Articles de revues sur le sujet « Pab1 »
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Ardelean, Radu, Adriana Popa, Ecaterina Stela Drăgan, Corneliu-Mircea Davidescu, and Maria Ignat. "New Polymeric Adsorbents Functionalized with Aminobenzoic Groups for the Removal of Residual Antibiotics." Molecules 27, no. 9 (2022): 2894. http://dx.doi.org/10.3390/molecules27092894.
Texte intégralAmirkhosravi, Ali, Todd V. Meyer, Liza Robles-Carrillo та ін. "β2-Glycoprotein 1 Antibodies Directly Activate the Platelet IgG Receptor, FcγRIIa, and Cause Thrombosis in FCGR2A Transgenic but Not in Wild Type Mice". Blood 120, № 21 (2012): 106. http://dx.doi.org/10.1182/blood.v120.21.106.106.
Texte intégralMangus, David A., Nadia Amrani, and Allan Jacobson. "Pbp1p, a Factor Interacting withSaccharomyces cerevisiae Poly(A)-Binding Protein, Regulates Polyadenylation." Molecular and Cellular Biology 18, no. 12 (1998): 7383–96. http://dx.doi.org/10.1128/mcb.18.12.7383.
Texte intégralMangkalaphiban, Kotchaphorn, Robin Ganesan, and Allan Jacobson. "Pleiotropic effects of PAB1 deletion: Extensive changes in the yeast proteome, transcriptome, and translatome." PLOS Genetics 20, no. 9 (2024): e1011392. http://dx.doi.org/10.1371/journal.pgen.1011392.
Texte intégralDufresne, Philippe J., Eliane Ubalijoro, Marc G. Fortin, and Jean-François Laliberté. "Arabidopsis thaliana class II poly(A)-binding proteins are required for efficient multiplication of turnip mosaic virus." Journal of General Virology 89, no. 9 (2008): 2339–48. http://dx.doi.org/10.1099/vir.0.2008/002139-0.
Texte intégralYao, Gang, Yueh-Chin Chiang, Chongxu Zhang, Darren J. Lee, Thomas M. Laue, and Clyde L. Denis. "PAB1 Self-Association Precludes Its Binding to Poly(A), Thereby Accelerating CCR4 Deadenylation In Vivo." Molecular and Cellular Biology 27, no. 17 (2007): 6243–53. http://dx.doi.org/10.1128/mcb.00734-07.
Texte intégralAmrani, N., M. Minet, M. Le Gouar, F. Lacroute, and F. Wyers. "Yeast Pab1 interacts with Rna15 and participates in the control of the poly(A) tail length in vitro." Molecular and Cellular Biology 17, no. 7 (1997): 3694–701. http://dx.doi.org/10.1128/mcb.17.7.3694.
Texte intégralKonopka, Catherine A., Melissa N. Locke, Pamela S. Gallagher, et al. "A yeast model for polyalanine-expansion aggregation and toxicity." Molecular Biology of the Cell 22, no. 12 (2011): 1971–84. http://dx.doi.org/10.1091/mbc.e11-01-0037.
Texte intégralAnderson, J. T., M. R. Paddy, and M. S. Swanson. "PUB1 is a major nuclear and cytoplasmic polyadenylated RNA-binding protein in Saccharomyces cerevisiae." Molecular and Cellular Biology 13, no. 10 (1993): 6102–13. http://dx.doi.org/10.1128/mcb.13.10.6102-6113.1993.
Texte intégralAnderson, J. T., M. R. Paddy, and M. S. Swanson. "PUB1 is a major nuclear and cytoplasmic polyadenylated RNA-binding protein in Saccharomyces cerevisiae." Molecular and Cellular Biology 13, no. 10 (1993): 6102–13. http://dx.doi.org/10.1128/mcb.13.10.6102.
Texte intégralCosson, Bertrand, Anne Couturier, Svetlana Chabelskaya, et al. "Poly(A)-Binding Protein Acts in Translation Termination via Eukaryotic Release Factor 3 Interaction and Does Not Influence [PSI+] Propagation." Molecular and Cellular Biology 22, no. 10 (2002): 3301–15. http://dx.doi.org/10.1128/mcb.22.10.3301-3315.2002.
Texte intégralKobayashi, Tetsuo, Yuji Funakoshi, Shin-ichi Hoshino, and Toshiaki Katada. "The GTP-binding Release Factor eRF3 as a Key Mediator Coupling Translation Termination to mRNA Decay." Journal of Biological Chemistry 279, no. 44 (2004): 45693–700. http://dx.doi.org/10.1074/jbc.m405163200.
Texte intégralWyers, Françoise, Michèle Minet, Marie Elisabeth Dufour, Le Thuy Anh Vo, and François Lacroute. "Deletion of the PAT1 Gene Affects Translation Initiation and Suppresses a PAB1 Gene Deletion in Yeast." Molecular and Cellular Biology 20, no. 10 (2000): 3538–49. http://dx.doi.org/10.1128/mcb.20.10.3538-3549.2000.
Texte intégralZhong, Guo-wei, Ping Jiang, Wei-ran Qiao, Yuan-wei Zhang, Wen-fan Wei, and Ling Lu. "Protein Phosphatase 2A (PP2A) Regulatory Subunits ParA and PabA Orchestrate Septation and Conidiation and Are Essential for PP2A Activity in Aspergillus nidulans." Eukaryotic Cell 13, no. 12 (2014): 1494–506. http://dx.doi.org/10.1128/ec.00201-14.
Texte intégralBrown, Justin T., Xianmei Yang, and Arlen W. Johnson. "Inhibition of mRNA Turnover in Yeast by an xrn1 Mutation Enhances the Requirement for eIF4E Binding to eIF4G and for Proper Capping of Transcripts by Ceg1p." Genetics 155, no. 1 (2000): 31–42. http://dx.doi.org/10.1093/genetics/155.1.31.
Texte intégralWegkamp, Arno, Wietske van Oorschot, Willem M. de Vos, and Eddy J. Smid. "Characterization of the Role of para-Aminobenzoic Acid Biosynthesis in Folate Production by Lactococcus lactis." Applied and Environmental Microbiology 73, no. 8 (2007): 2673–81. http://dx.doi.org/10.1128/aem.02174-06.
Texte intégralDunn, E. F. "Yeast poly(A)-binding protein, Pab1, and PAN, a poly(A) nuclease complex recruited by Pab1, connect mRNA biogenesis to export." Genes & Development 19, no. 1 (2005): 90–103. http://dx.doi.org/10.1101/gad.1267005.
Texte intégralKahan, Darren N., Ruofan Chen, Joshua Riback, Christopher Katanski, Allan Drummond, and Tobin R. Sosnick. "Molecular Factors Underlying Stress-Triggered Phase-Separation of Pab1." Biophysical Journal 116, no. 3 (2019): 350a. http://dx.doi.org/10.1016/j.bpj.2018.11.1903.
Texte intégralWANG, HONG, LIJUN WANG, QINQIN HU, RONGHUI WANG, YANBIN LI, and MICHAEL KIDD. "Rapid and Sensitive Detection of Campylobacter jejuni in Poultry Products Using a Nanoparticle-Based Piezoelectric Immunosensor Integrated with Magnetic Immunoseparation." Journal of Food Protection 81, no. 8 (2018): 1321–30. http://dx.doi.org/10.4315/0362-028x.jfp-17-381.
Texte intégralJames, Timothy Y., Robert P. Boulianne, Alan P. F. Bottoli, José D. Granado, Markus Aebi, and Ursula Kües. "The pab1 gene of Coprinus cinereus encodes a bifunctional protein for para-aminobenzoic acid (PABA) synthesis: implications for the evolution of fused PABA synthases." Journal of Basic Microbiology 42, no. 2 (2002): 91. http://dx.doi.org/10.1002/1521-4028(200205)42:2<91::aid-jobm91>3.0.co;2-8.
Texte intégralPintard, Lionel, Dieter Kressler, and Bruno Lapeyre. "Spb1p Is a Yeast Nucleolar Protein Associated with Nop1p and Nop58p That Is Able To BindS-Adenosyl-l-Methionine In Vitro." Molecular and Cellular Biology 20, no. 4 (2000): 1370–81. http://dx.doi.org/10.1128/mcb.20.4.1370-1381.2000.
Texte intégralPadariya, Monikaben, and Umesh Kalathiya. "The Binding Specificity of PAB1 with Poly(A) mRNA, Regulated by Its Structural Folding." Biomedicines 10, no. 11 (2022): 2981. http://dx.doi.org/10.3390/biomedicines10112981.
Texte intégralLe, Hanh, Su-Chih Chang, Robert L. Tanguay, and Daniel R. Gallie. "The Wheat Poly (A)-Binding Protein Functionally Complements Pab1 in Yeast." European Journal of Biochemistry 243, no. 1-2 (1997): 350–57. http://dx.doi.org/10.1111/j.1432-1033.1997.0350a.x.
Texte intégralZhang, Yirong, Linquan Bai, and Zixin Deng. "Functional characterization of the first two actinomycete 4-amino-4-deoxychorismate lyase genes." Microbiology 155, no. 7 (2009): 2450–59. http://dx.doi.org/10.1099/mic.0.026336-0.
Texte intégralCui, Ningning, Haihui Tong, Yan Li, et al. "Role of Prealbumin in Predicting the Prognosis of Severely and Critically Ill COVID-19 Patients." American Journal of Tropical Medicine and Hygiene 105, no. 3 (2021): 718–26. http://dx.doi.org/10.4269/ajtmh.21-0234.
Texte intégralZhang, Chongxu, Xin Wang, Shiwha Park, et al. "Only a subset of the PAB1-mRNP proteome is present in mRNA translation complexes." Protein Science 23, no. 8 (2014): 1036–49. http://dx.doi.org/10.1002/pro.2490.
Texte intégralBoeck, Ronald, Bruno Lapeyre, Christine E. Brown, and Alan B. Sachs. "Capped mRNA Degradation Intermediates Accumulate in the Yeast spb8-2 Mutant." Molecular and Cellular Biology 18, no. 9 (1998): 5062–72. http://dx.doi.org/10.1128/mcb.18.9.5062.
Texte intégralLahoz, Aurelia, María Alcaide-Gavilán, Rafael R. Daga, and Juan Jimenez. "Antagonistic Roles of PP2A-Pab1 and Etd1 in the Control of Cytokinesis in Fission Yeast." Genetics 186, no. 4 (2010): 1261–70. http://dx.doi.org/10.1534/genetics.110.121368.
Texte intégralBrandariz-Núñez, Alberto, Fuxing Zeng, Quan Ngoc Lam, and Hong Jin. "Sbp1 modulates the translation of Pab1 mRNA in a poly(A)- and RGG-dependent manner." RNA 24, no. 1 (2017): 43–55. http://dx.doi.org/10.1261/rna.062547.117.
Texte intégralMeaux, Stacie, Ambro van Hoof, and Kristian E. Baker. "Nonsense-Mediated mRNA Decay in Yeast Does Not Require PAB1 or a Poly(A) Tail." Molecular Cell 29, no. 1 (2008): 134–40. http://dx.doi.org/10.1016/j.molcel.2007.10.031.
Texte intégralWang, Le, Pan Li, Pei Zeng, et al. "Dosage suppressors of gpn2ts mutants and functional insights into the role of Gpn2 in budding yeast." PLOS ONE 19, no. 12 (2024): e0313597. https://doi.org/10.1371/journal.pone.0313597.
Texte intégralWyers, Françoise, Michèle Minet, Marie Elisabeth Dufour, Le Thuy Anh Vo, and François Lacroute. "Deletion of the PAT1 Gene Affects Translation Initiation and Suppresses a PAB1 Gene Deletion in Yeast." Molecular and Cellular Biology 20, no. 10 (2000): 3538–49. http://dx.doi.org/10.1128/.20.10.3538-3549.2000.
Texte intégralMoqtaderi, Zarmik, Joseph V. Geisberg, and Kevin Struhl. "Extensive Structural Differences of Closely Related 3′ mRNA Isoforms: Links to Pab1 Binding and mRNA Stability." Molecular Cell 72, no. 5 (2018): 849–61. http://dx.doi.org/10.1016/j.molcel.2018.08.044.
Texte intégralBrambilla, Marco, Francesca Martani, Stefano Bertacchi, Ilaria Vitangeli, and Paola Branduardi. "The Saccharomyces cerevisiae poly (A) binding protein (Pab1): Master regulator of mRNA metabolism and cell physiology." Yeast 36, no. 1 (2018): 23–34. http://dx.doi.org/10.1002/yea.3347.
Texte intégralKonitufe Claudius, Abubakar Sabo Baba, and Aliyu Abubakar. "Influence of Pulverized Animal Bone and Animal Bone Ash on the Mechanical Properties of Normal Strength Concrete using Response Surface Method." CONSTRUCTION 3, no. 1 (2023): 63–74. http://dx.doi.org/10.15282/construction.v3i1.9097.
Texte intégralChen, Ruofan, Julia Shangguan, Darren N. Kahan, Joshua A. Riback, D. A. Drummond, and Tobin R. Sosnick. "Molecular basis of stress-triggered phase separation of Pab1 mediated by folded domains rather than disordered regions." Biophysical Journal 121, no. 3 (2022): 146a. http://dx.doi.org/10.1016/j.bpj.2021.11.1988.
Texte intégralSwisher, Kylie D., and Roy Parker. "Localization to, and Effects of Pbp1, Pbp4, Lsm12, Dhh1, and Pab1 on Stress Granules in Saccharomyces cerevisiae." PLoS ONE 5, no. 4 (2010): e10006. http://dx.doi.org/10.1371/journal.pone.0010006.
Texte intégralBRUNE, C. "Yeast poly(A)-binding protein Pab1 shuttles between the nucleus and the cytoplasm and functions in mRNA export." RNA 11, no. 4 (2005): 517–31. http://dx.doi.org/10.1261/rna.7291205.
Texte intégralHorton, Lynn E., Philip James, Elizabeth A. Craig, and Jack O. Hensold. "The Yeast hsp70 Homologue Ssa Is Required for Translation and Interacts with Sis1 and Pab1 on Translating Ribosomes." Journal of Biological Chemistry 276, no. 17 (2001): 14426–33. http://dx.doi.org/10.1074/jbc.m100266200.
Texte intégralValentini, Sandro R., Jason M. Casolari, Carla C. Oliveira, Pamela A. Silver, and Anne E. McBride. "Genetic Interactions of Yeast Eukaryotic Translation Initiation Factor 5A (eIF5A) Reveal Connections to Poly(A)-Binding Protein and Protein Kinase C Signaling." Genetics 160, no. 2 (2002): 393–405. http://dx.doi.org/10.1093/genetics/160.2.393.
Texte intégralGaillard, Hélène, and Andrés Aguilera. "A Novel Class of mRNA-containing Cytoplasmic Granules Are Produced in Response to UV-Irradiation." Molecular Biology of the Cell 19, no. 11 (2008): 4980–92. http://dx.doi.org/10.1091/mbc.e08-02-0193.
Texte intégralTadauchi, Tomofumi, Toshifumi Inada, Kunihiro Matsumoto, and Kenji Irie. "Posttranscriptional Regulation of HO Expression by the Mkt1-Pbp1 Complex." Molecular and Cellular Biology 24, no. 9 (2004): 3670–81. http://dx.doi.org/10.1128/mcb.24.9.3670-3681.2004.
Texte intégralAssis, Ludmila A., Moezio V. C. Santos Filho, Joao R. da Cruz Silva, et al. "Identification of novel proteins and mRNAs differentially bound to the Leishmania Poly(A) Binding Proteins reveals a direct association between PABP1, the RNA-binding protein RBP23 and mRNAs encoding ribosomal proteins." PLOS Neglected Tropical Diseases 15, no. 10 (2021): e0009899. http://dx.doi.org/10.1371/journal.pntd.0009899.
Texte intégralPeltz, S. W., J. L. Donahue, and A. Jacobson. "A mutation in the tRNA nucleotidyltransferase gene promotes stabilization of mRNAs in Saccharomyces cerevisiae." Molecular and Cellular Biology 12, no. 12 (1992): 5778–84. http://dx.doi.org/10.1128/mcb.12.12.5778-5784.1992.
Texte intégralPeltz, S. W., J. L. Donahue, and A. Jacobson. "A mutation in the tRNA nucleotidyltransferase gene promotes stabilization of mRNAs in Saccharomyces cerevisiae." Molecular and Cellular Biology 12, no. 12 (1992): 5778–84. http://dx.doi.org/10.1128/mcb.12.12.5778.
Texte intégralMarin, Ambroise, Emmanuel Denimal, Lucie Bertheau, Stéphane Guyot, Ludovic Journaux, and Paul Molin. "Automatic Counting of Intra-Cellular Ribonucleo-Protein Aggregates in Saccharomyces cerevisiae Using a Textural Approach." Microscopy and Microanalysis 25, no. 1 (2019): 164–79. http://dx.doi.org/10.1017/s1431927619000084.
Texte intégralKops, Anne de Bruyn, Jordan E. Burke, and Christine Guthrie. "Brr6 plays a role in gene recruitment and transcriptional regulation at the nuclear envelope." Molecular Biology of the Cell 29, no. 21 (2018): 2578–90. http://dx.doi.org/10.1091/mbc.e18-04-0258.
Texte intégralTurtola, Matti, M. Cemre Manav, Ananthanarayanan Kumar, et al. "Three-layered control of mRNA poly(A) tail synthesis in Saccharomyces cerevisiae." Genes & Development 35, no. 17-18 (2021): 1290–303. http://dx.doi.org/10.1101/gad.348634.121.
Texte intégralKitamura, Satoshi, Yutaka Oono, and Issay Narumi. "Arabidopsis pab1, a mutant with reduced anthocyanins in immature seeds from banyuls, harbors a mutation in the MATE transporter FFT." Plant Molecular Biology 90, no. 1-2 (2015): 7–18. http://dx.doi.org/10.1007/s11103-015-0389-8.
Texte intégralLee, Darren, Takbum Ohn, Yueh-Chin Chiang, et al. "PUF3 Acceleration of Deadenylation in Vivo Can Operate Independently of CCR4 Activity, Possibly Involving Effects on the PAB1–mRNP Structure." Journal of Molecular Biology 399, no. 4 (2010): 562–75. http://dx.doi.org/10.1016/j.jmb.2010.04.034.
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