Relevant bibliographies by topics / Proteolysis

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Proteolysis'

Author: Grafiati
Published: 4 June 2021
Last updated: 25 July 2025

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Journal articles on the topic "Proteolysis"

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Navegantes, Luiz Carlos C., Neusa M. Z. Resano, Renato H. Migliorini, and 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, no. 5 (1999): E883—E889. http://dx.doi.org/10.1152/ajpendo.1999.277.5.e883.

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Overall proteolysis and the activity of skeletal muscle proteolytic systems were investigated in rats submitted to guanethidine-induced adrenergic blockade for 4 days. In soleus, overall proteolysis increased by 15–20% during the first 2 days of guanethidine treatment but decreased to levels below control values after 4 days. Extensor digitorum longus (EDL) did not show the initial increase in total proteolysis, which was already reduced after 2 days of guanethidine treatment. The initial rise in the rate of protein degradation in soleus was accompanied by an increased activity of the Ca2+-dep
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Navegantes, Luiz Carlos C., Neusa M. Z. Resano, Renato H. Migliorini та 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, № 3 (2001): E449—E454. http://dx.doi.org/10.1152/ajpendo.2001.281.3.e449.

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Overall proteolysis and the activity of skeletal muscle proteolytic systems were investigated in rats 1, 2, or 4 days after adrenodemedullation. Adrenodemedullation reduced plasma epinephrine by 95% and norepinephrine by 35% but did not affect muscle norepinephrine content. In soleus and extensor digitorum longus (EDL) muscles, rates of overall proteolysis increased by 15–20% by 2 days after surgery but returned to normal levels after 4 days. The rise in rates of protein degradation was accompanied by an increased activity of Ca2+-dependent proteolysis in both muscles, with no significant chan
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LARBAUD, Daniel, Michèle BALAGE, Daniel TAILLANDIER, Lydie COMBARET, Jean GRIZARD, and 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, no. 6 (2001): 551–58. http://dx.doi.org/10.1042/cs1010551.

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In order to characterize the poorly defined mechanisms that account for the anti-proteolytic effects of insulin in skeletal muscle, we investigated in rats the effects of a 3h systemic euglycaemic hyperinsulinaemic clamp on lysosomal, Ca2+-dependent proteolysis, and on ubiquitin/proteasome-dependent proteolysis. Proteolysis was measured in incubated fast-twitch mixed-fibre extensor digitorum longus (EDL) and slow-twitch red-fibre soleus muscles harvested at the end of insulin infusion. Insulin inhibited proteolysis (P < 0.05) in both muscles. This anti-proteolytic effect disappeared in the
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Kominami, Yuri, Tatsuya Hayashi, Tetsuji Tokihiro, and Hideki Ushio. "A Novel Analysis of the Peptide Terminome Characterizes Dynamics of Proteolytic Regulation in Vertebrate Skeletal Muscle Under Severe Stress." Proteomes 7, no. 1 (2019): 6. http://dx.doi.org/10.3390/proteomes7010006.

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In healthy cells, proteolysis is orderly executed to maintain basal homeostasis and normal physiology. Dyscontrol in proteolysis under severe stress condition induces cell death, but the dynamics of proteolytic regulation towards the critical phase remain unclear. Teleosts have been suggested an alternative model for the study of proteolysis under severe stress. In this study, horse mackerel (Trachurus japonicus) was used and exacerbated under severe stress conditions due to air exposure. Although the complete genome for T. japonicus is not available, a transcriptomic analysis was performed to
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Volodymyr, Yukalo, Datsyshyn Kateryna, and Storozh Liudmyla. "COMPARISON OF PRODUCTS OF WHEY PROTEINS CONCENTRATE PROTEOLYSIS, OBTAINED BY DIFFERENT PROTEOLYTIC PREPARATIONS." Eastern-European Journal of Enterprise Technologies 5, no. 11 (101) (2019): 40–47. https://doi.org/10.15587/1729-4061.2019.177314.

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An important source of bioactive peptides is hydrolyzed products based on milk whey: hypoallergenic products, hydrolyzates for baby food, and products for athletes. However, in their production, proteolytic preparations of different origin are used. This may affect the degree of proteolysis of the biologically active peptides (BAP) proteins-precursors, the proteolysis products molecular weight distribution and, accordingly, the probability of BAP formation. A comparison of the degree of whey protein concentrate (WPC) proteins proteolysis and the molecular weight distribution of proteolysis pro
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Portbury, Andrea L., Monte S. Willis, and Cam Patterson. "Tearin' Up My Heart: Proteolysis in the Cardiac Sarcomere." Journal of Biological Chemistry 286, no. 12 (2011): 9929–34. http://dx.doi.org/10.1074/jbc.r110.170571.

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Proteolysis within the cardiac sarcomere is a constantly evolving area of research. Three major pathways of proteolysis have been identified as being active within the cardiac sarcomere, namely the ubiquitin-proteasome system, autophagy, and the calpain system. The role of ubiquitin-proteasome system-mediated proteolysis in cardiovascular health and disease has been known for some time; however, it is now apparent that other proteolytic systems also aid in the stabilization of cardiac sarcomere structure and function. This minireview focuses on the individual as well as cooperative involvement
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Sun, Z., W. Carpiaux, D. Fan, Y. Fan, R. Lakshminarayanan, and J. Moradian-Oldak. "Apatite Reduces Amelogenin Proteolysis by MMP-20 and KLK4 in vitro." Journal of Dental Research 89, no. 4 (2010): 344–48. http://dx.doi.org/10.1177/0022034509360660.

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Two enamel proteases, matrix metalloproteinase-20 (MMP-20) and kallikrein 4 (KLK4), are known to cleave amelogenin and are necessary for proper enamel formation. However, the effect of hydroxyapatite (HAP) on the proteolytic activity of these enzymes remains unclear. To investigate whether apatite affects normal amelogenin proteolysis, we used 2 different isoforms of amelogenin combined with the appropriate enzymes to analyze proteolytic processing rates in the presence or absence of synthetic hydroxyapatite (HAP) crystals (N = 3). We found a distinct dose-dependent relationship between the am
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Picard, Catherine, Isabelle Plard, Dominique Rongdaux-Gaida, and Jean-Claude Collin. "Detection of proteolysis in raw milk stored at low temperature by an inhibition ELISA." Journal of Dairy Research 61, no. 3 (1994): 395–404. http://dx.doi.org/10.1017/s0022029900030818.

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SummaryAn inhibition ELISA (enzyme-linked immunosorbent assay) was developed for the determination of caseinomacropeptide (CMP) in order to estimate the proteolysis of κ-casein due to the enzymes of psychrotrophic bacteria in bulk raw milk. The CMP present in milk was quantified specifically by an antibody. The limit of detection was ∽ 0·1 μg/ml and the CV was < 10%. This method was used to study the proteolytic activity of three strains of psychrotrophic Pseudomonas fluorescens in raw milk and to analyse different raw milk samples supplied by four dairy plants. The proteolytic activity for
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Adasheva, Daria A., Olga S. Lebedeva, Daria V. Goliusova, et al. "PAPP-A-Specific IGFBP-4 Proteolysis in Human Induced Pluripotent Stem Cell-Derived Cardiomyocytes." International Journal of Molecular Sciences 24, no. 9 (2023): 8420. http://dx.doi.org/10.3390/ijms24098420.

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The insulin-like growth factors IGF-I and IGF-II—as well as their binding proteins (IGFBPs), which regulate their bioavailability—are involved in many pathological and physiological processes in cardiac tissue. Pregnancy-associated plasma protein A (PAPP-A) is a metalloprotease that preferentially cleaves IGFBP-4, releasing IGF and activating its biological activity. Previous studies have shown that PAPP-A-specific IGFBP-4 proteolysis is involved in the pathogenesis of cardiovascular diseases, such as ischemia, heart failure, and acute coronary syndrome. However, it remains unclear whether PAP
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Shang, F., and 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, no. 1 (1995): 297–303. http://dx.doi.org/10.1042/bj3070297.

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Roles for ubiquitin (an 8.5 kDa polypeptide) involve its conjugation to proteins as a signal to initiate degradation and as a stress protein. We investigated ubiquitin conjugation and ubiquitin-dependent proteolytic activities in cultured bovine lens epithelial cells (BLECs) upon oxidative challenge. A 44% decrease in intracellular glutathione confirmed oxidative stress upon incubation with 1 mM H2O2. After 30 min incubation, endogenous high-molecular-mass ubiquitin conjugates decreased 73%, and intracellular proteolysis decreased about 50%. In the supernatants of the oxidatively treated BLECs
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Dissertations / Theses on the topic "Proteolysis"

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El-Daher, Marie-Thérèse. "Huntingtin proteolysis and toxicity." Thesis, Paris 11, 2013. http://www.theses.fr/2013PA11T029/document.

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La maladie de Huntington (MH) est une maladie neurodégénérative héréditaire autosomique dominante. Elle est due à l’expansion anormale de polyglutamine dans la partie N-terminal de la protéine huntingtine (HTT). Une des étapes clés de la pathologie est le clivage de la HTT pleine longueur en fragments N-terminaux plus petits, contenant l’expansion de polyglutamine, et qui sont toxiques pour les neurones. En effet, les clivages de la HTT mutée génère des fragments N-terminaux (N-ter) de tailles comprises entre les acides aminés 1-105 et 1-586 observés dans des extraits de cerveaux de patients M
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Clay, L. "CDC20 function, regulation and proteolysis." Thesis, University of Cambridge, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.597750.

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The destruction of mitotic cyclins and other key regulators uses ubiquitin mediated proteolysis controlled via the activation of the ubiquitin ligase the Anaphase Promoting Complex/Cyclosome (APC/C), and its adaptor proteins Cdc20 and Cdh1. The spindle assembly checkpoint coordinates the APC/C with microtubule attachment and sets the timing from NEBD to anaphase. Cdc20 is inactivated by the spindle assembly checkpoint to prevent premature anaphase onset. Once the spindle assembly checkpoint is satisfied, Cdc20 can be released and activate the APC/C. However, cyclin A is degraded independently
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Slee, Adrian. "Regulation of skeletal muscle proteolysis." Thesis, University of Nottingham, 2005. http://eprints.nottingham.ac.uk/13105/.

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Proteolysis is a component of protein turnover, controlled by multiple proteolytic systems. Alterations in system components within skeletal muscle has been associated with hypertrophy, remodelling, atrophy, apoptosis and metabolic dysregulation. Key components may have novel regulatory roles, e. g. calpain-3 and cathepsin-L. Experiments described within this thesis investigated the hypothesis that the gene expression of specific proteolytic system components within skeletal muscle may be co-ordinately regulated and altered during nutritional and pharmacological states known to modify protein
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Andréasson, Claes. "Ligand-activated proteolysis in nutrient signaling /." Stockholm, 2004. http://diss.kib.ki.se/2004/91-7140-075-3/.

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Hutton, David Alan. "Studies on mucin isolation and proteolysis." Thesis, University of Newcastle Upon Tyne, 1991. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.287272.

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Canning, Mary. "Ubiquitin-mediated proteolysis and Drosophila embryogenesis." Thesis, University of Edinburgh, 2000. http://hdl.handle.net/1842/13305.

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Ubiquitination provides a means of rapidly and irreversibly eliminating an unwanted protein from the cell, and is therefore a potentially effective tool for regulating cellular behaviour. Ubiquitin-mediated proteolysis is involved in such diverse physiological functions as growth control, cell signalling, differentiation and the immune response. The aim of this research has been to investigate its role in <i>Drosophila </i>embryogenesis. Protein ubiquitination is a stepwise process carried out by three classes of enzyme known as E1s, E2s and E3s. The E1 (ubiquitin-activating enzyme), generates
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Smith, Kate L. "Tumour associated proteolysis and protein metabolism." Thesis, Aston University, 1992. http://publications.aston.ac.uk/12604/.

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The effect of cancer cachexia on protein metabolism has been studied in mice transplanted with the MAC16 adenocarcinoma. The progressive cachexia induced by the MAC16 tumour was characterised by a reduction in carcass nitrogen between 16-30% weight loss and a reciprocal increase in tumour nitrogen content. Carcass nitrogen loss was accompanied by a concomitant decrease in gastrocnemius muscle weight and nitrogen content and also by a decrease in liver nitrogen content. The loss of gastrocnemius muscle throughout the progression of cachexia was attributable to a 60% decrease in the rate of prot
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Lemberg, Marius Kaspar. "Intramembrane proteolysis by the aspartic protease SPP /." Zürich, 2003. http://e-collection.ethbib.ethz.ch/show?type=diss&nr=15327.

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Potocka, Isabel. "Cell-cycle regulated proteolysis in Caulobacter crescentus." Thesis, Imperial College London, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.252229.

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Campbell, William. "Characterisation of the proteolysis of chromogranin A." Thesis, Queen's University Belfast, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.301777.

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Books on the topic "Proteolysis"

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Chondrogianni, Niki, Elah Pick, and Anna Gioran. Proteostasis and Proteolysis. CRC Press, 2021. http://dx.doi.org/10.1201/9781003048138.

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Antonov, Vladimir K. Chemistry of Proteolysis. Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-662-00979-6.

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Keil, Borivoj. Specificity of Proteolysis. Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-48380-6.

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Abatangelo, G., L. Donati, and W. Vanscheidt, eds. Proteolysis in Wound Repair. Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-642-61130-8.

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Dougan, David A., ed. Regulated Proteolysis in Microorganisms. Springer Netherlands, 2013. http://dx.doi.org/10.1007/978-94-007-5940-4.

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1946-, Mellgren Ronald L., and Murachi Takashi 1926-, eds. Intracellular calcium-dependent proteolysis. CRC Press, 1990.

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K, Hopsu-Havu Väinö, Järvinen M, Kirschke Heidrun, and International Conference on Proteolysis and Protein Turnover (11th : 1996 : Turku, Finland), eds. Proteolysis in cell functions. IOS Press, 1997.

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C, Taylor Joseph, and Mittman Charles, eds. Pulmonary emphysema and proteolysis, 1986. Academic Press, 1987.

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Smith, Kate Louise. Tumour associated proteolysis and protein metabolism. Aston University. Department of Pharmaceutical Sciences, 1992.

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Falokun, Christopher D. Aspects of molecular recognition in limited proteolysis. UMIST, 1996.

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Book chapters on the topic "Proteolysis"

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Bond, Judith S., Timothy R. Keiffer, and Qi Sun. "Pericellular Proteolysis." In Extracellular Matrix Degradation. Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-16861-1_4.

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Brix, Klaudia, Christopher J. Scott, and Margarete M. S. Heck. "Compartmentalization of Proteolysis." In Proteases: Structure and Function. Springer Vienna, 2013. http://dx.doi.org/10.1007/978-3-7091-0885-7_3.

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Tatsuta, Takashi, and Thomas Langer. "Studying Proteolysis Within Mitochondria." In Methods in Molecular Biology. Humana Press, 2007. http://dx.doi.org/10.1007/978-1-59745-365-3_25.

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Bøgh, Katrine Lindholm, and Jeppe Madura Larsen. "Reducing Allergenicity by Proteolysis." In Agents of Change. Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-55482-8_19.

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Lindon, Catherine, and Barbara Di Fiore. "Measuring Proteolysis in Mitosis." In Methods in Molecular Biology. Humana Press, 2009. http://dx.doi.org/10.1007/978-1-60327-993-2_16.

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Rodriguez-Gonzalez, Agustin, and Kathleen M. Sakamoto. "Proteolysis Targeting Chimeric Molecules." In Modulation of Protein Stability in Cancer Therapy. Springer US, 2009. http://dx.doi.org/10.1007/978-0-387-69147-3_9.

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Hook, Vivian Y. H., and Liane Mende-Mueller. "Proteolysis in Neurodegenerative Diseases." In Molecular Mechanisms of Neurodegenerative Diseases. Humana Press, 2001. https://doi.org/10.1007/978-1-59259-006-3_5.

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Antonov, Vladimir K. "Introduction." In Chemistry of Proteolysis. Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-662-00979-6_1.

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Antonov, Vladimir K. "Substrates." In Chemistry of Proteolysis. Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-662-00979-6_2.

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Antonov, Vladimir K. "Enzymes." In Chemistry of Proteolysis. Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-662-00979-6_3.

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Conference papers on the topic "Proteolysis"

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Batlle, J., M. F. López-Fernández, C. López-Berges, S. D. Berkowitz, Z. M. Ruggeri, and T. S. Zimmerman. "PROTEOLYTIC DEGRADATION OF VON WILLEBRAND FACTOR AFTER DDAVP ADMINISTRATION IN NORMAL INDIVIDUALS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644121.

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The infusion of l-Deamino-8-D-Arginine Vasopressin (DDAVP) in normal individuals is followed by an increase in factor VIII/von Willebrand factor in plasma and by the appearance of larger multimers of von Willebrand factor (vWF) than those seen in the resting state. Since the larger multimers are rapidly cleared and proteolysis is known to cause disaggregation of large multimers, we evaluated the degree of vWF proteolysis after DDAVP. DDAVP was infused into eight normal adult volunteers and the relative proportions of the intact 225 kDa subunit and the 189, 176 and 140 kDa fragments were compar
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Ghosh, A., R. D. Coakley, D. B. Hill, M. Kesimer, N. E. Alexis, and R. Tarran. "Vaping-Induced Proteolysis Causes Airway Dehydration." In American Thoracic Society 2023 International Conference, May 19-24, 2023 - Washington, DC. American Thoracic Society, 2023. http://dx.doi.org/10.1164/ajrccm-conference.2023.207.1_meetingabstracts.a4060.

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Gao, Jinfeng, Chuhan Meng, and Vivian FT Yuan. "Clinical application of proteolysis targeting chimeras." In International Conference on Modern Medicine and Global Health (ICMMGH 2023), edited by Sheiladevi Sukumaran. SPIE, 2023. http://dx.doi.org/10.1117/12.3000206.

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Bischel, Kristen Moriah, Philip Emmerich, Tonela Qyli, et al. "Abstract 403: Versican proteolysis in endometrial cancer." In Proceedings: AACR Annual Meeting 2020; April 27-28, 2020 and June 22-24, 2020; Philadelphia, PA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.am2020-403.

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Antipina, M. I., E. G. Chupakhin, V. V. Kakotkin, M. A. Agapov, and E. V. Semina. "MOLECULAR THERAPY OF NEURODEGENERATIVE PATHOLOGIES USING TARGETED UBIQUITIN-DEPENDENT PROTEOLYSIS OF PROTEIN TARGETS WITH PROTACS (PROTEOLYSIS TARGETING CHIMERAS)." In X Международная конференция молодых ученых: биоинформатиков, биотехнологов, биофизиков, вирусологов и молекулярных биологов — 2023. Novosibirsk State University, 2023. http://dx.doi.org/10.25205/978-5-4437-1526-1-287.

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Aggregation of microtubule-associated tau protein (MAPT) due to its hyperphosphorylation is a hallmark of Alzheimer’s disease (AD). Therefore, targeting MAPT is one of the promising approaches for AD therapy. PROTAC (Proteolysis Targeting Chimeras) system is one of the possible therapy options for neurodegenerative diseases, which is used to selectively degrade a target protein in a cell.
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duVERLE, DAVID, ICHIGAKU TAKIGAWA, YASUKO ONO, HIROYUKI SORIMACHI, and HIROSHI MAMITSUKA. "CaMPDB: A RESOURCE FOR CALPAIN AND MODULATORY PROTEOLYSIS." In Proceedings of the 9th Annual International Workshop on Bioinformatics and Systems Biology (IBSB 2009). IMPERIAL COLLEGE PRESS, 2010. http://dx.doi.org/10.1142/9781848165786_0017.

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Roslan, Nur Farhana, Bee Lyn Chew, Hoe-Han Goh, and Nurulhikma Md Isa. "Sequence analysis of PROTEOLYSIS 6 from Solanum lycopersicum." In THE 2017 UKM FST POSTGRADUATE COLLOQUIUM: Proceedings of the University Kebangsaan Malaysia, Faculty of Science and Technology 2017 Postgraduate Colloquium. Author(s), 2018. http://dx.doi.org/10.1063/1.5027977.

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Berkowitz, S. D., H. Nozaki, K. Titani, T. Murachi, and T. S. Zimmerman. "CALPAIN AND ELASTASE ARE NOT RESPONSIBLE FOR THE VON WILLEBRAND FACTOR FRAGMENTS IN NORMAL PLASMA AND IIA VON WILLEBRAND DISEASE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644103.

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Recent evidence suggests that proteolysis plays an important role in some forms of inherited and acquired von Willebrand disease (vWD). Using monoclonal epitope mapping, we have examined the proteolysis of the von Willebrand factor (vWF) subunit with platelet calcium activated neutral protease (CANP) and human leukocyte elastase and found that they are not responsible for the proteolytic cleavage sejen in normal individuals and IIA vWD. Previously we have shown that in vivo proteolysis of vWF is a normal event with a small but consistent proportion of plasma vWF being composed of 189, 176, and
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Wallace, Robert W., E. Ann Tallant, and Lynn M. Brumley. "POSSIBLE ROLE FOR THE CA2+-DEPENDENT PROTEASE (CALPAIN I) AS AN IRREVERSIBLE ACTIVATOR OF CA2+/CALMODULIN-MEDIATED REACTIONS IN THE HUMAN PLATELET." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644528.

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Calmodulin (CaM)-binding proteins have been identified in human platelets using Western blotting techniques and 125I-CaM. Ten proteins of 245, 225. 175, 150, 90. 82(2), 60 and 41(2) kilodaltons (kDa) bind 125I-CaM in a Ca2+-dependent manner; the binding is blocked by both trifluoperazine and nonradiolabeled CaM. The 225 and 90 kDa proteins are labeled by antisera against myosin light chain kinase (MLCK); the 60 kDa and one of the 82 kDa proteins have been identified as the CaM-dependent phosphatase (calcineurin) and caldesmon. The other proteins are presumed to be other Ca2+/CaM regulated enzy
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Parise, L. V., B. Steiner, L. Nannizzi, and D. A. Phillips. "PEPTIDES FROM FIBRINOGENAND FIBRONECTIN CHANGE THE CONFORMATIONOF PURIFIED PLATELET GLYCOPROTEIN IIb-IIIa." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643697.

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Specific amino acid sequences in fibrinogen and fibronectin appear to mediate the binding of these ligands to the glycoprotein (GP) IIb-IIIacomplex in platelets. Thesesequences include LGGAKQAGDV from the y chain of fibrinogen, and RGD(S) from the a chain of fibrinogenand the cell-binding domain of fibronectin. Several recent reports suggest thatfibrinogen and/or peptides with these sequences cause clustering of GPIIb-IIIa on the platelet surface and Na+/H+ exchange in epinephrine-stimulated platelets. Thus, it is possible that occupancy of specific sites on GP Ilb-IIIa affects its conformatio
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Reports on the topic "Proteolysis"

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Harper, Jeffrey. Identification of Genes Regulated by Proteolysis. Defense Technical Information Center, 2002. http://dx.doi.org/10.21236/ada408062.

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Carlson, Kelsey, Kenneth J. Prusa, Chris A. Fedler, et al. Proteolysis Influences Tenderness of Aged Pork Loins. Iowa State University, 2017. http://dx.doi.org/10.31274/ans_air-180814-328.

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Mudryj, Maria. Calpain-Dependent Proteolysis of the Androgen Receptor. Defense Technical Information Center, 2009. http://dx.doi.org/10.21236/ada517269.

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Strohmaier, Heimo M., and Steven Reed. The Role of Deregulated Cyclin E Proteolysis in Breast Cancer Development. Defense Technical Information Center, 2002. http://dx.doi.org/10.21236/ada409788.

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Drogen, Frank van, Steven Reed, and Heimo M. Strohmaier. The Role of Deregulated Cyclin E Proteolysis in Breast Cancer Development. Defense Technical Information Center, 2003. http://dx.doi.org/10.21236/ada418341.

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Spruck, Charles H. Identification of Substances for Ubiquitin-Dependent Proteolysis During Breast Tumor Progression. Defense Technical Information Center, 2008. http://dx.doi.org/10.21236/ada510763.

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Srikanth, Appikonda. The Role of Ubiquitin-Mediated Proteolysis of Cyclin D in Breast Cancer. Defense Technical Information Center, 2005. http://dx.doi.org/10.21236/ada455151.

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Block, Karen L. The Role of Ubiquitin-Mediated Proteolysis of Cyclin D in Breast Cancer. Defense Technical Information Center, 2003. http://dx.doi.org/10.21236/ada416662.

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Khokha, Rama. Molecular Tracking of Proteolysis During Breast Cancer Cell Extravasation: Blockage of Therapeutic Inhibitors. Defense Technical Information Center, 2002. http://dx.doi.org/10.21236/ada411429.

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Xiong, Yue. G1 Cell Cycle Control by Regulated Proteolysis in Normal and Tumorigenic Breast Cells. Defense Technical Information Center, 2002. http://dx.doi.org/10.21236/ada415516.

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