Artykuły w czasopismach na temat „Proteolysis”
Utwórz poprawne odniesienie w stylach APA, MLA, Chicago, Harvard i wielu innych
Sprawdź 50 najlepszych artykułów w czasopismach naukowych na temat „Proteolysis”.
Przycisk „Dodaj do bibliografii” jest dostępny obok każdej pracy w bibliografii. Użyj go – a my automatycznie utworzymy odniesienie bibliograficzne do wybranej pracy w stylu cytowania, którego potrzebujesz: APA, MLA, Harvard, Chicago, Vancouver itp.
Możesz również pobrać pełny tekst publikacji naukowej w formacie „.pdf” i przeczytać adnotację do pracy online, jeśli odpowiednie parametry są dostępne w metadanych.
Przeglądaj artykuły w czasopismach z różnych dziedzin i twórz odpowiednie bibliografie.
Navegantes, Luiz Carlos C., Neusa M. Z. Resano, Renato H. Migliorini i Isis C. Kettelhut. "Effect of guanethidine-induced adrenergic blockade on the different proteolytic systems in rat skeletal muscle". American Journal of Physiology-Endocrinology and Metabolism 277, nr 5 (1.11.1999): E883—E889. http://dx.doi.org/10.1152/ajpendo.1999.277.5.e883.
Pełny tekst źródłaNavegantes, Luiz Carlos C., Neusa M. Z. Resano, Renato H. Migliorini i Ísis C. Kettelhut. "Catecholamines inhibit Ca2+-dependent proteolysis in rat skeletal muscle through β2-adrenoceptors and cAMP". American Journal of Physiology-Endocrinology and Metabolism 281, nr 3 (1.09.2001): E449—E454. http://dx.doi.org/10.1152/ajpendo.2001.281.3.e449.
Pełny tekst źródłaLARBAUD, Daniel, Michèle BALAGE, Daniel TAILLANDIER, Lydie COMBARET, Jean GRIZARD i Didier ATTAIX. "Differential regulation of the lysosomal, Ca2+-dependent and ubiquitin/proteasome-dependent proteolytic pathways in fast-twitch and slow-twitch rat muscle following hyperinsulinaemia". Clinical Science 101, nr 6 (26.10.2001): 551–58. http://dx.doi.org/10.1042/cs1010551.
Pełny tekst źródłaKominami, Yuri, Tatsuya Hayashi, Tetsuji Tokihiro i Hideki Ushio. "A Novel Analysis of the Peptide Terminome Characterizes Dynamics of Proteolytic Regulation in Vertebrate Skeletal Muscle Under Severe Stress". Proteomes 7, nr 1 (13.02.2019): 6. http://dx.doi.org/10.3390/proteomes7010006.
Pełny tekst źródłaPortbury, Andrea L., Monte S. Willis i Cam Patterson. "Tearin' Up My Heart: Proteolysis in the Cardiac Sarcomere". Journal of Biological Chemistry 286, nr 12 (21.01.2011): 9929–34. http://dx.doi.org/10.1074/jbc.r110.170571.
Pełny tekst źródłaSun, Z., W. Carpiaux, D. Fan, Y. Fan, R. Lakshminarayanan i J. Moradian-Oldak. "Apatite Reduces Amelogenin Proteolysis by MMP-20 and KLK4 in vitro". Journal of Dental Research 89, nr 4 (16.02.2010): 344–48. http://dx.doi.org/10.1177/0022034509360660.
Pełny tekst źródłaPicard, Catherine, Isabelle Plard, Dominique Rongdaux-Gaida i Jean-Claude Collin. "Detection of proteolysis in raw milk stored at low temperature by an inhibition ELISA". Journal of Dairy Research 61, nr 3 (sierpień 1994): 395–404. http://dx.doi.org/10.1017/s0022029900030818.
Pełny tekst źródłaSolioz, M. "Role of proteolysis in copper homoeostasis". Biochemical Society Transactions 30, nr 4 (1.08.2002): 688–91. http://dx.doi.org/10.1042/bst0300688.
Pełny tekst źródłaShang, F., i A. Taylor. "Oxidative stress and recovery from oxidative stress are associated with altered ubiquitin conjugating and proteolytic activities in bovine lens epithelial cells". Biochemical Journal 307, nr 1 (1.04.1995): 297–303. http://dx.doi.org/10.1042/bj3070297.
Pełny tekst źródłaMitch, William E., James L. Bailey, Xiaonan Wang, Claudine Jurkovitz, David Newby i S. Russ Price. "Evaluation of signals activating ubiquitin-proteasome proteolysis in a model of muscle wasting". American Journal of Physiology-Cell Physiology 276, nr 5 (1.05.1999): C1132—C1138. http://dx.doi.org/10.1152/ajpcell.1999.276.5.c1132.
Pełny tekst źródłaFranch, Harold A., Xiaonan Wang, Sira Sooparb, Nikia S. Brown i Jie Du. "Phosphatidylinositol 3-Kinase Activity Is Required for Epidermal Growth Factor to Suppress Proteolysis". Journal of the American Society of Nephrology 13, nr 4 (kwiecień 2002): 903–9. http://dx.doi.org/10.1681/asn.v134903.
Pełny tekst źródłaLockwood, Thomas D. "Redox-dependent and redox-independent subcomponents of protein degradation in perfused myocardium". American Journal of Physiology-Endocrinology and Metabolism 276, nr 5 (1.05.1999): E945—E954. http://dx.doi.org/10.1152/ajpendo.1999.276.5.e945.
Pełny tekst źródłaChristensen, M., P. Henckel i P. P. Purslow. "Postmortem proteolysis in pork does not depend on fibre type distribution". Proceedings of the British Society of Animal Science 2001 (2001): 79. http://dx.doi.org/10.1017/s1752756200004610.
Pełny tekst źródłaManfredi, L. H., D. Lustrino, J. Machado, W. A. Silveira, N. M. Zanon, L. C. Navegantes i I. C. Kettelhut. "Adrenodemedullation activates the Ca2+-dependent proteolysis in soleus muscles from rats exposed to cold". Journal of Applied Physiology 122, nr 2 (1.02.2017): 317–26. http://dx.doi.org/10.1152/japplphysiol.00198.2016.
Pełny tekst źródłaArtemyeva, K. A., E. I. Goufman, I. I. Stepanova, N. B. Tikhonova, M. N. Boltovskaya, E. A. Ponomarenko, I. M. Bogdanova, M. V. Mnikhovich i L. M. Mikhaleva. "The level of IgG proteolytic fragments as an additional prognostic biomarker of prostate cancer". CLINICAL AND EXPERIMENTAL MORPHOLOGY 11, nr 2 (2022): 22–31. http://dx.doi.org/10.31088/cem2022.11.2.22-31.
Pełny tekst źródłaZamir, Oded, Per-Olof Hasselgren, Takashi Higashiguchi, Janice A. Frederick i Josef E. Fischer. "Tumour necrosis factor (TNF) and interleukin-1 (IL-1) induce muscle proteolysis through different mechanisms". Mediators of Inflammation 1, nr 4 (1992): 247–50. http://dx.doi.org/10.1155/s0962935192000371.
Pełny tekst źródłaMoazed, Bita, i M. Desautels. "Control of proteolysis by norepinephrine and insulin in brown adipocytes: role of ATP, phosphatidylinositol 3-kinase, and p70 S6K". Canadian Journal of Physiology and Pharmacology 80, nr 6 (1.06.2002): 541–52. http://dx.doi.org/10.1139/y02-078.
Pełny tekst źródłaFagan, J. M., i A. L. Goldberg. "The rate of protein degradation in isolated skeletal muscle does not correlate with reduction-oxidation status". Biochemical Journal 227, nr 3 (1.05.1985): 689–94. http://dx.doi.org/10.1042/bj2270689.
Pełny tekst źródłaTAILLANDIER, Daniel, Eveline AUROUSSEAU, Dominique MEYNIAL-DENIS, Daniel BECHET, Marc FERRARA, Patrick COTTIN, André DUCASTAING i in. "Coordinate activation of lysosomal, Ca2+-activated and ATP-ubiquitin-dependent proteinases in the unweighted rat soleus muscle". Biochemical Journal 316, nr 1 (15.05.1996): 65–72. http://dx.doi.org/10.1042/bj3160065.
Pełny tekst źródłaBarrett, E. J., L. A. Jahn, D. M. Oliveras i D. A. Fryburg. "Chloroquine does not exert insulin-like actions on human forearm muscle metabolism". American Journal of Physiology-Endocrinology and Metabolism 268, nr 5 (1.05.1995): E820—E824. http://dx.doi.org/10.1152/ajpendo.1995.268.5.e820.
Pełny tekst źródłaMahmoud, Samar A., i Peter Chien. "Regulated Proteolysis in Bacteria". Annual Review of Biochemistry 87, nr 1 (20.06.2018): 677–96. http://dx.doi.org/10.1146/annurev-biochem-062917-012848.
Pełny tekst źródłaMañas-García, Laura, Charlotte Denhard, Javier Mateu, Xavier Duran, Joaquim Gea i Esther Barreiro. "Beneficial Effects of Resveratrol in Mouse Gastrocnemius: A Hint to Muscle Phenotype and Proteolysis". Cells 10, nr 9 (15.09.2021): 2436. http://dx.doi.org/10.3390/cells10092436.
Pełny tekst źródłavan de Winkel, J. G., R. van Ommen, T. W. Huizinga, M. A. de Raad, W. B. Tuijnman, P. J. Groenen, P. J. Capel, R. A. Koene i W. J. Tax. "Proteolysis induces increased binding affinity of the monocyte type II FcR for human IgG." Journal of Immunology 143, nr 2 (15.07.1989): 571–78. http://dx.doi.org/10.4049/jimmunol.143.2.571.
Pełny tekst źródłaMyagkonosov, D. S., I. T. Smykov, D. V. Abramov i I. N. Delitskaya. "Influence of different types of fermentation-produced chymosin on quality of soft cheeses". IOP Conference Series: Earth and Environmental Science 1052, nr 1 (1.07.2022): 012076. http://dx.doi.org/10.1088/1755-1315/1052/1/012076.
Pełny tekst źródłaTOURNU, Cécile, Alain OBLED, Marie-Paule ROUX, Marc FERRARA, Satoshi OMURA i Daniel M. BÉCHET. "Glucose regulates protein catabolism in ras-transformed fibroblasts through a lysosomal-dependent proteolytic pathway". Biochemical Journal 357, nr 1 (25.06.2001): 255–61. http://dx.doi.org/10.1042/bj3570255.
Pełny tekst źródłaLavatelli, Francesca, Giulia Mazzini, Stefano Ricagno, Federica Iavarone, Paola Rognoni, Paolo Milani, Mario Nuvolone i in. "Mass spectrometry characterization of light chain fragmentation sites in cardiac AL amyloidosis: insights into the timing of proteolysis". Journal of Biological Chemistry 295, nr 49 (20.09.2020): 16572–84. http://dx.doi.org/10.1074/jbc.ra120.013461.
Pełny tekst źródłaHutton, D. A., J. P. Pearson, A. Allen i S. N. E. Foster. "Mucolysis of the colonic mucus barrier by faecal proteinases: Inhibition by interacting polyacrylate". Clinical Science 78, nr 3 (1.03.1990): 265–71. http://dx.doi.org/10.1042/cs0780265.
Pełny tekst źródłaEwald, S. J., i P. H. Refling. "Co-immunoprecipitation of the Ly-5 molecule and an endogenous protease: a proteolytic system requiring a reducing agent and Ca2+1." Journal of Immunology 134, nr 4 (1.04.1985): 2513–19. http://dx.doi.org/10.4049/jimmunol.134.4.2513.
Pełny tekst źródłaBaracos, V. E., C. DeVivo, D. H. Hoyle i A. L. Goldberg. "Activation of the ATP-ubiquitin-proteasome pathway in skeletal muscle of cachectic rats bearing a hepatoma". American Journal of Physiology-Endocrinology and Metabolism 268, nr 5 (1.05.1995): E996—E1006. http://dx.doi.org/10.1152/ajpendo.1995.268.5.e996.
Pełny tekst źródłaBaracos, V., R. E. Greenberg i A. L. Goldberg. "Influence of calcium and other divalent cations on protein turnover in rat skeletal muscle". American Journal of Physiology-Endocrinology and Metabolism 250, nr 6 (1.06.1986): E702—E710. http://dx.doi.org/10.1152/ajpendo.1986.250.6.e702.
Pełny tekst źródłaMaupin-Furlow, Julie A. "Proteolytic systems of archaea: slicing, dicing, and mincing in the extreme". Emerging Topics in Life Sciences 2, nr 4 (14.11.2018): 561–80. http://dx.doi.org/10.1042/etls20180025.
Pełny tekst źródłaRivera, G. M., i J. E. Fortune. "Selection of the Dominant Follicle and Insulin-Like Growth Factor (IGF)-Binding Proteins: Evidence that Pregnancy-Associated Plasma Protein A Contributes to Proteolysis of IGF-Binding Protein 5 in Bovine Follicular Fluid". Endocrinology 144, nr 2 (1.02.2003): 437–46. http://dx.doi.org/10.1210/en.2002-220657.
Pełny tekst źródłaSIVANANDAM, Arun S., Subburaman MOHAN, Hirohito KITA, Sanjay KAPUR, Shin-Tai CHEN, Thomas A. LINKHART, Gyorgy BAGI, David J. BAYLINK i Xuezhong QIN. "Studies on regulation of IGF (insulin-like growth factor)-binding protein (IGFBP) 4 proteolysis by pregnancy-associated plasma protein-A (PAPP-A) in cells treated with phorbol ester". Biochemical Journal 379, nr 1 (1.04.2004): 57–64. http://dx.doi.org/10.1042/bj20030937.
Pełny tekst źródłaScolari, G., M. Vescovo, P. G. Sarra i V. Bottazzi. "Proteolysis in cheese made with liposome-entrapped proteolytic enzymes". Le Lait 73, nr 3 (1993): 281–92. http://dx.doi.org/10.1051/lait:1993326.
Pełny tekst źródłaKudryashova, I. V. "Proteolysis and proteolytic enzymes in structural plasticity of synapses". Neurochemical Journal 3, nr 3 (wrzesień 2009): 164–72. http://dx.doi.org/10.1134/s1819712409030027.
Pełny tekst źródłaGermain, D., J. Hendley i B. Futcher. "DNA damage inhibits proteolysis of the B-type cyclin Clb5 in S. cerevisiae". Journal of Cell Science 110, nr 15 (1.08.1997): 1813–20. http://dx.doi.org/10.1242/jcs.110.15.1813.
Pełny tekst źródłaFontana, Angelo, Patrizia Polverino De Laureto, Barbara Spolaore, Erica Frare, Paola Picotti i Marcello Zambonin. "Probing protein structure by limited proteolysis." Acta Biochimica Polonica 51, nr 2 (30.06.2004): 299–321. http://dx.doi.org/10.18388/abp.2004_3573.
Pełny tekst źródłaTawa, N. E., I. C. Kettelhut i A. L. Goldberg. "Dietary protein deficiency reduces lysosomal and nonlysosomal ATP-dependent proteolysis in muscle". American Journal of Physiology-Endocrinology and Metabolism 263, nr 2 (1.08.1992): E326—E334. http://dx.doi.org/10.1152/ajpendo.1992.263.2.e326.
Pełny tekst źródłaLi, Anguo, i Tze-Chein Wun. "Proteolysis of Tissue Factor Pathway Inhibitor (TFPI) by Plasmin: Effect on TFPI Activity". Thrombosis and Haemostasis 80, nr 09 (1998): 423–27. http://dx.doi.org/10.1055/s-0037-1615224.
Pełny tekst źródłaCortesio, Christa L., Lindsy R. Boateng, Timothy M. Piazza, David A. Bennin i Anna Huttenlocher. "Calpain-mediated Proteolysis of Paxillin Negatively Regulates Focal Adhesion Dynamics and Cell Migration". Journal of Biological Chemistry 286, nr 12 (26.01.2011): 9998–10006. http://dx.doi.org/10.1074/jbc.m110.187294.
Pełny tekst źródłaMosoni, L., T. Malmezat, M. C. Valluy, M. L. Houlier, D. Attaix i P. Patureau Mirand. "Lower recovery of muscle protein lost during starvation in old rats despite a stimulation of protein synthesis". American Journal of Physiology-Endocrinology and Metabolism 277, nr 4 (1.10.1999): E608—E616. http://dx.doi.org/10.1152/ajpendo.1999.277.4.e608.
Pełny tekst źródłaReboul, A., J. Arvieux, J. F. Wright i M. G. Colomb. "Proteolytic fragmentation of tetanus toxin by subcellular fractions of JY, a B lymphoblastoid cell line". Biochemical Journal 277, nr 1 (1.07.1991): 47–51. http://dx.doi.org/10.1042/bj2770047.
Pełny tekst źródłaKatrukha, Aleksei G., Anastasia V. Bereznikova, Vladimir L. Filatov, Tatiana V. Esakova, Olga V. Kolosova, Kim Pettersson, Timo Lövgren i in. "Degradation of cardiac troponin I: implication for reliable immunodetection". Clinical Chemistry 44, nr 12 (1.12.1998): 2433–40. http://dx.doi.org/10.1093/clinchem/44.12.2433.
Pełny tekst źródłaMañas-García, Laura, Nuria Bargalló, Joaquim Gea i Esther Barreiro. "Muscle Phenotype, Proteolysis, and Atrophy Signaling During Reloading in Mice: Effects of Curcumin on the Gastrocnemius". Nutrients 12, nr 2 (31.01.2020): 388. http://dx.doi.org/10.3390/nu12020388.
Pełny tekst źródłaMintoo, Mubashir, Amritangshu Chakravarty i Ronak Tilvawala. "N-Terminomics Strategies for Protease Substrates Profiling". Molecules 26, nr 15 (3.08.2021): 4699. http://dx.doi.org/10.3390/molecules26154699.
Pełny tekst źródłaGraef, Martin, Georgeta Seewald i Thomas Langer. "Substrate Recognition by AAA+ ATPases: Distinct Substrate Binding Modes in ATP-Dependent Protease Yme1 of the Mitochondrial Intermembrane Space". Molecular and Cellular Biology 27, nr 7 (29.01.2007): 2476–85. http://dx.doi.org/10.1128/mcb.01721-06.
Pełny tekst źródłaVoelkel-Johnson, C., A. J. Entingh, W. S. Wold, L. R. Gooding i S. M. Laster. "Activation of intracellular proteases is an early event in TNF-induced apoptosis." Journal of Immunology 154, nr 4 (15.02.1995): 1707–16. http://dx.doi.org/10.4049/jimmunol.154.4.1707.
Pełny tekst źródłaChang, Hao, Philip M. Smallwood, John Williams i Jeremy Nathans. "Intramembrane Proteolysis of Astrotactins". Journal of Biological Chemistry 292, nr 8 (18.01.2017): 3506–16. http://dx.doi.org/10.1074/jbc.m116.768077.
Pełny tekst źródłaWard, Donald E., Keith R. Shockley, Lara S. Chang, Ryan D. Levy, Joshua K. Michel, Shannon B. Conners i Robert M. Kelly. "Proteolysis in hyperthermophilic microorganisms". Archaea 1, nr 1 (2002): 63–74. http://dx.doi.org/10.1155/2002/503191.
Pełny tekst źródłaDebigaré, Richard, i S. Russ Price. "Proteolysis, the ubiquitin-proteasome system, and renal diseases". American Journal of Physiology-Renal Physiology 285, nr 1 (lipiec 2003): F1—F8. http://dx.doi.org/10.1152/ajprenal.00244.2002.
Pełny tekst źródła