Статті в журналах з теми "Inactive surface mutants"
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Honegger, A. M., A. Schmidt, A. Ullrich, and J. Schlessinger. "Separate endocytic pathways of kinase-defective and -active EGF receptor mutants expressed in same cells." Journal of Cell Biology 110, no. 5 (May 1, 1990): 1541–48. http://dx.doi.org/10.1083/jcb.110.5.1541.
Повний текст джерелаMo, Xiu-Lei, Rui Yang, and Ya-Xiong Tao. "Functions of transmembrane domain 3 of human melanocortin-4 receptor." Journal of Molecular Endocrinology 49, no. 3 (September 26, 2012): 221–35. http://dx.doi.org/10.1530/jme-12-0162.
Повний текст джерелаKinne, Anita, Stephan Roth, Heike Biebermann, Josef Köhrle, Annette Grüters, and Ulrich Schweizer. "Surface translocation and tri-iodothyronine uptake of mutant MCT8 proteins are cell type-dependent." Journal of Molecular Endocrinology 43, no. 6 (July 31, 2009): 263–71. http://dx.doi.org/10.1677/jme-09-0043.
Повний текст джерелаFilippa, Nathalie, Carol L. Sable, Brian A. Hemmings, and Emmanuel Van Obberghen. "Effect of Phosphoinositide-Dependent Kinase 1 on Protein Kinase B Translocation and Its Subsequent Activation." Molecular and Cellular Biology 20, no. 15 (August 1, 2000): 5712–21. http://dx.doi.org/10.1128/mcb.20.15.5712-5721.2000.
Повний текст джерелаZorreguieta, Angeles, Christine Finnie, and J. Allan Downie. "Extracellular Glycanases of Rhizobium leguminosarum Are Activated on the Cell Surface by an Exopolysaccharide-Related Component." Journal of Bacteriology 182, no. 5 (March 1, 2000): 1304–12. http://dx.doi.org/10.1128/jb.182.5.1304-1312.2000.
Повний текст джерелаYamanouchi, Jun, Takaaki Hato, Hiroshi Fujiwara, Yoshihiro Yakushijin та Masaki Yasukawa. "A Glycan Wedge Between βTD and βI Domains Activates Integrin αIIbβ3",. Blood 118, № 21 (18 листопада 2011): 3259. http://dx.doi.org/10.1182/blood.v118.21.3259.3259.
Повний текст джерелаMoon, Andrea F., Philippe Gaudu, and Lars C. Pedersen. "Structural characterization of the virulence factor nuclease A fromStreptococcus agalactiae." Acta Crystallographica Section D Biological Crystallography 70, no. 11 (October 23, 2014): 2937–49. http://dx.doi.org/10.1107/s1399004714019725.
Повний текст джерелаFerjoux, Geraldine, Frederic Lopez, Jean-Pierre Esteve, Audrey Ferrand, Eric Vivier, Frederic Vely, Nathalie Saint-Laurent, Lucien Pradayrol, Louis Buscail, and Christiane Susini. "Critical Role of Src and SHP-2 in sst2 Somatostatin Receptor-mediated Activation of SHP-1 and Inhibition of Cell Proliferation." Molecular Biology of the Cell 14, no. 9 (September 2003): 3911–28. http://dx.doi.org/10.1091/mbc.e03-02-0069.
Повний текст джерелаEbanks, R. O., and D. E. Isenman. "Evidence for the involvement of arginine 462 and the flanking sequence of human C4 beta-chain in mediating C5 binding to the C4b subcomponent of the classical complement pathway C5 convertase." Journal of Immunology 154, no. 6 (March 15, 1995): 2808–20. http://dx.doi.org/10.4049/jimmunol.154.6.2808.
Повний текст джерелаOhradanova, Anna, Daniela Vullo, Juraj Kopacek, Claudia Temperini, Tatiana Betakova, Silvia Pastorekova, Jaromir Pastorek, and Claudiu T. Supuran. "Reconstitution of carbonic anhydrase activity of the cell-surface-binding protein of vaccinia virus." Biochemical Journal 407, no. 1 (September 12, 2007): 61–67. http://dx.doi.org/10.1042/bj20070816.
Повний текст джерелаWright, J. H., P. Drueckes, J. Bartoe, Z. Zhao, S. H. Shen, and E. G. Krebs. "A role for the SHP-2 tyrosine phosphatase in nerve growth-induced PC12 cell differentiation." Molecular Biology of the Cell 8, no. 8 (August 1997): 1575–85. http://dx.doi.org/10.1091/mbc.8.8.1575.
Повний текст джерелаYamanouchi, Jun, Takaaki Hato, Yoshihiro Yakushijin, Ikuya Sakai та Masaki Yasukawa. "Identification of Critical Residues for Affinity Regulation of β3 Integrins in the β6-α7 Loop of the I-Like Domain." Blood 108, № 11 (16 листопада 2006): 1526. http://dx.doi.org/10.1182/blood.v108.11.1526.1526.
Повний текст джерелаSchwake, Michael, Thomas Friedrich, and Thomas J. Jentsch. "An Internalization Signal in ClC-5, an Endosomal Cl−Channel Mutated in Dent's Disease." Journal of Biological Chemistry 276, no. 15 (December 14, 2000): 12049–54. http://dx.doi.org/10.1074/jbc.m010642200.
Повний текст джерелаFang, Eric G. C., and Ralph A. Dean. "Site-Directed Mutagenesis of the magB Gene Affects Growth and Development in Magnaporthe grisea." Molecular Plant-Microbe Interactions® 13, no. 11 (November 2000): 1214–27. http://dx.doi.org/10.1094/mpmi.2000.13.11.1214.
Повний текст джерелаWalters, Jad, Joshua L. Schipper, Paul Swartz, Carla Mattos, and A. Clay Clark. "Allosteric modulation of caspase 3 through mutagenesis." Bioscience Reports 32, no. 4 (June 28, 2012): 401–11. http://dx.doi.org/10.1042/bsr20120037.
Повний текст джерелаDe la Vieja, Antonio, Christopher S. Ginter, and Nancy Carrasco. "Molecular Analysis of a Congenital Iodide Transport Defect: G543E Impairs Maturation and Trafficking of the Na+/I− Symporter." Molecular Endocrinology 19, no. 11 (November 1, 2005): 2847–58. http://dx.doi.org/10.1210/me.2005-0162.
Повний текст джерелаKittanakom, Saranya, Emmanuelle Cordat, and Reinhart A. F. Reithmeier. "Dominant-negative effect of Southeast Asian ovalocytosis anion exchanger 1 in compound heterozygous distal renal tubular acidosis." Biochemical Journal 410, no. 2 (February 12, 2008): 271–81. http://dx.doi.org/10.1042/bj20070615.
Повний текст джерелаIng, Bryant, Alina Shteiman-Kotler, MaryLisa Castelli, Pauline Henry, Youngshil Pak, Bryan Stewart, Gabrielle L. Boulianne, and Daniela Rotin. "Regulation of Commissureless by the Ubiquitin Ligase DNedd4 Is Required for Neuromuscular Synaptogenesis in Drosophila melanogaster." Molecular and Cellular Biology 27, no. 2 (October 30, 2006): 481–96. http://dx.doi.org/10.1128/mcb.00463-06.
Повний текст джерелаStrittmatter, S. M., D. Valenzuela, and M. C. Fishman. "An amino-terminal domain of the growth-associated protein GAP-43 mediates its effects on filopodial formation and cell spreading." Journal of Cell Science 107, no. 1 (January 1, 1994): 195–204. http://dx.doi.org/10.1242/jcs.107.1.195.
Повний текст джерелаLavillette, Dimitri, and David Kabat. "Porcine Endogenous Retroviruses Infect Cells Lacking Cognate Receptors by an Alternative Pathway: Implications for Retrovirus Evolution and Xenotransplantation." Journal of Virology 78, no. 16 (August 15, 2004): 8868–77. http://dx.doi.org/10.1128/jvi.78.16.8868-8877.2004.
Повний текст джерелаHands, Sarah L., Lisa E. Holland, Mireille Vankemmelbeke, Lauren Fraser, Colin J. Macdonald, Geoffrey R. Moore, Richard James, and Christopher N. Penfold. "Interactions of TolB with the Translocation Domain of Colicin E9 Require an Extended TolB Box." Journal of Bacteriology 187, no. 19 (October 1, 2005): 6733–41. http://dx.doi.org/10.1128/jb.187.19.6733-6741.2005.
Повний текст джерелаBriken, V., D. Lankar, and C. Bonnerot. "New evidence for two MHC class II-restricted antigen presentation pathways by overexpression of a small G protein." Journal of Immunology 159, no. 10 (November 15, 1997): 4653–58. http://dx.doi.org/10.4049/jimmunol.159.10.4653.
Повний текст джерелаEnz, Sabine, Heidi Brand, Claudia Orellana, Susanne Mahren, and Volkmar Braun. "Sites of Interaction between the FecA and FecR Signal Transduction Proteins of Ferric Citrate Transport in Escherichia coli K-12." Journal of Bacteriology 185, no. 13 (July 1, 2003): 3745–52. http://dx.doi.org/10.1128/jb.185.13.3745-3752.2003.
Повний текст джерелаQin, Haixia, Michael A. Frohman, and Wendy B. Bollag. "Phospholipase D2 Mediates Acute Aldosterone Secretion in Response to Angiotensin II in Adrenal Glomerulosa Cells." Endocrinology 151, no. 5 (March 10, 2010): 2162–70. http://dx.doi.org/10.1210/en.2009-1159.
Повний текст джерелаShetty, Sreerama, Malathesha Ganachari, Ming-Cheh Liu, Ali Azghani, Harish Muniyappa, and Steven Idell. "Regulation of urokinase receptor expression by phosphoglycerate kinase is independent of its catalytic activity." American Journal of Physiology-Lung Cellular and Molecular Physiology 289, no. 4 (October 2005): L591—L598. http://dx.doi.org/10.1152/ajplung.00319.2004.
Повний текст джерелаCain, Natalie E., and Chris A. Kaiser. "Transport activity–dependent intracellular sorting of the yeast general amino acid permease." Molecular Biology of the Cell 22, no. 11 (June 2011): 1919–29. http://dx.doi.org/10.1091/mbc.e10-10-0800.
Повний текст джерелаMcCallum, Nadine, Markus Bischoff, Hideki Maki, Akihito Wada, and Brigitte Berger-Bächi. "TcaR, a Putative MarR-Like Regulator of sarS Expression." Journal of Bacteriology 186, no. 10 (May 15, 2004): 2966–72. http://dx.doi.org/10.1128/jb.186.10.2966-2972.2004.
Повний текст джерелаBurns, Michael L., Thomas M. Malott, Kevin J. Metcalf, Benjamin J. Hackel, Jonah R. Chan, and Eric V. Shusta. "Directed Evolution of Brain-Derived Neurotrophic Factor for Improved Folding and Expression in Saccharomyces cerevisiae." Applied and Environmental Microbiology 80, no. 18 (July 11, 2014): 5732–42. http://dx.doi.org/10.1128/aem.01466-14.
Повний текст джерелаYu, Xiaochun, Kailash D. Sharma, Tsuyoshi Takahashi, Ryo Iwamoto, and Eisuke Mekada. "Ligand-independent Dimer Formation of Epidermal Growth Factor Receptor (EGFR) Is a Step Separable from Ligand-induced EGFR Signaling." Molecular Biology of the Cell 13, no. 7 (July 2002): 2547–57. http://dx.doi.org/10.1091/mbc.01-08-0411.
Повний текст джерелаSERPA, Jacinta, Nuno MENDES, Celso A. REIS, Luis F. SANTOS SILVA, Raquel ALMEIDA, Jacques LE PENDU, and Leonor DAVID. "Two new FUT2 (fucosyltransferase 2 gene) missense polymorphisms, 739G→A and 839T→C, are partly responsible for non-secretor status in a Caucasian population from Northern Portugal." Biochemical Journal 383, no. 3 (October 26, 2004): 469–74. http://dx.doi.org/10.1042/bj20040803.
Повний текст джерелаKEYNAN, Shoshana, Nigel M. HOOPER, and Anthony J. TURNER. "Identification by site-directed mutagenesis of three essential histidine residues in membrane dipeptidase, a novel mammalian zinc peptidase." Biochemical Journal 326, no. 1 (August 15, 1997): 47–51. http://dx.doi.org/10.1042/bj3260047.
Повний текст джерелаShipitsin, Michail, and Larry A. Feig. "RalA but Not RalB Enhances Polarized Delivery of Membrane Proteins to the Basolateral Surface of Epithelial Cells." Molecular and Cellular Biology 24, no. 13 (July 1, 2004): 5746–56. http://dx.doi.org/10.1128/mcb.24.13.5746-5756.2004.
Повний текст джерелаJané-Valbuena, Judit, Laura A. Breun, Leslie A. Schiff та Max L. Nibert. "Sites and Determinants of Early Cleavages in the Proteolytic Processing Pathway of Reovirus Surface Protein σ3". Journal of Virology 76, № 10 (15 травня 2002): 5184–97. http://dx.doi.org/10.1128/jvi.76.10.5184-5197.2002.
Повний текст джерелаWood, Jeremy P., Jay R. Silveira, Nicole M. Maille, Laura M. Haynes, and Paula B. Tracy. "Prothrombin activation on the activated platelet surface optimizes expression of procoagulant activity." Blood 117, no. 5 (February 3, 2011): 1710–18. http://dx.doi.org/10.1182/blood-2010-09-311035.
Повний текст джерелаBurke, John E., Olga Perisic, Glenn R. Masson, Oscar Vadas та Roger L. Williams. "Oncogenic mutations mimic and enhance dynamic events in the natural activation of phosphoinositide 3-kinase p110α (PIK3CA)". Proceedings of the National Academy of Sciences 109, № 38 (4 вересня 2012): 15259–64. http://dx.doi.org/10.1073/pnas.1205508109.
Повний текст джерелаAkimoto, Megumi, Makiko Ishihara, Kenji Kizawa, Hidenari Takahara, and Masaki Unno. "Two crystal forms of peptidylarginine deiminase typeIII (PAD3)." Acta Crystallographica Section A Foundations and Advances 70, a1 (August 5, 2014): C937. http://dx.doi.org/10.1107/s2053273314090627.
Повний текст джерелаFrumence, Etienne, Sandrine Genetet, Pierre Ripoche, Achille Iolascon, Immacolata Andolfo, Caroline Le Van Kim, Yves Colin, Isabelle Mouro-Chanteloup, and Claude Lopez. "Rapid Cl−/HCO3−exchange kinetics of AE1 in HEK293 cells and hereditary stomatocytosis red blood cells." American Journal of Physiology-Cell Physiology 305, no. 6 (September 15, 2013): C654—C662. http://dx.doi.org/10.1152/ajpcell.00142.2013.
Повний текст джерелаYang, Li-Kun, and Ya-Xiong Tao. "Alanine Scanning Mutagenesis of the DRYxxI Motif and Intracellular Loop 2 of Human Melanocortin-4 Receptor." International Journal of Molecular Sciences 21, no. 20 (October 15, 2020): 7611. http://dx.doi.org/10.3390/ijms21207611.
Повний текст джерелаOwen-Schaub, L. B., W. Zhang, J. C. Cusack, L. S. Angelo, S. M. Santee, T. Fujiwara, J. A. Roth, A. B. Deisseroth, W. W. Zhang, and E. Kruzel. "Wild-type human p53 and a temperature-sensitive mutant induce Fas/APO-1 expression." Molecular and Cellular Biology 15, no. 6 (June 1995): 3032–40. http://dx.doi.org/10.1128/mcb.15.6.3032.
Повний текст джерелаMolinari, Antonio, Carla Giorgetti, Jacqueline Lansen, Fabrizio Vaghi, Gaetano Orsini, Elena Maria Faioni, and Pier Mannuccio Mannucci. "Thrombomodulin Is a Cofactor for Thrombin Degradation of Recombinant Single-Chain Urokinase Plasminogen Activator "In Vitro" and in a Perfused Rabbit Heart Model." Thrombosis and Haemostasis 67, no. 02 (1992): 226–32. http://dx.doi.org/10.1055/s-0038-1648417.
Повний текст джерелаBach, Horacio, Yevgeny Berdichevsky, and David Gutnick. "An Exocellular Protein from the Oil-Degrading Microbe Acinetobacter venetianus RAG-1 Enhances the Emulsifying Activity of the Polymeric Bioemulsifier Emulsan." Applied and Environmental Microbiology 69, no. 5 (May 2003): 2608–15. http://dx.doi.org/10.1128/aem.69.5.2608-2615.2003.
Повний текст джерелаKothari, Hema, Ramesh Nayak, L. Vijaya Mohan Rao, and Usha Pendurthi. "Cryptic Vs. Active Tissue Factor: Cystine186-Cystine 209 Disulfide Bond Switch Is Not the Answer." Blood 114, no. 22 (November 20, 2009): 333. http://dx.doi.org/10.1182/blood.v114.22.333.333.
Повний текст джерелаLi, Wei, Douglas Metcalf, Roman Gorelik, Renhao Li, Neal Mitra, Vikas Nanda, Peter B. Law, James D. Lear, William F. DeGrado та Joel S. Bennett. "Heteromeric and Homomeric Transmembrane Domain Associations Regulate αIIbβ3 Function." Blood 104, № 11 (16 листопада 2004): 329. http://dx.doi.org/10.1182/blood.v104.11.329.329.
Повний текст джерелаLeader, Avi, Ronit Mor-Cohen, Nurit Rosenberg, Ron Ram, Uri Seligsohn, Aida Inbal та Judith Lahav. "The Role Of Protein Disulfide Isomerase In The Post-Ligation Phase Of β3 Integrin-Dependent Cell Adhesion". Blood 122, № 21 (15 листопада 2013): 2307. http://dx.doi.org/10.1182/blood.v122.21.2307.2307.
Повний текст джерелаElsen, Sylvie, Ophélie Duché, and Annette Colbeau. "Interaction between the H2Sensor HupUV and the Histidine Kinase HupT Controls HupSL HydrogenaseSynthesis in Rhodobactercapsulatus." Journal of Bacteriology 185, no. 24 (December 15, 2003): 7111–19. http://dx.doi.org/10.1128/jb.185.24.7111-7119.2003.
Повний текст джерелаOzawa, Masayuki, and Rolf Kemler. "The Membrane-proximal Region of the E-Cadherin Cytoplasmic Domain Prevents Dimerization and Negatively Regulates Adhesion Activity." Journal of Cell Biology 142, no. 6 (September 21, 1998): 1605–13. http://dx.doi.org/10.1083/jcb.142.6.1605.
Повний текст джерелаNirmala, Jayaveeramuthu, Tom Drader, Xianming Chen, Brian Steffenson, and Andris Kleinhofs. "Stem Rust Spores Elicit Rapid RPG1 Phosphorylation." Molecular Plant-Microbe Interactions® 23, no. 12 (December 2010): 1635–42. http://dx.doi.org/10.1094/mpmi-06-10-0136.
Повний текст джерелаShon, D. Judy, Stacy A. Malaker, Kayvon Pedram, Emily Yang, Venkatesh Krishnan, Oliver Dorigo, and Carolyn R. Bertozzi. "An enzymatic toolkit for selective proteolysis, detection, and visualization of mucin-domain glycoproteins." Proceedings of the National Academy of Sciences 117, no. 35 (August 17, 2020): 21299–307. http://dx.doi.org/10.1073/pnas.2012196117.
Повний текст джерелаStewart, Andrew K., Prabhakar S. Kedar, Boris E. Shmukler, David H. Vandorpe, Ann Hsu, Bertil Glader, Alicia Rivera, Carlo Brugnara, and Seth L. Alper. "Functional characterization and modified rescue of novel AE1 mutation R730C associated with overhydrated cation leak stomatocytosis." American Journal of Physiology-Cell Physiology 300, no. 5 (May 2011): C1034—C1046. http://dx.doi.org/10.1152/ajpcell.00447.2010.
Повний текст джерелаPowner, Dale J., Matthew N. Hodgkin та Michael J. O. Wakelam. "Antigen-stimulated Activation of Phospholipase D1b by Rac1, ARF6, and PKCα in RBL-2H3 Cells". Molecular Biology of the Cell 13, № 4 (квітень 2002): 1252–62. http://dx.doi.org/10.1091/mbc.01-05-0235.
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