx.doi.org/10.1083/jcb.200304074.
Повний текст джерелаMitchell, E. J., and A. M. Zimmerman. "Biochemical evidence for the presence of an actin protein in Tetrahymena pyriformis." Journal of Cell Science 73, no. 1 (February 1, 1985): 279–97. http://dx.doi.org/10.1242/jcs.73.1.279.
Повний текст джерелаSaunders, Jared T., and Jean E. Schwarzbauer. "Fibronectin matrix as a scaffold for procollagen proteinase binding and collagen processing." Molecular Biology of the Cell 30, no. 17 (August 2019): 2218–26. http://dx.doi.org/10.1091/mbc.e19-03-0140.
Повний текст джерелаRodell, Christopher B., Ryan J. Wade, Brendan P. Purcell, Neville N. Dusaj, and Jason A. Burdick. "Selective Proteolytic Degradation of Guest–Host Assembled, Injectable Hyaluronic Acid Hydrogels." ACS Biomaterials Science & Engineering 1, no. 4 (March 9, 2015): 277–86. http://dx.doi.org/10.1021/ab5001673.
Повний текст джерелаKato, A., K. Yamamoto, S. Miyazaki, SM Jung, M. Moroi, and N. Aoki. "Molecular basis for Glanzmann's thrombasthenia (GT) in a compound heterozygote with glycoprotein IIb gene: a proposal for the classification of GT based on the biosynthetic pathway of glycoprotein IIb-IIIa complex." Blood 79, no. 12 (June 15, 1992): 3212–18. http://dx.doi.org/10.1182/blood.v79.12.3212.3212.
Повний текст джерелаKato, A., K. Yamamoto, S. Miyazaki, SM Jung, M. Moroi, and N. Aoki. "Molecular basis for Glanzmann's thrombasthenia (GT) in a compound heterozygote with glycoprotein IIb gene: a proposal for the classification of GT based on the biosynthetic pathway of glycoprotein IIb-IIIa complex." Blood 79, no. 12 (June 15, 1992): 3212–18. http://dx.doi.org/10.1182/blood.v79.12.3212.bloodjournal79123212.
Повний текст джерелаSwanekamp, Ria J., Jade J. Welch та Bradley L. Nilsson. "Proteolytic stability of amphipathic peptide hydrogels composed of self-assembled pleated β-sheet or coassembled rippled β-sheet fibrils". Chem. Commun. 50, № 70 (2014): 10133–36. http://dx.doi.org/10.1039/c4cc04644g.
Повний текст джерелаVilaça, H., G. Pereira, T. G. Castro, B. F. Hermenegildo, J. Shi, T. Q. Faria, N. Micaêlo, et al. "New self-assembled supramolecular hydrogels based on dehydropeptides." Journal of Materials Chemistry B 3, no. 30 (2015): 6355–67. http://dx.doi.org/10.1039/c5tb00501a.
Повний текст джерелаMu, C. Jenny, David A. LaVan, Robert S. Langer, and Bruce R. Zetter. "Self-Assembled Gold Nanoparticle Molecular Probes for Detecting Proteolytic Activity In Vivo." ACS Nano 4, no. 3 (February 10, 2010): 1511–20. http://dx.doi.org/10.1021/nn9017334.
Повний текст джерелаDodonova, Svetlana O., Simone Prinz, Virginia Bilanchone, Suzanne Sandmeyer, and John A. G. Briggs. "Structure of the Ty3/Gypsy retrotransposon capsid and the evolution of retroviruses." Proceedings of the National Academy of Sciences 116, no. 20 (April 29, 2019): 10048–57. http://dx.doi.org/10.1073/pnas.1900931116.
Повний текст джерелаZuber, Guy, Jason McDermott, Sonya Karanjia, Weiyi Zhao, Michael F. Schmid, and Eric Barklis. "Assembly of Retrovirus Capsid-Nucleocapsid Proteins in the Presence of Membranes or RNA." Journal of Virology 74, no. 16 (August 15, 2000): 7431–41. http://dx.doi.org/10.1128/jvi.74.16.7431-7441.2000.
Повний текст джерелаYu, I. M., H. A. Holdaway, P. R. Chipman, R. J. Kuhn, M. G. Rossmann, and J. Chen. "Association of the pr Peptides with Dengue Virus at Acidic pH Blocks Membrane Fusion." Journal of Virology 83, no. 23 (September 16, 2009): 12101–7. http://dx.doi.org/10.1128/jvi.01637-09.
Повний текст джерелаMurphy, Brona M., Amanda J. O'Neill, Colin Adrain, R. William G. Watson, and Seamus J. Martin. "The Apoptosome Pathway to Caspase Activation in Primary Human Neutrophils Exhibits Dramatically Reduced Requirements for Cytochrome c." Journal of Experimental Medicine 197, no. 5 (February 24, 2003): 625–32. http://dx.doi.org/10.1084/jem.20021862.
Повний текст джерелаvan Asch, Barbara, and Luís Filipe Teixeira da Costa. "Patterns and tempo of PCSK9 pseudogenizations suggest an ancient divergence in mammalian cholesterol homeostasis mechanisms." Genetica 149, no. 1 (January 30, 2021): 1–19. http://dx.doi.org/10.1007/s10709-021-00113-x.
Повний текст джерелаWickström, Claes, and Ingemar Carlstedt. "N-terminal Cleavage of the Salivary MUC5B Mucin." Journal of Biological Chemistry 276, no. 50 (October 15, 2001): 47116–21. http://dx.doi.org/10.1074/jbc.m106593200.
Повний текст джерелаRyu, Jungki, and Chan Beum Park. "High stability of self-assembled peptide nanowires against thermal, chemical, and proteolytic attacks." Biotechnology and Bioengineering 105, no. 2 (February 1, 2010): 221–30. http://dx.doi.org/10.1002/bit.22544.
Повний текст джерелаHall, M. R., and W. Gibson. "Independently cloned halves of cytomegalovirus assemblin, An and Ac, can restore proteolytic activity to assemblin mutants by intermolecular complementation." Journal of virology 71, no. 2 (1997): 956–64. http://dx.doi.org/10.1128/jvi.71.2.956-964.1997.
Повний текст джерелаGenové, Elsa, Nausika Betriu та Carlos E. Semino. "β-Sheet to Random Coil Transition in Self-Assembling Peptide Scaffolds Promotes Proteolytic Degradation". Biomolecules 12, № 3 (7 березня 2022): 411. http://dx.doi.org/10.3390/biom12030411.
Повний текст джерелаWu, Shenjie, Wenqi Song, Catherine C. L. Wong та Yigong Shi. "Bax inhibitor 1 is a γ-secretase–independent presenilin-binding protein". Proceedings of the National Academy of Sciences 116, № 1 (17 грудня 2018): 141–47. http://dx.doi.org/10.1073/pnas.1810870116.
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