Zeitschriftenartikel zum Thema „SERPINH1“
Geben Sie eine Quelle nach APA, MLA, Chicago, Harvard und anderen Zitierweisen an
Machen Sie sich mit Top-50 Zeitschriftenartikel für die Forschung zum Thema "SERPINH1" bekannt.
Neben jedem Werk im Literaturverzeichnis ist die Option "Zur Bibliographie hinzufügen" verfügbar. Nutzen Sie sie, wird Ihre bibliographische Angabe des gewählten Werkes nach der nötigen Zitierweise (APA, MLA, Harvard, Chicago, Vancouver usw.) automatisch gestaltet.
Sie können auch den vollen Text der wissenschaftlichen Publikation im PDF-Format herunterladen und eine Online-Annotation der Arbeit lesen, wenn die relevanten Parameter in den Metadaten verfügbar sind.
Sehen Sie die Zeitschriftenartikel für verschiedene Spezialgebieten durch und erstellen Sie Ihre Bibliographie auf korrekte Weise.
Al-Khatib, Sohaib M., Ayah N. Al-Bzour, Mohammad N. Al-Majali, Laila M. Sa’d, Joud A. Alramadneh, Nour R. Othman, Abdel-Hameed Al-Mistarehi und Safwan Alomari. „Exploring Genetic Determinants: A Comprehensive Analysis of Serpin B Family SNPs and Prognosis in Glioblastoma Multiforme Patients“. Cancers 16, Nr. 6 (10.03.2024): 1112. http://dx.doi.org/10.3390/cancers16061112.
Der volle Inhalt der QuelleJin, Xiao-Sheng, Lu-Xi Chen, Ting-Ting Ji und Rong-Zhou Li. „SERPINH1 promoted the proliferation and metastasis of colorectal cancer by activating PI3K/Akt/mTOR signaling pathway“. World Journal of Gastrointestinal Oncology 16, Nr. 5 (15.05.2024): 1890–907. http://dx.doi.org/10.4251/wjgo.v16.i5.1890.
Der volle Inhalt der QuelleHaj, Amelia K., Sean J. Jurgens, Xin Wang, Justine Ryu, Seung Hoan Choi, Steven P. Grover, Simone Sanna-Cherchi, Alec A. Schmaier, Patrick Ellinor und Pavan K. Bendapudi. „Rare Germline Loss-of-Function Variants in HSP47 ( SERPINH1) Are Associated with an Intermediate Osteogenesis Imperfecta Phenotype Characterized By Atopic Inflammation and Increased Risk of Thrombosis“. Blood 142, Supplement 1 (28.11.2023): 3934. http://dx.doi.org/10.1182/blood-2023-189896.
Der volle Inhalt der QuelleMueller, S. K., A. L. Nocera, S. T. Dillon, T. A. Libermann, O. Wendler und B. S. Bleier. „Tissue and Exosomal Serine Protease Inhibitors Are Significantly Overexpressed in Chronic Rhinosinusitis With Nasal Polyps“. American Journal of Rhinology & Allergy 33, Nr. 4 (27.02.2019): 359–68. http://dx.doi.org/10.1177/1945892419831108.
Der volle Inhalt der QuelleZhang, Yin, Chun-Yuan Li, Wei Ge und Yi Xiao. „Exploration of the Key Proteins in the Normal-Adenoma-Carcinoma Sequence of Colorectal Cancer Evolution Using In-Depth Quantitative Proteomics“. Journal of Oncology 2021 (11.06.2021): 1–19. http://dx.doi.org/10.1155/2021/5570058.
Der volle Inhalt der QuelleBertram, Stefanie, Juliet Padden, Julia Kälsch, Maike Ahrens, Leona Pott, Ali Canbay, Frank Weber et al. „Novel immunohistochemical markers differentiate intrahepatic cholangiocarcinoma from benign bile duct lesions“. Journal of Clinical Pathology 69, Nr. 7 (04.01.2016): 619–26. http://dx.doi.org/10.1136/jclinpath-2015-203418.
Der volle Inhalt der QuelleZhang, Yin, Chun-Yuan Li, Meng Pan, Jing-Ying Li, Wei Ge, Lai Xu und Yi Xiao. „Exploration of the Key Proteins of High-Grade Intraepithelial Neoplasia to Adenocarcinoma Sequence Using In-Depth Quantitative Proteomics Analysis“. Journal of Oncology 2021 (29.11.2021): 1–13. http://dx.doi.org/10.1155/2021/5538756.
Der volle Inhalt der Quellevan Leeuwen, L. Leonie, Mitchel J. R. Ruigrok, Henri G. D. Leuvenink und Peter Olinga. „Slice of Life: Porcine Kidney Slices for Testing Antifibrotic Drugs in a Transplant Setting“. Transplantology 4, Nr. 2 (14.04.2023): 59–70. http://dx.doi.org/10.3390/transplantology4020007.
Der volle Inhalt der QuelleBrzhozovskiy, Alexander G., Alexey S. Kononikhin, Lyudmila Ch Pastushkova, Daria N. Kashirina, Maria I. Indeykina, Igor A. Popov, Marc-Antoine Custaud, Irina M. Larina und Evgeny N. Nikolaev. „The Effects of Spaceflight Factors on the Human Plasma Proteome, Including Both Real Space Missions and Ground-Based Experiments“. International Journal of Molecular Sciences 20, Nr. 13 (29.06.2019): 3194. http://dx.doi.org/10.3390/ijms20133194.
Der volle Inhalt der QuelleAl-Khatib, Sohaib, Mohammad Nitham Almajali, Ayah Al-Bzour, Joud Al-Ramadneh, Laila Sa'd und Noor Othman. „Abstract 5594: Exploring genetic determinants: A comprehensive analysis of SERPINB family variants and prognosis in Jordanian glioblastoma multiforme patients“. Cancer Research 84, Nr. 6_Supplement (22.03.2024): 5594. http://dx.doi.org/10.1158/1538-7445.am2024-5594.
Der volle Inhalt der QuelleZhang, Hailin, Xiaodi Yan, Hongmei Gu, Qiang Xue und Xiancheng Liu. „High SERPINH1 expression predicts poor prognosis in lung adenocarcinoma“. Journal of Thoracic Disease 14, Nr. 12 (Dezember 2022): 4785–802. http://dx.doi.org/10.21037/jtd-22-1518.
Der volle Inhalt der QuelleZhang, Shuyuan, Weiwei Zhang, Bin Wu, Liang Xia, Liwen Li, Kai Jin, Yangfan Zou und Caixing Sun. „Hub gene target of glioblastoma: LOX, SERPINH1 and TGFBI“. Medicine 101, Nr. 45 (11.11.2022): e31418. http://dx.doi.org/10.1097/md.0000000000031418.
Der volle Inhalt der QuelleXia, Kezhou, Xinghan Huang, Yingchun Zhao, Isabelle Yang und Weichun Guo. „SERPINH1 enhances the malignancy of osteosarcoma via PI3K-Akt signaling pathway“. Translational Oncology 39 (Januar 2024): 101802. http://dx.doi.org/10.1016/j.tranon.2023.101802.
Der volle Inhalt der QuelleCochran, Blake J., David R. Croucher, Sergei Lobov, Darren N. Saunders und Marie Ranson. „Dependence on Endocytic Receptor Binding via a Minimal Binding Motif Underlies the Differential Prognostic Profiles of SerpinE1 and SerpinB2 in Cancer“. Journal of Biological Chemistry 286, Nr. 27 (23.05.2011): 24467–75. http://dx.doi.org/10.1074/jbc.m111.225706.
Der volle Inhalt der QuelleCharone, Senda, Erika Calvano Küchler, Aline de Lima Leite, Mileni Silva Fernandes, Vinicius Taioqui Pelá, Tatiana Martini, Bárbara Margarido Brondino et al. „Analysis of Polymorphisms in Genes Differentially Expressed in the Enamel of Mice with Different Genetic Susceptibilities to Dental Fluorosis“. Caries Research 53, Nr. 2 (27.08.2018): 228–33. http://dx.doi.org/10.1159/000491554.
Der volle Inhalt der QuelleDrögemüller, Cord, Doreen Becker, Adrian Brunner, Bianca Haase, Patrick Kircher, Frank Seeliger, Michael Fehr, Ulrich Baumann, Kerstin Lindblad-Toh und Tosso Leeb. „A Missense Mutation in the SERPINH1 Gene in Dachshunds with Osteogenesis Imperfecta“. PLoS Genetics 5, Nr. 7 (24.07.2009): e1000579. http://dx.doi.org/10.1371/journal.pgen.1000579.
Der volle Inhalt der QuelleWinkler, Ingrid G., Jean Hendy, Paul Coughlin, Anita Horvath und Jean-Pierre Lévesque. „Serine protease inhibitors serpina1 and serpina3 are down-regulated in bone marrow during hematopoietic progenitor mobilization“. Journal of Experimental Medicine 201, Nr. 7 (28.03.2005): 1077–88. http://dx.doi.org/10.1084/jem.20042299.
Der volle Inhalt der QuelleKranc, Wiesława, Maciej Brązert, Katarzyna Ożegowska, Joanna Budna-Tukan, Piotr Celichowski, Maurycy Jankowski, Artur Bryja et al. „Response to abiotic and organic substances stimulation belongs to ontologic groups significantly up-regulated in porcine immature oocytes“. Medical Journal of Cell Biology 6, Nr. 3 (01.12.2018): 91–100. http://dx.doi.org/10.2478/acb-2018-0015.
Der volle Inhalt der QuelleZapata, Liliana Mejia. „Novel heterozygous mutations in gene SERPINH1 cause autosomal recessive osteogenesis imperfecta type X“. Bone Reports 14 (April 2021): 100994. http://dx.doi.org/10.1016/j.bonr.2021.100994.
Der volle Inhalt der QuelleKishimoto, Yo, Masaru Yamashita, Alice Wei, Yutaka Toya, Shuyun Ye, Christina Kendziorski und Nathan V. Welham. „Reversal of Vocal Fold Mucosal Fibrosis Using siRNA against the Collagen-Specific Chaperone Serpinh1“. Molecular Therapy - Nucleic Acids 16 (Juni 2019): 616–25. http://dx.doi.org/10.1016/j.omtn.2019.04.014.
Der volle Inhalt der QuelleSong, Y., D. Zhao, X. Xu, F. Lv, L. Li, Y. Jiang, O. Wang, W. Xia, X. Xing und M. Li. „Novel compound heterozygous mutations in SERPINH1 cause rare autosomal recessive osteogenesis imperfecta type X“. Osteoporosis International 29, Nr. 6 (09.03.2018): 1389–96. http://dx.doi.org/10.1007/s00198-018-4448-2.
Der volle Inhalt der QuelleTian, Shan, Pailan Peng, Jiao Li, Huan Deng, Na Zhan, Zhi Zeng und Weiguo Dong. „SERPINH1 regulates EMT and gastric cancer metastasis via the Wnt/β-catenin signaling pathway“. Aging 12, Nr. 4 (24.02.2020): 3574–93. http://dx.doi.org/10.18632/aging.102831.
Der volle Inhalt der QuelleBurgener, Sabrina S., Mathias Baumann, Paola Basilico, Eileen Remold-O’Donnell, Ivo P. Touw und Charaf Benarafa. „Myeloid conditional deletion and transgenic models reveal a threshold for the neutrophil survival factor Serpinb1“. Biological Chemistry 397, Nr. 9 (01.09.2016): 897–905. http://dx.doi.org/10.1515/hsz-2016-0132.
Der volle Inhalt der QuelleAlhalabi, O., M. Göttmann, M. Gold, M. Fletcher, T. Hielscher, M. Iskar, T. Kessler et al. „P04.04 Optimizing dasatinib for glioblastoma treatment“. Neuro-Oncology 23, Supplement_2 (01.09.2021): ii19. http://dx.doi.org/10.1093/neuonc/noab180.061.
Der volle Inhalt der QuelleHuang, H., T. Chen, L. Zhen, L. Yiming, P. Shengmeng, C. Yongming, L. Lingfeng, Z. Jie und G. Zhenghui. „Mechanism of SERPINH1 in promoting bone metastasis of prostate cancer by inhibiting P62 ubiquitination degradation“. European Urology 83 (Februar 2023): S1661. http://dx.doi.org/10.1016/s0302-2838(23)01186-7.
Der volle Inhalt der QuelleSivaprasad, Umasundari, Kayla Kinker, Aaron Gibson, Stacey Bass, Nicolas Hershey, Jocelyn Biagini Myers, Melinda Butsch Kovacic, Lisa Martin und Gurjit Khurana Hershey. „Role of SERPINB3, SERPINB4, and their mouse homolog Serpinb3a in allergen-induced cutaneous inflammation. (P3347)“. Journal of Immunology 190, Nr. 1_Supplement (01.05.2013): 210.5. http://dx.doi.org/10.4049/jimmunol.190.supp.210.5.
Der volle Inhalt der QuelleGajewski, T., Y. Zha, B. Thurner und G. Schuler. „Association of gene expression profile in metastatic melanoma and survival to a dendritic cell-based vaccine“. Journal of Clinical Oncology 27, Nr. 15_suppl (20.05.2009): 9002. http://dx.doi.org/10.1200/jco.2009.27.15_suppl.9002.
Der volle Inhalt der QuelleKamikawaji, Kazuto, Naohiko Seki, Masaki Watanabe, Hiroko Mataki, Tomohiro Kumamoto, Koichiro Takagi, Keiko Mizuno und Hiromasa Inoue. „Regulation of LOXL2 and SERPINH1 by antitumor microRNA-29a in lung cancer with idiopathic pulmonary fibrosis“. Journal of Human Genetics 61, Nr. 12 (04.08.2016): 985–93. http://dx.doi.org/10.1038/jhg.2016.99.
Der volle Inhalt der QuelleRazali, Nurhanani, Azlina Abdul Aziz, Chor Yin Lim und Sarni Mat Junit. „Investigation into the effects of antioxidant-rich extract ofTamarindus indicaleaf on antioxidant enzyme activities, oxidative stress and gene expression profiles in HepG2 cells“. PeerJ 3 (01.10.2015): e1292. http://dx.doi.org/10.7717/peerj.1292.
Der volle Inhalt der QuelleKantaputra, Piranit, Teerada Daroontum, Mati Chuamanochan, Suteeraporn Chaowattanapanit, Salin Kiratikanon, Charoen Choonhakarn, Worrachet Intachai et al. „SERPINB3, Adult-Onset Immunodeficiency, and Generalized Pustular Psoriasis“. Genes 14, Nr. 2 (19.01.2023): 266. http://dx.doi.org/10.3390/genes14020266.
Der volle Inhalt der QuelleFazlic, M., R. Fairclough, S. Fraser, R. Young, G. Jenkin, M. Knight und M. McDonagh. „434. Identification of differentially expressed proteins in ovine chorion rupture sites at preterm and term using proteomics“. Reproduction, Fertility and Development 20, Nr. 9 (2008): 114. http://dx.doi.org/10.1071/srb08abs434.
Der volle Inhalt der QuelleKawagoe, Kosuke, Masumi Wada, Tetsuya Idichi, Reona Okada, Yasutaka Yamada, Shogo Moriya, Keishi Okubo et al. „Regulation of aberrantly expressed SERPINH1 by antitumor miR-148a-5p inhibits cancer cell aggressiveness in gastric cancer“. Journal of Human Genetics 65, Nr. 8 (31.03.2020): 647–56. http://dx.doi.org/10.1038/s10038-020-0746-6.
Der volle Inhalt der QuelleMarshall, Charlotte, Jaime Lopez, Laura Crookes, Rebecca C. Pollitt und Meena Balasubramanian. „A novel homozygous variant in SERPINH1 associated with a severe, lethal presentation of osteogenesis imperfecta with hydranencephaly“. Gene 595, Nr. 1 (Dezember 2016): 49–52. http://dx.doi.org/10.1016/j.gene.2016.09.035.
Der volle Inhalt der QuellePomerleau, V., V. Reyes-Nicolas, C. Jurkovic, F. Boisvert und N. Perreault. „A7 FOXL1+ TELOCYTES IN MOUSE COLON ORCHESTRATE ECM BIODYNAMICS AND WOUND REPAIR RESOLUTION“. Journal of the Canadian Association of Gastroenterology 5, Supplement_1 (21.02.2022): 8–9. http://dx.doi.org/10.1093/jcag/gwab049.006.
Der volle Inhalt der QuelleCrawford, Andrew A., Sean Bankier, Elisabeth Altmaier, Catriona L. K. Barnes, David W. Clark, Raili Ermel, Nele Friedrich et al. „Variation in the SERPINA6/SERPINA1 locus alters morning plasma cortisol, hepatic corticosteroid binding globulin expression, gene expression in peripheral tissues, and risk of cardiovascular disease“. Journal of Human Genetics 66, Nr. 6 (20.01.2021): 625–36. http://dx.doi.org/10.1038/s10038-020-00895-6.
Der volle Inhalt der QuelleWidmer, C., J. M. Gebauer, E. Brunstein, S. Rosenbaum, F. Zaucke, C. Drogemuller, T. Leeb und U. Baumann. „Molecular basis for the action of the collagen-specific chaperone Hsp47/SERPINH1 and its structure-specific client recognition“. Proceedings of the National Academy of Sciences 109, Nr. 33 (30.07.2012): 13243–47. http://dx.doi.org/10.1073/pnas.1208072109.
Der volle Inhalt der QuelleHaj, A., S. Jurgens, X. Wang, J. Ryu, S. Choi, S. Grover, P. Ellinor und P. Bendapudi. „LB 01.4 Rare Germline Loss of Function Variants in SERPINH1 (HSP47) are Associated with Increased Risk of Thrombosis“. Research and Practice in Thrombosis and Haemostasis 7 (Oktober 2023): 100291. http://dx.doi.org/10.1016/j.rpth.2023.100291.
Der volle Inhalt der QuelleZvereff, Val, Azza Abd El Moneim Attia, Amal Al Tenaiji, Sana Islam, Anushree Dileep und Shalini Behl. „P699: Identification of a novel pathogenic variant in SERPINH1 associated with a presentation of osteogenesis imperfecta: Case study“. Genetics in Medicine Open 2 (2024): 101603. http://dx.doi.org/10.1016/j.gimo.2024.101603.
Der volle Inhalt der QuelleMarques, Patrícia Isabel, Zélia Ferreira, Manuella Martins, Joana Figueiredo, Diana Isabel Silva, Patrícia Castro, Ramiro Morales-Hojas, Joana Simões-Correia und Susana Seixas. „SERPINA2 Is a Novel Gene with a Divergent Function from SERPINA1“. PLoS ONE 8, Nr. 6 (24.06.2013): e66889. http://dx.doi.org/10.1371/journal.pone.0066889.
Der volle Inhalt der QuelleKloth, JN, A. Gorter, GJ Fleuren, J. Oosting, S. Uljee, N. ter Haar, EJ Dreef, GG Kenter und ES Jordanova. „Elevated expression of SerpinA1 and SerpinA3 in HLA-positive cervical carcinoma“. Journal of Pathology 215, Nr. 3 (Juli 2008): 222–30. http://dx.doi.org/10.1002/path.2347.
Der volle Inhalt der QuelleLi, Mengdi, Shuheng Huang, Yong Zhang, Zhi Song, Haijun Fu, Zhengmei Lin und Xin Huang. „Regulation of the unfolded protein response transducer IRE1α by SERPINH1 aggravates periodontitis with diabetes mellitus via prolonged ER stress“. Cellular Signalling 91 (März 2022): 110241. http://dx.doi.org/10.1016/j.cellsig.2022.110241.
Der volle Inhalt der QuelleWu, Gang, Xueming Ju, Youyu Wang, Zhixi Li und Xianfeng Gan. „Up-regulation of SNHG6 activates SERPINH1 expression by competitive binding to miR-139-5p to promote hepatocellular carcinoma progression“. Cell Cycle 18, Nr. 16 (01.07.2019): 1849–67. http://dx.doi.org/10.1080/15384101.2019.1629772.
Der volle Inhalt der QuelleWang, Yanni, Zhe Liu, Zhen Li, Haina Shi, Yujun Kang, Jianfu Wang, Jinqiang Huang und Li Jiang. „Effects of heat stress on respiratory burst, oxidative damage and SERPINH1 (HSP47) mRNA expression in rainbow trout Oncorhynchus mykiss“. Fish Physiology and Biochemistry 42, Nr. 2 (27.11.2015): 701–10. http://dx.doi.org/10.1007/s10695-015-0170-6.
Der volle Inhalt der QuelleBostanci, Mehmet Suhha, Merih Bayram, Suleyman Murat Bakacak, Ozge Kizilkale Yildirim, Rukset Attar, Gazi Yildirim, Emin Umit Bagriacik und Baran Celtemen. „The role of TWIST, SERPINB5, and SERPIN1 genes in uterine leiomyomas“. Journal of the Turkish German Gynecological Association 15, Nr. 2 (16.06.2014): 92–95. http://dx.doi.org/10.5152/jtgga.2014.13005.
Der volle Inhalt der QuelleChristiansen, Helena E., Ulrike Schwarze, Shawna M. Pyott, Abdulrahman AlSwaid, Mohammed Al Balwi, Shatha Alrasheed, Melanie G. Pepin, Mary Ann Weis, David R. Eyre und Peter H. Byers. „Homozygosity for a Missense Mutation in SERPINH1, which Encodes the Collagen Chaperone Protein HSP47, Results in Severe Recessive Osteogenesis Imperfecta“. American Journal of Human Genetics 86, Nr. 3 (März 2010): 389–98. http://dx.doi.org/10.1016/j.ajhg.2010.01.034.
Der volle Inhalt der QuelleWahlmüller, Felix Christof, Barbora Sokolikova, Daniela Rieger und Margarethe Geiger. „New lipid interaction partners stimulate the inhibition of activated protein C by cell-penetrating protein C inhibitor“. Thrombosis and Haemostasis 111, Nr. 01 (2014): 41–52. http://dx.doi.org/10.1160/th13-06-0478.
Der volle Inhalt der QuelleWang, H., S. Parry, G. Macones, M. D. Sammel, H. Kuivaniemi, G. Tromp, G. Argyropoulos et al. „A functional SNP in the promoter of the SERPINH1 gene increases risk of preterm premature rupture of membranes in African Americans“. Proceedings of the National Academy of Sciences 103, Nr. 36 (28.08.2006): 13463–67. http://dx.doi.org/10.1073/pnas.0603676103.
Der volle Inhalt der QuelleLee, Eun-Ju, Daniel Dykas, Allen Bale, Caroline Cromwell, Terri L. Parker, Stephanie Halene, Adrienne Burns, Xiaopan Yao und Alfred I. Lee. „Whole Exome Sequencing in Evaluation of Thrombophilia: A Novel 33-Gene Panel“. Blood 126, Nr. 23 (03.12.2015): 3529. http://dx.doi.org/10.1182/blood.v126.23.3529.3529.
Der volle Inhalt der QuelleBiasiolo, Alessandra, Michele Sandre, Stefania Ferro, Santina Quarta, Mariagrazia Ruvoletto, Gianmarco Villano, Cristian Turato, Maria Guido, Oriano Marin und Patrizia Pontisso. „Epitope-Specific Anti-SerpinB3 Antibodies for SerpinB3 Recognition and Biological Activity Inhibition“. Biomolecules 13, Nr. 5 (25.04.2023): 739. http://dx.doi.org/10.3390/biom13050739.
Der volle Inhalt der QuelleSeo, Yu-Mi, Seok Hwang-Bo, Soo-Ah Im, Myungshin Kim und Young-Ah Youn. „Predictive Value of Heat-Shock Protein Gene Expression on Severe Neonatal Hypoxic-Ischemic Encephalopathy“. Diagnostics 12, Nr. 4 (13.04.2022): 981. http://dx.doi.org/10.3390/diagnostics12040981.
Der volle Inhalt der Quelle