Добірка наукової літератури з теми "PCSK1"
Оформте джерело за APA, MLA, Chicago, Harvard та іншими стилями
Ознайомтеся зі списками актуальних статей, книг, дисертацій, тез та інших наукових джерел на тему "PCSK1".
Біля кожної праці в переліку літератури доступна кнопка «Додати до бібліографії». Скористайтеся нею – і ми автоматично оформимо бібліографічне посилання на обрану працю в потрібному вам стилі цитування: APA, MLA, «Гарвард», «Чикаго», «Ванкувер» тощо.
Також ви можете завантажити повний текст наукової публікації у форматі «.pdf» та прочитати онлайн анотацію до роботи, якщо відповідні параметри наявні в метаданих.
Статті в журналах з теми "PCSK1":
Parvaz, Najmeh, and Zahra Jalali. "Molecular evolution of PCSK family: Analysis of natural selection rate and gene loss." PLOS ONE 16, no. 10 (October 28, 2021): e0259085. http://dx.doi.org/10.1371/journal.pone.0259085.
Gagnon, Jeffrey, Janice Mayne, Majambu Mbikay, John Woulfe, and Michel Chrétien. "Expression of PCSK1 (PC1/3), PCSK2 (PC2) and PCSK3 (furin) in mouse small intestine." Regulatory Peptides 152, no. 1-3 (January 2009): 54–60. http://dx.doi.org/10.1016/j.regpep.2008.07.006.
Xu, Xu, Egor Volcotrub, and Svetlana B. Ten. "LBSUN131 Leptin Level, BMI And Genetics In Early Onset Obesity." Journal of the Endocrine Society 6, Supplement_1 (November 1, 2022): A5. http://dx.doi.org/10.1210/jendso/bvac150.009.
Clément, Karine, Martin Wabitsch, Erica Van den Akker, Jesús Argente, Ceclila Scimia, Madhura Srinivasan, Guojun Yuan, and Peter Kühnen. "ODP607 Long-term Efficacy of Setmelanotide in Patients With POMC or LEPR Deficiency Obesity." Journal of the Endocrine Society 6, Supplement_1 (November 1, 2022): A14—A15. http://dx.doi.org/10.1210/jendso/bvac150.030.
Aerts, Laetitia, Nathalie A. Terry, Nina N. Sainath, Clarivet Torres, Martín G. Martín, Bruno Ramos-Molina, and John W. Creemers. "Novel Homozygous Inactivating Mutation in the PCSK1 Gene in an Infant with Congenital Malabsorptive Diarrhea." Genes 12, no. 5 (May 10, 2021): 710. http://dx.doi.org/10.3390/genes12050710.
Velazquez-Roman, Jorge, Uriel A. Angulo-Zamudio, Nidia Leon-Sicairos, Hector Flores-Villaseñor, Miriam Benitez-Baez, Ana Espinoza-Salomón, Alejandra Karam-León, et al. "Association of PCSK1 and PPARG1 Allelic Variants with Obesity and Metabolic Syndrome in Mexican Adults." Genes 14, no. 9 (September 8, 2023): 1775. http://dx.doi.org/10.3390/genes14091775.
Ayers, Kristin L., Benjamin S. Glicksberg, Alastair S. Garfield, Simonne Longerich, Joseph A. White, Pengwei Yang, Lei Du, et al. "Melanocortin 4 Receptor Pathway Dysfunction in Obesity: Patient Stratification Aimed at MC4R Agonist Treatment." Journal of Clinical Endocrinology & Metabolism 103, no. 7 (May 2, 2018): 2601–12. http://dx.doi.org/10.1210/jc.2018-00258.
Van Dijck, Evelien, Sigri Beckers, Sara Diels, Tammy Huybrechts, An Verrijken, Kim Van Hoorenbeeck, Stijn Verhulst, Guy Massa, Luc Van Gaal, and Wim Van Hul. "Rare Heterozygous PCSK1 Variants in Human Obesity: The Contribution of the p.Y181H Variant and a Literature Review." Genes 13, no. 10 (September 27, 2022): 1746. http://dx.doi.org/10.3390/genes13101746.
Morash, Michael G., Angela B. MacDonald, Roger P. Croll, and Younes Anini. "Molecular cloning, ontogeny and tissue distribution of zebrafish (Danio rerio) prohormone convertases: pcsk1 and pcsk2." General and Comparative Endocrinology 162, no. 2 (June 2009): 179–87. http://dx.doi.org/10.1016/j.ygcen.2009.03.013.
Sanders, SS. "PCSK1 variants: genetic risk factors for obesity." Clinical Genetics 75, no. 4 (April 2009): 318–19. http://dx.doi.org/10.1111/j.1399-0004.2009.01171_1.x.
Дисертації з теми "PCSK1":
Choquet, Hélène. "Contribution du gène PCSK1 aux formes monogéniques et polygéniques d'obésité." Phd thesis, Université du Droit et de la Santé - Lille II, 2010. http://tel.archives-ouvertes.fr/tel-00576415.
Choquet, Hélène. "Contribution du gène PCSK1 aux formes monogéniques et polygéniques d’obésité." Thesis, Lille 2, 2010. http://www.theses.fr/2010LIL2S012/document.
Four whole genome studies basing on positional cloning approach revealed a region ofchromosome 5q linked to traits related to obesity, this region contained the gene coding forthe prohormone convertase 1 named PCSK1. Pc1 mutation in mice has been associated withobesity, hyperphagia and increased metabolic efficiency. In human, PCSK1 deficiency is amonogenic form of obesity. The first case of complete PCSK1 deficiency has been identifiedin 1997 and since two other cases were discovered. Deleterious PCSK1 mutations carrierswere either homozygous or compound heterozygous and presented severe phenotypes, such asobesity, intestinal troubles and endocrine disorders. Surprisingly, the family members whowere heterozygous for these mutations appeared clinically unaffected. Overall of these studieshighlighted PCSK1 as a candidate gene for obesity.We have therefore decided to assess the contribution of PCSK1 gene to polygenicobesity risk. To assess the contribution of PCSK1 to polygenic obesity risk, we genotyped tagsingle nucleotide polymorphisms in a total of 13,659 European individuals from eightindependent case-control or family-based cohorts. The non-synonymous variants rs6232,encoding N221D, and cluster rs6234-rs6235, encoding the Q665E-S690T pair, wereconsistently associated with obesity in adults and children (P=7.27 x 10-8 and P=2.31 x 10-12,respectively). Functional analysis revealed a significant impairment of the N221D mutant onPC1/3 protein catalytic activity.In continuity of this study we decided to assess the involvement of PCSK1 gene inmonogenic obesity, knowing that only three cases of complete PCSK1 deficiency have beenreported up to now. The objectives of this study were to evaluate the prevalence of rarePCSK1 mutations contributing to human obesity and to investigate the mode of inheritance ofobesity in the context of PCSK1 deficiency. We sequenced exons of the PCSK1 gene in 845non-consanguineous extremely obese subjects of European origin and we identified eightnovel PCSK1 non-synonymous mutations in eight carriers, all heterozygous. Wecharacterized the functional consequences of the detected mutations on PC1/3 protein and wefound that 62.5% of mutations detected were predicted to be deleterious in silico and werevealed that 87.5% of mutations had an effect on the autoactivation or on the enzymaticactivity of PC1/3 in vitro. In order to estimate the degree of penetrance for the sevenpathogenic mutations, we genotyped 6,060 obese and 6,274 lean subjects. We assessed a 6-fold enrichment of these PCSK1 mutations in obese subjects (P = 0.007). We provided thefirst evidence of an increased obesity risk in heterozygous carriers of loss of functionmutations in PCSK1 gene, confirming a co-dominant mode of transmission of obesity withincomplete penetrance for this gene. The penetrance of obesity was estimated to 54.5% for108heterozygous carriers of deleterious PCSK1 mutations. Partial PCSK1 deficiency mightexplain ~ 0.83% of extreme obesity.To conclude, in addition of the syndromic forms of obesity due to a complete PCSK1deficiency, we provided the strong evidence of the contribution of common non-synonymousvariants in obesity risk and we highlighted that a partial PCSK1 deficiency is associated withan increased risk of obesity
Guerardel, Audrey. "Analyse de deux gènes candidats physiologiques et positionnels de l'obésité humaine CART et PCSK1." Lille 2, 2005. http://www.theses.fr/2005LIL2S012.
Common obesity is a multifactorial disease, whose recent increase, is related to the modernization of life. This epidemic is the consequence of a physical inactivity and an unlimited access to over-nutrition and consumption of caloric food. Nevertheless, many familial studies and the identification of monogenic forms of obesity indicate that genetic factors are also involved. All determinants of the polygenic forms are still unknown, recent studies show the role of genes in the signalling of insulin (ENPP1) and metabolic pathways of neurotransmitters (GABA, serotonin) which would predispose to obesity in a sedentary, high calorie lifestyle. The identification of genetic factors in the polygenic diseases such as obesity is assessed by direct studies of physiological genes and by indirect analyses with positional candidate genes located in chromosomal regions of linkage to phenotype traits. Two genome wide-scans on French Caucasian families show the importance of the locus 5cen-q. Among many genes located in this region ; CART (5q12-q13) and PCSK1 (5q15-q21) genes are expressed in the central nervous system (principally in the hypothalamus) and are involved in the control of food intake and the regulation of energy homeostasis. The analysis of a 5,4 Kb region of the CART gene (Cocaine and Amphetamine Regulated Transcript), including the promoter, 3 exons, introns and the 3'UTR, resulted in the identification of a promoter SNP (SNP-3608T>C) which is associated with the polygenic obesity. In a general population, this polymorphism is also associated, with subfractions of plasma cholesterol and apolipoproteins which suggests that the CART gene maybe implicated in lipid metabolism and atherogenesis. Within a Danish study of menopausal women, the SNP-3608T>C was shown to effect remodelling of the bone mass (on arm BMD). PCSK1 (Proprotein Convertase Subtilisin/kexin type 1) Gene code for a neuroendocrine member of the family of subtilisin-like proprotein convertases and is important for the maturation of pro-hormones and neuropeptides precursors such as the proinsulin and POMC. PCSK1 gene mutations are responsible for a number of rare monogenic forms of severe obesity. The analysis of this gene in a polygenic context enabled the identification of frequent mutations including a non-synonymous exonic variant which is associated with adult and/or childhood polygenic obesity. The genetic approach validates physiological hypotheses and improves current understanding of metabolic pathways, and suggests a pleiotropic effect of the CART gene and that the CART and PCSK1 genes are implicated in polygenic obesity
Folon, Lise. "Étude de l'impact des variants génétiques rares sur l'obésité monogénique." Electronic Thesis or Diss., Université de Lille (2022-....), 2023. https://pepite-depot.univ-lille.fr/ToutIDP/EDBSL/2023/2023ULILS059.pdf.
Obesity is a complex multifactorial disease with a strong genetic component. Unlike common obesity, which is a polygenic disease, monogenic forms of obesity are caused by a single rare genetic variant with a strong and deleterious effect. These monogenic forms are rare, early-onset and generally very severe, affecting around 5% of individuals with obesity. Most rare mutations associated with monogenic obesity are found in genes within the leptin-melanocortin pathway, which is crucial for the regulation of food intake. Identifying these genes is crucial for understanding the pathophysiology of obesity and developing new treatments.I initially studied rare heterozygous variants of the PCSK1 gene, which encodes the prohormone convertase 1 (PC1/3) enzyme. PC1/3 is involved in the leptin-melanocortin pathway. Biallelic mutations in PCSK1 cause early-onset obesity with severe endocrinopathy. Patients with PCSK1 deficiency (heterozygous or homozygous) can now be treated with setmelanotide injections to promote weight loss. However, the impact of rare heterozygous variants of PCSK1 on obesity and their relevance in precision medicine are still not well-defined. In the RaDiO study, which included 9,320 participants, 65 rare heterozygous variants of PCSK1 were identified and assessed in vitro. These variants were classified into five groups based on the severity of their impact on the enzymatic activity of PC1/3. Association analysis results revealed that rare variants inducing a complete loss of function significantly increased the risk of obesity and body mass index (BMI), whereas variants in other groups with partial or neutral effects on PC1/3 activity had no impact on adiposity. We observed that in silico prediction tools were unreliable in detecting mutations leading to a complete loss of function.Subsequently, I focused on rare variants of the DYRK1B gene. Although this gene is not directly involved in the leptin-melanocortin pathway, pathogenic variants of DYRK1B have been described in several patients with central obesity, type 2 diabetes (T2D), and coronary artery disease. However, the impact of rare DYRK1B variants has not been assessed on a large scale. In the RaDiO study, which included 9,353 participants, 65 rare variants in DYRK1B were detected. Following in vitro analysis of each variant, we identified 20 pathogenic or likely pathogenic variants (P/LP) according to the criteria of the American College of Medical Genetics and Genomics. Among these P/LP variants, six showed an effect leading to a complete loss of function of DYRK1B (P/LP-full). Association analyses showed that P/LP-full variants of DYRK1B were strongly associated with increased BMI and fasting glucose levels, as well as a heightened risk of obesity and T2D, whereas P/LP variants had only a modest effect on adiposity and no impact on glucose homeostasis.In conclusion, the use of functional genetics has demonstrated that only heterozygous variants of PCSK1 and DYRK1B with a complete loss of function cause monogenic obesity. For DYRK1B, obesity is additionally associated with T2D. These results underscore the critical significance of assessing the functional impact of mutations in vitro for genetic diagnosis and the potential selection of appropriate treatments. We have demonstrated that in silico prediction tests are currently not precise enough
Bhat, Mamatha. "Expression of PCSK9 in Hepatocellular Carcinoma." Thesis, McGill University, 2012. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=106271.
Contexte et hypothèses: Le carcinome hépatocellulaire (CHC) est le 5e cancer le plus courant dans le monde entier et la 3ème cause de décès par cancer dans le monde entier, avec une survie médiane à 5 ans de 8,9%. La reconnaissance tardive en raison du manque de biomarqueurs pour détecter la maladie résécable, une résistance aux agents anticancéreux, ainsi qu'une maladie du foie sous-jacente limitant l'utilisation de chimiothérapie hépatotoxique sont des facteurs qui diminuent le taux de survie. Les proprotéines convertases (PCs) sont des sérine-protéases qui convertissent une variété de facteurs de croissance, glycoprotéines de surface cellulaire, les récepteurs, et les métalloprotéinases à leurs formes actives, contrôlant ainsi l'activité biologique de ces protéines. On a démontré l'expression augmentée de PCs dans de diverses tumeurs malignes. On a prouvé que les facteurs de croissance impliqués dans le CHC, tels que l'IGF-1, HGF, VEGF et PDGF, sont convertis à leurs forme actives par les PC. Notre hypothèse est que l'expression de proprotéines convertases est élevée dans le CHC, permettant l'activation de différentes protéines essentielles dans le développement et la progression du CHC. L'objectif de recherche était d'évaluer l'expression des PCs PCSK9, furine et PC5 dans le CHC par rapport aux stroma environnant, zones péri-cirrhotiques, et foie normal afin de déterminer si un gradient d'expression existe. PCSK9 en particulier est connu comme étant plus exprimé chez le foie régénérateur post-hepatectomie. Les diapositives de pathologie de CHC stockés dans le département de pathologie du CUSM ont été examinés par une pathologiste, et les zones appropriées (tumeur de CHC, interface de tumeur et du foie, le foie cirrhotique, et d'autres échantillons d'hépatite et de foie normal) dans les blocs de tissu correspondants ont été creusés et ont été incorporées dans un microarray de tissu (TMA). Des lignes cellulaires de CHC etablies, dont le HepG2 et le Huh7, avec des profils d'expression de PC connus, ont été incorporées sous forme de pastilles de cellules dans la TMA, afin de servir de témoins positifs et négatifs. La TMA a été sectionnée en diapositives, qui ont été colorées avec des anticorps de la PCSK9, furine et PC5. On a découvert que le niveau d'expression de PCSK9 était diminuée dans les CHC avec un pire prognostique. L'expression augmentée de PCSK9 dans les CHC plus aggressifs pourrait indiquer un rôle du PCSK9 dans la tumorigenèse, directement ou indirectement. Il se peut que les CHCs plus aggressifs sont capables de modifier l'environnement local pour apprivoiser l'énergie métabolique, et que le PCSK9 permet que le cholestérol soit utilisé comme source d'énergie. La confirmation de son importance fonctionnelle avec mRNA pourrait potentiellement mener au développement de chimiothérapie ciblée avec des anticorps contre le PCSK9 (stratégie en étude pour l'hypercholestérolémie). Compte tenu des options chimiothérapeutiques actuellement limitées pour le CHC, une telle constatation pourrait améliorer la prise en charge clinique du CHC.
DA, DALT LORENZO. "IMPACT OF PCSK9 ON EXTRAHEPATIC TISSUES." Doctoral thesis, Università degli Studi di Milano, 2021. http://hdl.handle.net/2434/813080.
Background and Aim: Proprotein convertase subtilisin Kexin type 9 (PCSK9) is a 692-amino acid glycoprotein that belongs to the family of proprotein convertases. It is produced mainly by the liver and secreted into the circulation. PCSK9 interacts with several receptors of the LDLr family, including VLDLr, LRP1 but also with CD36, and drives their degradation in the lysosome. As a consequence, PCSK9 deficiency results in increased expression of LDLr family receptors and favors lipid accumulation in extrahepatic tissues. Lipids overload is associated with mitochondrial dysfunction and tissue damage in different organs including the pancreas and the heart. We wondered whether the lack of both circulating and locally produced PCSK9 may affect lipid accumulation on extrahepatic tissues such as the pancreas and the heart those affecting their functionality. Methods: 2-months old WT, Pcsk9 KO, Albumin CRE PCSK9LoxP/LoxP conditional KO (lacking PCSK9 production selectively in the liver and thus presenting undetectable PCSK9 protein in the circulation) and Double KO LDLr-Pcsk9 male mice were fed for 20 weeks with SFD or HFD. GTT, ITT, insulin and C-peptide plasma levels, pancreas morphology, and cholesterol accumulation in pancreatic islets were studied in the different animal models. Moreover, echocardiographic analysis of the heart and functional tests were performed on these mice. Mitochondrial respiration was investigated under resting conditions and following maximal coupling and uncoupling conditions in all mice models followed by mitochondrial protein profiling by western blotting and extensive metabolomic analysis. Results: Glucose clearance was significantly reduced in Pcsk9 KO mice fed with a standard or a high-fat diet for 20 weeks compared with WT animals; insulin sensitivity, however, was not affected. A detailed analysis of pancreas morphology of Pcsk9 KO mice vs. controls revealed larger islets with increased accumulation of cholesteryl esters, paralleled by increased insulin intracellular levels and decreased plasma insulin, and C-peptide levels. This phenotype was completely reverted in Pcsk9/Ldlr DKO mice implying that increased LDLR could explain the phenotype observed. Of note mice lacking circulating PCSK9 did not present an impaired phenotype, thus indicating that circulating, liver-derived PCSK9 does not impact beta-cell function and insulin secretion. In parallel, a detailed characterization of heart function revealed that Pcsk9 KO displays a phenotype characteristic of heart failure with preserved ejection fraction. Moreover, PCSK9 KO mice present a reduced running resistance without muscular defects coupled to major adaptations in cardiac metabolism and mitochondrial functionality due to heart cholesterol accumulation. A similar phenotype was observed in LDLr Double KO confirming an effect independent of LDLr expression. The cardiac phenotype is completed reverted in the liver selective KO model thus excluding the involvement of circulating PCSK9 in the development of Heart Failure with preserved Ejection Fraction. Translational studies showed that human subjects carrying the R46L loss of function polymorphism displayed increased left ventricular mass without alterations in ejection fraction compared to R46R BMI-matched controls. Conclusion/Discussion: PCSK9 locally produced in the pancreas and the heart affects limits lipid accumulation in an LDLr dependent manner in the pancreas and an LDLr independent manner in the heart thus contributing to maintaining tissue homeostasis. Genetic PCSK9 deficiency leads to the development of glucose intolerance and heart failure with preserved ejection fraction in mice models and humans.
Stefan, Elias. "Familjär hyperkolesterolemi (FH) – analys av prevalens i Stockholm och hälsoekonomiska konsekvenser av tidigdiagnostik och behandling." Thesis, Uppsala universitet, Institutionen för farmaci, 2021. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-434844.
Giunzioni, I. "MACROPHAGE EXPRESSION OF PCSK9 INFLUENCES ATHEROSCLEROSIS DEVELOPMENT." Doctoral thesis, Università degli Studi di Milano, 2014. http://hdl.handle.net/2434/229332.
Kourimate, Sanae. "Pcsk9 : régulation et implication dans le syndrome métabolique." Nantes, 2008. https://archive.bu.univ-nantes.fr/pollux/show/show?id=4ac185ba-f999-45ff-9241-4278a9699b5c.
Proprotein convertase subtilisin/kexin type 9 (PCSK9) is a member of the serine protease family. Gain of function mutations within PCSK9 are associated with dominant forms of familial hypercholesterolemia. Inversely, humans harbouring loss of function mutations have a significant plasma LDLc reduction and a 88% decrease of the risk of coronary heart disease. In the endoplasmic reticulum Pro-PCSK9 undergoes an autocalytique clivage that is crucial for its secretion. Then, this secreted protein binds to the EGF-A domain of the LDLR and targets it to the lysosomes rather than to the cell surface. Both PCSK9 and the LDLR are up-regulated by statins via SREBP2. Using PCSK9 inhibitors may optimize the effects of this hypocholesterolemic drug. The first aim of my thesis was to investigate in vitro the mechanisms of PCSK9 repression by the fibrates which are PPARα synthetic agonists. Activation of PPARα down-regulates PCSK9 transcription at the promoter level and increase the expression of two others Proprotein convertases: furin and PC5/6A which are known to degrade PCSK9. Fibrates counteracts PCSK9 induction by statins and amplifies the effects of this hypocholesterolemic drugs on the LDLR acitivity. The second part of my studies was based on measuring the endogenous cleavage activity of PCSK9, using a fluorogenic peptide corresponding to the cleavage site of Pro-PCSK9. After validation of the specificity of this assay on mice primary hepatocytes from PCSK9-/-, I applied it to the test of several PCSK9 variants. The final part of my studies dealt about the characterisation of PCSK9 expression in diabetic and insulin resistant animal models. PCSK9 is an attractive therapeutic target for lowering plasma LDLc levels. This study clearly showed that PCSK9 transcriptional inhibition by fibrates might be envisaged in combination with statins. However, in vivo, in humans, the fibrates are rather known for their hypotriglyceridemic properties. The limited effect of fibrates on lowering LDLc might be explained by a counteracting pathway. Identifying this pathway is one of the promising perspectives of this thesis
CANCLINI, LAURA. "PROPROTEIN CONVERTASE SUBTILISIN/KEXIN TYPE 9 PREFERENTIALLY ASSOCIATES WITH A SPECIFIC LDL SUBFRACTION: A DETAILED CHARACTERIZATION AND STUDY OF THE EFFECTS OF ANTI-PCSK9 MABS TREATMENT." Doctoral thesis, Università degli Studi di Milano, 2022. https://hdl.handle.net/2434/947250.
Книги з теми "PCSK1":
Gessner-Ulrich, Katrin. Untersuchungen zur Expression und Funktion des linearen, mitochondrialen Plasmides pC1K1 von Claviceps purpurea. Berlin: J. Cramer, 1992.
Xu, Weiming. New Cardiovascular Research: PCSK9 As a New Therapeutic Target for Cardiovascular Disease. Independently Published, 2021.
Atta-ur-Rahman and M. Iqbal Choudhary, eds. Frontiers in Cardiovascular Drug Discovery: Volume 4. BENTHAM SCIENCE PUBLISHERS, 2019. http://dx.doi.org/10.2174/97816810839951180401.
Частини книг з теми "PCSK1":
Choquet, Hélène, Pieter Stijnen, and John W. M. Creemers. "Genetic and Functional Characterization of PCSK1." In Methods in Molecular Biology, 247–53. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-204-5_13.
Wright, R. Scott. "PCSK9 Inhibiting siRNA." In Stroke Revisited: Dyslipidemia in Stroke, 135–43. Singapore: Springer Singapore, 2021. http://dx.doi.org/10.1007/978-981-16-3923-4_12.
Ahmed, Zain, Prerak Juthani, Megan Lee, and Nihar R. Desai. "PCSK9 Inhibiting Monoclonal Antibodies." In Stroke Revisited: Dyslipidemia in Stroke, 125–33. Singapore: Springer Singapore, 2021. http://dx.doi.org/10.1007/978-981-16-3923-4_11.
Desnick, Robert J., Orlando Guntinas-Lichius, George W. Padberg, Gustav Schonfeld, Xiaobo Lin, Maurizio Averna, Pin Yue, et al. "FHBL due to Defective PCSK9." In Encyclopedia of Molecular Mechanisms of Disease, 653. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-29676-8_8889.
Wang, Zuo, Zhi-Han Tang, Yun-Chen Lv, Lu-Shan Liu, and Zhi-Sheng Jiang. "Bioinformatic Analysis of PCSK9 Related Caspase3 Activation." In Recent Advances in Computer Science and Information Engineering, 527–33. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-642-25778-0_73.
Ooi, Teik Chye, and Hussein Abujrad. "PCSK9 as a Biomarker of Cardiovascular Disease." In Biomarkers in Cardiovascular Disease, 125–51. Dordrecht: Springer Netherlands, 2016. http://dx.doi.org/10.1007/978-94-007-7678-4_20.
Ooi, Teik Chye, and Hussein Abujrad. "PCSK9 as a Biomarker of Cardiovascular Disease." In Biomarkers in Cardiovascular Disease, 1–27. Dordrecht: Springer Netherlands, 2015. http://dx.doi.org/10.1007/978-94-007-7741-5_20-1.
Farnier, Michel. "Statins and PCSK9 Inhibitors: Defining the Correct Patients." In Combination Therapy In Dyslipidemia, 99–117. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-20433-8_9.
Innocenti, Francesca, Valentina Di Maria, Alice Poggi, and Riccardo Pini. "Biomarkers of Sepsis and a Focus on PCSK9." In Biomarkers in Trauma, Injury and Critical Care, 1–28. Cham: Springer International Publishing, 2022. http://dx.doi.org/10.1007/978-3-030-87302-8_40-1.
Innocenti, Francesca, Valentina Di Maria, Alice Poggi, and Riccardo Pini. "Biomarkers of Sepsis and a Focus on PCSK9." In Biomarkers in Trauma, Injury and Critical Care, 785–812. Cham: Springer International Publishing, 2023. http://dx.doi.org/10.1007/978-3-031-07395-3_40.
Тези доповідей конференцій з теми "PCSK1":
Sha, Xiangtong, and Yueqiang Wang. "PCSK1 Variants and Obesity: Relationship in Different Population." In 2021 International Conference on Public Art and Human Development ( ICPAHD 2021). Paris, France: Atlantis Press, 2022. http://dx.doi.org/10.2991/assehr.k.220110.187.
Vistica, David T., Susan Kenney, Dominic A. Scudiero, Russell A. Reinhart, Michael H. Selby, Donna O. Butcher, and Robert H. Shoemaker. "Abstract 1621: The proprotein convertase PCSK1 is a novel drug target in alveolar soft part sarcoma (ASPS)." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-1621.
Tent, Michiel. "Oral PCSK9 inhibitor significantly lowers LDL-C." In ACC 2023 Scientific Session, edited by Marc Bonaca. Baarn, the Netherlands: Medicom Medical Publishers, 2023. http://dx.doi.org/10.55788/629cbf29.
Martin Plagaro, Cesar, Kepa B. Uribe, Asier Benito Vicente, Rocio Alonso Estraba, Unai Galicia Garcia, Shifa Jebari Benslaiman, and Asier Larrea Sebal. "Hiperkolesterolemia Familiarra: PCSK9 aldaeren karakterizazioa tratamendu pertsonalizaturako." In III. Ikergazte. Nazioarteko ikerketa euskaraz. Bilbao: UEU arg, 2019. http://dx.doi.org/10.26876/ikergazte.iii.04.10.
Niemann, B., L. Li, F. Knapp, R. Schulz, and S. Rohrbach. "Modifying Epicardial PCSK9 Expression to Protect Cardiac Function?" In 48th Annual Meeting German Society for Thoracic, Cardiac, and Vascular Surgery. Georg Thieme Verlag KG, 2019. http://dx.doi.org/10.1055/s-0039-1678923.
Ferrer Machín, A., S. Martin Rodriguez, J. Vilar Rodriguez, MDLA Padron Garcia, M. Vera Cabrera, J. Arias Blaco, and MDC Villastrigo Garcia. "4CPS-178 Effect of pcsk9 inhibitors on hypercholesterolemia." In 28th EAHP Congress, Bordeaux, France, 20-21-22 March 2024. British Medical Journal Publishing Group, 2024. http://dx.doi.org/10.1136/ejhpharm-2024-eahp.282.
Lecis, M., E. Viglione, S. Strobino, and G. Ceravolo. "5PSQ-017 PCSK-9 inhibitors: real world effectiveness." In 25th EAHP Congress, 25th–27th March 2020, Gothenburg, Sweden. British Medical Journal Publishing Group, 2020. http://dx.doi.org/10.1136/ejhpharm-2020-eahpconf.334.
Martin, V. Merino, MP Ortega-Garcia, P. Blasco-Segura, J. Sanfeliu Garcia, A. Lopez Carrasco, R. del Rio San Cristobal, and I. Toledo Guasp. "4CPS-035 Effectiveness and safety of monoclonal antibody pcsk9 inhibitors." In Abstract Book, 23rd EAHP Congress, 21st–23rd March 2018, Gothenburg, Sweden. British Medical Journal Publishing Group, 2018. http://dx.doi.org/10.1136/ejhpharm-2018-eahpconf.126.
Ly, Kévin, Anna Kwiatkowska, Sophie Routhier, Roxane Desjardins, Monika Lewandowska, Adam Prahl, Josée Hamelin, Nabil G. Seidah, Yves Dory, and Robert Day. "Development of Peptide Inhibitors Disrupting PCSK9-LDLR Protein-Protein Interactions." In The Twenty-Third American and the Sixth International Peptide Symposium. Prompt Scientific Publishing, 2013. http://dx.doi.org/10.17952/23aps.2013.110.
Sáez Rodríguez, MI, JJ Arenas Villafranca, B. Montero Salgado, PA Chinchurreta Capote, and B. Tortajada Goitia. "4CPS-119 Real-world experience with PCSK9 inhibitors protocol for hypercholesterolaemia." In 26th EAHP Congress, Hospital pharmacists – changing roles in a changing world, 23–25 March 2022. British Medical Journal Publishing Group, 2022. http://dx.doi.org/10.1136/ejhpharm-2022-eahp.146.
Звіти організацій з теми "PCSK1":
Zhang, Lingnan, Fang Zhang, Xinwei Jia, Junmin Xie, Yeran Zhu, Xiaozhe Zhou, and Chang Meng. Targeting PCSK9 in Heterozygous familial hypercholesterolemia: a meta-analysis of randomized controlled trials. INPLASY - International Platform of Registered Systematic Review and Meta-analysis Protocols, March 2024. http://dx.doi.org/10.37766/inplasy2024.3.0095.
Yu, Yani, Lei Chen, Honghong Zhang, Zihao Fu, Qi Liu, Haijing Zhao, Yuqi Liu, and Yundai Chen. Racial differences in the safety and efficacy of PCSK9 inhibitors in the treatment of hyperlipidemia:A Systematic review and meta-analysis. INPLASY - International Platform of Registered Systematic Review and Meta-analysis Protocols, November 2021. http://dx.doi.org/10.37766/inplasy2021.11.0047.
Niu, Xiaowei, and Shuwen Hu. Efficacy and safety of PCSK9 inhibitors and statin lipid-lowering therapy in coronary atherosclerosis: A meta-analysis of randomized trials. INPLASY - International Platform of Registered Systematic Review and Meta-analysis Protocols, December 2022. http://dx.doi.org/10.37766/inplasy2022.12.0019.
Sun, Jing-Chao. The intense lipid-lowering strategies of PCSK9 inhibitor or ezetimibe for cardiovascular events in patients with coronary heart disease: a systemic review and meta-analysis. INPLASY - International Platform of Registered Systematic Review and Meta-analysis Protocols, April 2023. http://dx.doi.org/10.37766/inplasy2023.4.0040.