Статті в журналах з теми "Protein turn-over"
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Knap, P. W., and J. W. Schrama. "Simulation of growth in pigs: approximation of protein turn-over parameters." Animal Science 63, no. 3 (December 1996): 533–47. http://dx.doi.org/10.1017/s1357729800015435.
Повний текст джерелаRoux, Z. "Incorporating turn-over in whole body protein retention ef.ciency in pigs." Animal Science 80, no. 1 (February 2005): 71–81. http://dx.doi.org/10.1079/asc40650071.
Повний текст джерелаKnap, P. W. "Stochastic simulation of growth in pigs: protein turn-over-dependent relations between body composition and maintenance requirements." Animal Science 63, no. 3 (December 1996): 549–61. http://dx.doi.org/10.1017/s1357729800015447.
Повний текст джерелаTesseraud, S., A. Besnard, R. Peresson, J. Michel, E. Le Bihan-Duval, and AM Chagneau. "Growth and muscle protein turn-over: effect of genotype and amino acids." Reproduction Nutrition Development 37, no. 3 (1997): 337–38. http://dx.doi.org/10.1051/rnd:19970320.
Повний текст джерелаRoux, C. Z. "Incorporating turn-over in whole body protein retention efficiency in cattle and sheep." Animal Science 80, no. 3 (June 2005): 345–51. http://dx.doi.org/10.1079/asc41610345.
Повний текст джерелаMuramatsu, T., Y. Ueda, T. Hirata, J. Okumura, and I. Tasaki. "A note on the effect of ageing on whole-body protein turn-over in goats." Animal Production 46, no. 3 (June 1988): 479–81. http://dx.doi.org/10.1017/s0003356100019097.
Повний текст джерелаDutra, S., F. Thuillier, D. Darmaun, B. Messing, M. Rongier, and J. F. Desjeux. "Protein turn-over assessed by leucine and glutamine fluxes in adult caeliac patients." Clinical Nutrition 11 (January 1992): 50. http://dx.doi.org/10.1016/0261-5614(92)90213-a.
Повний текст джерелаWhittemore, C. T., D. M. Green, and P. W. Knap. "Technical review of the energy and protein requirements of growing pigs: protein." Animal Science 73, no. 3 (December 2001): 363–73. http://dx.doi.org/10.1017/s1357729800058331.
Повний текст джерелаTyndall, Joel D. A., Bernhard Pfeiffer, Giovanni Abbenante, and David P. Fairlie. "Over One Hundred Peptide-Activated G Protein-Coupled Receptors Recognize Ligands with Turn Structure." Chemical Reviews 105, no. 3 (March 2005): 793–826. http://dx.doi.org/10.1021/cr040689g.
Повний текст джерелаBiermann, Esther, Martina Baack, Sandra Kreitz, and Rolf Knippers. "Synthesis and turn-over of the replicative Cdc6 protein during the HeLa cell cycle." European Journal of Biochemistry 269, no. 3 (February 1, 2002): 1040–46. http://dx.doi.org/10.1046/j.0014-2956.2001.02746.x.
Повний текст джерелаWhittemore, C. T., P. W. Knap, and D. M. Green. "Technical review of the energy and protein requirements of growing pigs: energy." Animal Science 73, no. 2 (October 2001): 199–215. http://dx.doi.org/10.1017/s1357729800058185.
Повний текст джерелаHuang, Anming, Leopold Kremser, Fabian Schuler, Doris Wilflingseder, Herbert Lindner, Stephan Geley, and Alexandra Lusser. "Phosphorylation of Drosophila CENP-A on serine 20 regulates protein turn-over and centromere-specific loading." Nucleic Acids Research 47, no. 20 (September 19, 2019): 10754–70. http://dx.doi.org/10.1093/nar/gkz809.
Повний текст джерелаTherkildsen, M., B. Riis, A. Karlsson, L. Kristensen, P. Ertbjerg, P. P. Purslow, M. Dall Aaslyng, and N. Oksbjerg. "Compensatory growth response in pigs, muscle protein turn-over and meat texture: effects of restriction/realimentation period." Animal Science 75, no. 3 (December 2002): 367–77. http://dx.doi.org/10.1017/s1357729800053145.
Повний текст джерелаRuiz-Gómez, Gloria, Joel D. A. Tyndall, Bernhard Pfeiffer, Giovanni Abbenante, and David P. Fairlie. "Update 1 of: Over One Hundred Peptide-Activated G Protein-Coupled Receptors Recognize Ligands with Turn Structure." Chemical Reviews 110, no. 4 (April 14, 2010): PR1—PR41. http://dx.doi.org/10.1021/cr900344w.
Повний текст джерелаOdolczyk, Norbert, Ewa Marzec, Maria Winiewska-Szajewska, Jarosław Poznański, and Piotr Zielenkiewicz. "Native Structure-Based Peptides as Potential Protein–Protein Interaction Inhibitors of SARS-CoV-2 Spike Protein and Human ACE2 Receptor." Molecules 26, no. 8 (April 9, 2021): 2157. http://dx.doi.org/10.3390/molecules26082157.
Повний текст джерелаKnap, P. W. "Stochastic simulation of growth in pigs: relations between body composition and maintenance requirements as mediated through protein turn-over and thermoregulation." Animal Science 71, no. 1 (April 2000): 11–30. http://dx.doi.org/10.1017/s1357729800054850.
Повний текст джерелаZitnik, Marinka, Rok Sosič, Marcus W. Feldman, and Jure Leskovec. "Evolution of resilience in protein interactomes across the tree of life." Proceedings of the National Academy of Sciences 116, no. 10 (February 14, 2019): 4426–33. http://dx.doi.org/10.1073/pnas.1818013116.
Повний текст джерелаAyana Gayathri, R. V., and D. A. Evans. "Culex quinquefasciatus Say larva adapts to temperature shock through changes in protein turn over and amino acid catabolism." Journal of Thermal Biology 74 (May 2018): 149–59. http://dx.doi.org/10.1016/j.jtherbio.2018.03.016.
Повний текст джерелаAl Tanoury, Ziad, Elisabeth Schaffner-Reckinger, Aliaksandr Halavatyi, Céline Hoffmann, Michèle Moes, Ermin Hadzic, Marie Catillon, Mikalai Yatskou, and Evelyne Friederich. "Quantitative Kinetic Study of the Actin-Bundling Protein L-Plastin and of Its Impact on Actin Turn-Over." PLoS ONE 5, no. 2 (February 15, 2010): e9210. http://dx.doi.org/10.1371/journal.pone.0009210.
Повний текст джерелаClark, Lilian, John Nicholson, and Ronald T. Hay. "Enhancer binding protein (EBP1) makes base and backbone contacts over one complete turn of the DNA double helix." Journal of Molecular Biology 206, no. 4 (April 1989): 615–26. http://dx.doi.org/10.1016/0022-2836(89)90570-6.
Повний текст джерелаPanja, Anindya Sundar, Bidyut Bandopadhyay, Akash Nag, and Smarajit Maiti. "Protein Secondary Structure Determination (PSSD): A New and Simple Approach." Current Proteomics 16, no. 3 (February 18, 2019): 246–53. http://dx.doi.org/10.2174/1570164615666180911113251.
Повний текст джерелаSun, Xiaotong, Hua Jin, Yangyang Li, Haiying Feng, Chunhong Liu, and Jing Xu. "The Molecular Properties of Peanut Protein: Impact of Temperature, Relative Humidity and Vacuum Packaging during Storage." Molecules 23, no. 10 (October 12, 2018): 2618. http://dx.doi.org/10.3390/molecules23102618.
Повний текст джерелаHorne, Jim E., та Sheena E. Radford. "A growing toolbox of techniques for studying β-barrel outer membrane protein folding and biogenesis". Biochemical Society Transactions 44, № 3 (9 червня 2016): 802–9. http://dx.doi.org/10.1042/bst20160020.
Повний текст джерелаStrunk, Bethany S., Noah Steinfeld, Sora Lee, Natsuko Jin, Cecilia Muñoz-Rivera, Garrison Meeks, Asha Thomas, et al. "Roles for a lipid phosphatase in the activation of its opposing lipid kinase." Molecular Biology of the Cell 31, no. 17 (August 1, 2020): 1835–45. http://dx.doi.org/10.1091/mbc.e18-09-0556.
Повний текст джерелаShitov, Alexandr V. "An Insight into the Bicarbonate Effect in Photosystem II through the Prism of the JIP Test." Photochem 2, no. 3 (September 15, 2022): 779–97. http://dx.doi.org/10.3390/photochem2030050.
Повний текст джерелаFahie, Kamau M. M., Kyriakos N. Papanicolaou, and Natasha E. Zachara. "Integration of O-GlcNAc into Stress Response Pathways." Cells 11, no. 21 (November 5, 2022): 3509. http://dx.doi.org/10.3390/cells11213509.
Повний текст джерелаFernandes, Ana Clara, Valerie Uytterhoeven, Sabine Kuenen, Yu-Chun Wang, Jan R. Slabbaert, Jef Swerts, Jaroslaw Kasprowicz, Stein Aerts, and Patrik Verstreken. "Reduced synaptic vesicle protein degradation at lysosomes curbs TBC1D24/sky-induced neurodegeneration." Journal of Cell Biology 207, no. 4 (November 24, 2014): 453–62. http://dx.doi.org/10.1083/jcb.201406026.
Повний текст джерелаRao, D. S., and K. J. McCracken. "Energy: protein interactions in growing boars of high genetic potential for lean growth. 2. Effects on chemical composition of gain and whole-body protein turn-over." Animal Science 54, no. 1 (February 1992): 83–93. http://dx.doi.org/10.1017/s0003356100020602.
Повний текст джерелаGreen, D. M., and C. T. Whittemore. "Architecture of a harmonized model of the growing pig for the determination of dietary net energy and protein requirements and of excretions into the environment (IMS Pig)." Animal Science 77, no. 1 (April 2003): 113–26. http://dx.doi.org/10.1017/s1357729800053716.
Повний текст джерелаPrelesnik, Jesse L., Robert G. Alberstein, Shuai Zhang, Harley Pyles, David Baker, Jim Pfaendtner, James J. De Yoreo, F. Akif Tezcan, Richard C. Remsing, and Christopher J. Mundy. "Ion-dependent protein–surface interactions from intrinsic solvent response." Proceedings of the National Academy of Sciences 118, no. 26 (June 25, 2021): e2025121118. http://dx.doi.org/10.1073/pnas.2025121118.
Повний текст джерелаToyama, Brandon H., Rafael Arrojo e Drigo, Varda Lev-Ram, Ranjan Ramachandra, Thomas J. Deerinck, Claude Lechene, Mark H. Ellisman, and Martin W. Hetzer. "Visualization of long-lived proteins reveals age mosaicism within nuclei of postmitotic cells." Journal of Cell Biology 218, no. 2 (December 14, 2018): 433–44. http://dx.doi.org/10.1083/jcb.201809123.
Повний текст джерелаGueudré, Thomas, Carlo Baldassi, Marco Zamparo, Martin Weigt, and Andrea Pagnani. "Simultaneous identification of specifically interacting paralogs and interprotein contacts by direct coupling analysis." Proceedings of the National Academy of Sciences 113, no. 43 (October 11, 2016): 12186–91. http://dx.doi.org/10.1073/pnas.1607570113.
Повний текст джерелаSainz, R. D., and J. E. Wolff. "Evaluation of hypotheses regarding mechanisms of action of growth promotants and repartitioning agents using a simulation model of lamb metabolism and growth." Animal Science 51, no. 3 (December 1990): 551–58. http://dx.doi.org/10.1017/s0003356100012587.
Повний текст джерелаGoulet, O., S. De Potter, H. Rongier, JJ Robert, C. Ricour, and D. Darmaun. "EFFECT OF GRADED NITROGEN INTAKES ON WHOLE BODY PROTEIN TURN OVER MEASURED WITH C-LEUCINE IN ADOLESCENTS ON PARENTERAL NUTRITION (PN)." Journal of Pediatric Gastroenterology and Nutrition 13, no. 3 (October 1991): 331. http://dx.doi.org/10.1097/00005176-199110000-00107.
Повний текст джерелаPowers, Kathleen. "The Prion as Nature’s Undead." Qui Parle 31, no. 1 (June 1, 2022): 109–42. http://dx.doi.org/10.1215/10418385-9669514.
Повний текст джерелаCampbell, Kevin, та Lukasz Kurgan. "Sequence-Only Based Prediction of β -Turn Location and Type Using Collocation of Amino Acid Pairs". Open Bioinformatics Journal 2, № 1 (6 серпня 2008): 37–49. http://dx.doi.org/10.2174/1875036200802010037.
Повний текст джерелаIlina, Tatiana V., Zhaoyong Xi, Teresa Brosenitsch, Nicolas Sluis-Cremer, and Rieko Ishima. "Large Multidomain Protein NMR: HIV-1 Reverse Transcriptase Precursor in Solution." International Journal of Molecular Sciences 21, no. 24 (December 15, 2020): 9545. http://dx.doi.org/10.3390/ijms21249545.
Повний текст джерелаBarber, J. R., and I. M. Verma. "Modification of fos proteins: phosphorylation of c-fos, but not v-fos, is stimulated by 12-tetradecanoyl-phorbol-13-acetate and serum." Molecular and Cellular Biology 7, no. 6 (June 1987): 2201–11. http://dx.doi.org/10.1128/mcb.7.6.2201-2211.1987.
Повний текст джерелаBarber, J. R., and I. M. Verma. "Modification of fos proteins: phosphorylation of c-fos, but not v-fos, is stimulated by 12-tetradecanoyl-phorbol-13-acetate and serum." Molecular and Cellular Biology 7, no. 6 (June 1987): 2201–11. http://dx.doi.org/10.1128/mcb.7.6.2201.
Повний текст джерелаBalasubramanian, Anuradha, Monica Markovski, Joel R. Hoskins, Shannon M. Doyle, and Sue Wickner. "Hsp90 of E. coli modulates assembly of FtsZ, the bacterial tubulin homolog." Proceedings of the National Academy of Sciences 116, no. 25 (June 3, 2019): 12285–94. http://dx.doi.org/10.1073/pnas.1904014116.
Повний текст джерелаSRIHARI, SRIGANESH, and HON WAI LEONG. "A SURVEY OF COMPUTATIONAL METHODS FOR PROTEIN COMPLEX PREDICTION FROM PROTEIN INTERACTION NETWORKS." Journal of Bioinformatics and Computational Biology 11, no. 02 (April 2013): 1230002. http://dx.doi.org/10.1142/s021972001230002x.
Повний текст джерелаSolomon, David A., M. Cristina Cardoso, and Erik S. Knudsen. "Dynamic targeting of the replication machinery to sites of DNA damage." Journal of Cell Biology 166, no. 4 (August 16, 2004): 455–63. http://dx.doi.org/10.1083/jcb.200312048.
Повний текст джерелаHöhn, Annika, Antonella Tramutola, and Roberta Cascella. "Proteostasis Failure in Neurodegenerative Diseases: Focus on Oxidative Stress." Oxidative Medicine and Cellular Longevity 2020 (March 27, 2020): 1–21. http://dx.doi.org/10.1155/2020/5497046.
Повний текст джерелаLoyer, P., J. H. Trembley, J. M. Lahti, and V. J. Kidd. "The RNP protein, RNPS1, associates with specific isoforms of the p34cdc2-related PITSLRE protein kinase in vivo." Journal of Cell Science 111, no. 11 (June 1, 1998): 1495–506. http://dx.doi.org/10.1242/jcs.111.11.1495.
Повний текст джерелаSilverman, J. A., J. Mehta, S. Brocher, and J. S. Amenta. "Analytical errors in measuring radioactivity in cell proteins and their effect on estimates of protein turnover in L cells." Biochemical Journal 226, no. 2 (March 1, 1985): 361–68. http://dx.doi.org/10.1042/bj2260361.
Повний текст джерелаTan, Maxine H., Sarah R. Smith, Kim K. Hixson, Justin Tan, James K. McCarthy, Adam B. Kustka, and Andrew E. Allen. "The Importance of Protein Phosphorylation for Signaling and Metabolism in Response to Diel Light Cycling and Nutrient Availability in a Marine Diatom." Biology 9, no. 7 (July 6, 2020): 155. http://dx.doi.org/10.3390/biology9070155.
Повний текст джерелаGunter, Stacey, and Corey A. Moffet. "39 Thoughts on the energetic efficiency of grazing cattle." Journal of Animal Science 97, Supplement_1 (July 2019): 69. http://dx.doi.org/10.1093/jas/skz053.156.
Повний текст джерелаGinting, Andi Raga, Rudy Hidayat, Sumariyono Sumariyono та Sukamto Koesnoe. "Role of Secreted Frizzled-Related Protein 1 and Tumor Necrosis Factor-α (TNF-α) in Bone Loss of Patients with Rheumatoid Arthritis". International Journal of Rheumatology 2020 (1 березня 2020): 1–7. http://dx.doi.org/10.1155/2020/9149762.
Повний текст джерелаPremrov Bajuk, Blanka, Petra Zrimšek, Maja Zakošek Pipan, Bruno Tilocca, Alessio Soggiu, Luigi Bonizzi, and Paola Roncada. "Proteomic Analysis of Fresh and Liquid-Stored Boar Spermatozoa." Animals 10, no. 4 (March 26, 2020): 553. http://dx.doi.org/10.3390/ani10040553.
Повний текст джерелаPereira, Ricardo N., and Rui M. Rodrigues. "Emergent Proteins-Based Structures—Prospects towards Sustainable Nutrition and Functionality." Gels 7, no. 4 (October 1, 2021): 161. http://dx.doi.org/10.3390/gels7040161.
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