Academic literature on the topic 'MFS proteins'
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Journal articles on the topic "MFS proteins":
Sekhwal, Manoj Kumar, Vinay Sharma, and Renu Sarin. "Identification of MFS proteins in sorghum using semantic similarity." Theory in Biosciences 132, no. 2 (January 9, 2013): 105–13. http://dx.doi.org/10.1007/s12064-012-0174-z.
Xiao, Qingjie, Mengxue Xu, Weiwei Wang, Tingting Wu, Weizhe Zhang, Wenming Qin, and Bo Sun. "Utilization of AlphaFold2 to Predict MFS Protein Conformations after Selective Mutation." International Journal of Molecular Sciences 23, no. 13 (June 29, 2022): 7235. http://dx.doi.org/10.3390/ijms23137235.
Ditty, Jayna L., and Caroline S. Harwood. "Conserved Cytoplasmic Loops Are Important for both the Transport and Chemotaxis Functions of PcaK, a Protein fromPseudomonas putida with 12 Membrane-Spanning Regions." Journal of Bacteriology 181, no. 16 (August 15, 1999): 5068–74. http://dx.doi.org/10.1128/jb.181.16.5068-5074.1999.
Severson, Aaron F., and Bruce Bowerman. "Myosin and the PAR proteins polarize microfilament-dependent forces that shape and position mitotic spindles in Caenorhabditis elegans." Journal of Cell Biology 161, no. 1 (April 14, 2003): 21–26. http://dx.doi.org/10.1083/jcb.200210171.
Rizal, S., Masrukhin, H. A. Nugroho, and S. Saputra. "Detection of major facilitator superfamily (MFS) transporter in Enterobacteriaceae isolated from chicken." IOP Conference Series: Earth and Environmental Science 1107, no. 1 (December 1, 2022): 012050. http://dx.doi.org/10.1088/1755-1315/1107/1/012050.
Varela, Manuel F., Anely Ortiz-Alegria, Manjusha Lekshmi, Jerusha Stephen, and Sanath Kumar. "Functional Roles of the Conserved Amino Acid Sequence Motif C, the Antiporter Motif, in Membrane Transporters of the Major Facilitator Superfamily." Biology 12, no. 10 (October 16, 2023): 1336. http://dx.doi.org/10.3390/biology12101336.
Zhang, Jialan, Yingbao Liu, Li Li, and Mengxiang Gao. "iTRAQ-Based Quantitative Proteomic Analysis Reveals Changes in Metabolite Biosynthesis in Monascus purpureus in Response to a Low-Frequency Magnetic Field." Toxins 10, no. 11 (October 29, 2018): 440. http://dx.doi.org/10.3390/toxins10110440.
Vardy, Eyal, Sonia Steiner-Mordoch, and Shimon Schuldiner. "Characterization of Bacterial Drug Antiporters Homologous to Mammalian Neurotransmitter Transporters." Journal of Bacteriology 187, no. 21 (November 1, 2005): 7518–25. http://dx.doi.org/10.1128/jb.187.21.7518-7525.2005.
Ginn, Samantha L., Melissa H. Brown, and Ronald A. Skurray. "The TetA(K) Tetracycline/H+ Antiporter from Staphylococcus aureus: Mutagenesis and Functional Analysis of Motif C." Journal of Bacteriology 182, no. 6 (March 15, 2000): 1492–98. http://dx.doi.org/10.1128/jb.182.6.1492-1498.2000.
Tortosa, Valentina, Maria Carmela Bonaccorsi di Patti, Federico Iacovelli, Andrea Pasquadibisceglie, Mattia Falconi, Giovanni Musci, and Fabio Polticelli. "Dynamical Behavior of the Human Ferroportin Homologue from Bdellovibrio bacteriovorus: Insight into the Ligand Recognition Mechanism." International Journal of Molecular Sciences 21, no. 18 (September 16, 2020): 6785. http://dx.doi.org/10.3390/ijms21186785.
Dissertations / Theses on the topic "MFS proteins":
Debbiche, Rim. "Influence des lipides sur la dynamique du transport du fer médié par la ferroportine-1 et sa modulation par des composés amphiphiles." Electronic Thesis or Diss., Brest, 2024. http://www.theses.fr/2024BRES0006.
Ferroportin-1(FPN1), the only known mammalian iron exporter, is expressed on the surface of various specialized cells involved in iron metabolism. This protein belongs to the Major Facilitator Superfamily (MFS) and releases intracellular iron through conformational changes oscillating between an open structure towards the cytoplasm (Inward-Facing) and an open structure towards the bloodstream (Outward-Facing; OF). It has been reported that FPN1 is preferentially localized in lipid-rafts, microdomains of the plasma membrane particularly enriched in cholesterol (CHOL). Early in the thesis, we hypothesized that direct interactions between FPN1 and surrounding lipids, notably CHOL, are necessary to stabilize FPN1 in the OF conformation and/or promote certain conformational changes. I confirmed the preferential colocalization of FPN1 in the lipid rafts of human embryonic kidney cells. The dependence of FPN1's iron export function on CHOL was examined by depletion/repletion (CHOL/epicholesterol). Mutational screening experiments supported by structural analyses of the experimental 3D structure of FPN1 in an OF state have identified three possible CHOL-binding sites (of the CARC/CRAC type). Based on molecular dynamics simulations in a simplified POPC-type lipid environment, we identify certain interactions between charged residues of the human FPN1 3D structure and the polar heads of the surrounding phospholipids, which could facilitate conformational changes of the transporter. Besides, I show, for the first time, that FPN1 function is modulated by synthetic amphiphilic compounds, ohmline and its derivatives. Through the development of a novel in vitro approach (PLA: Proximity Ligation Assay), I show that ohmline delocalizes FPN1 from lipid-rafts, thereby decreasing its interaction with its functional partner, ceruloplasmin (CP), a ferroxidase that catalyzes the oxidation of ferrous iron, and consequently its iron export function
Yousefian, Narek. "The three-component multidrug MFS-type efflux pump EmrAB-TolC from Escherichia coli : from cloning to structural analysis." Thesis, Bordeaux, 2020. http://www.theses.fr/2020BORD0065.
Currently, due to the misuse of antibiotics, we are facing a major public health problem. The resistance to antibiotics of certain bacterial strains makes the treatment of infections very complex. In this context, the present thesis project concerns the study of a bacterial efflux complex capable of transporting antibiotics from the cytoplasm to the outside of the cell. This complex is composed of an inner-membrane Major Facilitator Superfamily (MFS) transporter (EmrB, E. coli multidrug resistance), a channel of the outer membrane TolC (Tolerance to Colicin E1) and a periplasmic adapter (EmrA, E. coli multidrug resistance). Unlike RND-type efflux systems (such as AcrAB-TolC), little is known about the MFS-type EmrAB-TolC system. It is therefore important to study the entire complex on a structural and functional level, to analyse the marked differences between these two types of transport systems. The goal of my thesis project was to study at least one EmrAB-TolC complex from a structural point of view. For my studies the aim was to isolate the complex directly from bacteria overexpressing the three protein partners. In a first step, 15 homologous EmrAB-TolC systems were identified and their corresponding genes amplified from genomic DNA of different Gram-negative bacteria. Among the genes of the 15 systems, the genes coding for the E. coli and V. cholerae systems were further studied. The expression vectors encoded fluorescent markers for the monitoring of the expression levels of different proteins and for studying the formation of complexes. In a first step, the different protein expression levels (EmrB-mRFP1 and EmrA-sfGFP) were studied for several expression strains of E. coli by measuring the red and green fluorescence levels and by Western blot (anti-His, Myc, and Strep for EmrB, EmrA, and TolC). The E. coli strain C41(DE3) was best suited for co-expression of EmrAB-TolC. In a second step, the FSEC (Fluorescence detection Size Exclusion Chromatography) methodology was used to identify a complex suitable for structural study. Thus this method enabled the observation that the EmrAB-TolC complex of E. coli was produced in higher amount than that of V. cholerae. The final co-purification protocol consists in perfoming a gentle lysis of the bacteria using lysozyme, then after solubilization with DDM, the purification is started by a Ni2+-NTA affinity chromatography step followed by a size exclusion chromatography step. Finally, the fractions containing the three protein partners are used for the detergent-exchange by amphipol A8-35 before the structural study by electron microscopy. Negative stain EM-micrographs displayed elongated objects with a length of 33 nm in side view. An average image of EmrAB-TolC shows similarities to that of the AcrAB-TolC complex observed under similar conditions. Similarities included the characteristic densities of TolC. Whereas differences were found in the lower part of EmrAB which is thinner than the lower part of AcrAB. The densities visible above the amphipol-ring correspond to EmrA, which displays a channel-like structure as in AcrA. The channel however seems to extend further towards the amphipol belt. Since EmrB does not have an extended periplasmic domain as the RND proteins have, these densities are therefore solely assigned to EmrA. EmrA, on the other side, contacts TolC akin to the interaction of AcrA/MexA to their cognate outer membrane channels (TolC/OprM) in a ‘tip-to-tip’ fashion
Aufgrund des Missbrauchs von Antibiotika stehen wir derzeit vor einem großen Problem deröffentlichen Gesundheit. Die Antibiotikaresistenz bestimmter Bakterienstämme macht die Behandlungvon Infektionen sehr komplex.In diesem Zusammenhang befasst sich diese Arbeit mit der Untersuchung eines bakteriellenEffluxkomplexes, der Antibiotika vom Zytoplasma zur Außenseite der Zelle transportieren kann. DieserKomplex besteht aus einem Major Facilitator Superfamily (MFS) Transporter der inneren Membran(EmrB, E. coli multidrug resistance), einem Kanal der äußeren Membran TolC (Tolerance to Colicin E1)und einem periplasmatischen Adapter (EmrA, E. coli multidrug resistance).Im Gegensatz zu Effluxsystemen vom RND-Typ (wie AcrAB-TolC) ist über das EmrAB-TolCSystemvom MFS-Typ wenig bekannt. Es ist daher wichtig, den gesamten Komplex auf struktureller undfunktioneller Sicht zu untersuchen, um die deutlichen Unterschiede zwischen diesen beiden Arten vonEffluxsystemen zu analysieren.Ziel meiner Doktorarbeit war es, mindestens einen EmrAB-TolC-Komplex aus struktureller Sichtzu untersuchen. Ziel meiner Studien war es, den Komplex direkt aus Bakterien, die die dreiProteinpartner überexprimieren, zu isolieren. In einem ersten Schritt wurden 15 homologe EmrAB-TolCSystemeidentifiziert und ihre entsprechenden Gene aus der genomischen DNA verschiedenergramnegativer Bakterien amplifiziert. Unter den Genen der 15 Systeme wurden die Gene, die für die E.coli und V. cholerae Systeme kodieren, weiter untersucht. Die Expressionsvektoren codiertenfluoreszierende Marker zur Untersuchung der Expression verschiedener Proteine und zur Untersuchungder Komplexbildung. In einem ersten Schritt wurden die verschiedenen Niveaus der Proteinexpression(EmrB-mRFP1 und EmrA-sfGFP) für mehrere E. coli Expressionsstämme untersucht durch Messen derroten und grünen Fluoreszenzniveaus und durch Western Blot (Anti-His, Myc und Strep für EmrB, EmrAund TolC). Der Stamm von E. coli C41(DE3) war am besten für die Koexpression von EmrAB-TolC14 geeignet. In einem zweiten Schritt wurde die FSEC-Methode (Fluorescence Detection Size ExclusionChromatography) verwendet, um einen für Strukturuntersuchungen geeigneten Komplex zuidentifizieren. Somit konnte mit dieser Methode festgestellt werden, dass der EmrAB-TolC-Komplex vonE. coli in größerer Menge als der von V. cholerae produziert wurde.Das endgültige Ko-Reinigungsprotokoll besteht darin, eine sanfte Lyse der Bakterien unterVerwendung von Lysozym durchzuführen. Nach der Solubilisierung mit DDM wird die Reinigung durcheinen Ni2+-NTA Affinitätschromatographieschritt gefolgt von einemGrößenausschlusschromatographieschritt gestartet. Schließlich werden die Fraktionen, die die dreiProteinpartner enthalten, für den Detergensaustausch durch Amphipol A8-35 vor derStrukturuntersuchung durch Elektronenmikroskopie verwendet.EM-Aufnahmen mit negativer Kontrastierung zeigten längliche Objekte mit einer Länge von 33nm in Seitenansicht. Ein durch Mittlung der Partikel erhaltenes Bild von EmrAB-TolC zeigt Ähnlichkeitenmit dem des AcrAB-TolC-Komplexes, der unter ähnlichen Bedingungen beobachtet wurde.Ähnlichkeiten schlossen die charakteristischen Dichten von TolC ein. Während im unteren Teil vonEmrAB Unterschiede festgestellt wurden, der dünner ist als der untere Teil von AcrAB. Die über demAmphipolring sichtbaren Dichten entsprechen EmrA, das wie bei AcrA eine kanalartige Strukturaufweist. Der Kanal scheint sich jedoch weiter in Richtung des Amphipolgürtels zu erstrecken. Da EmrBkeine erweiterte periplasmatische Domäne aufweist wie die RND-Proteine, werden diese Dichten daherausschließlich EmrA zugeordnet. Auf der anderen Seite kontaktiert EmrA TolC, ähnlich der Interaktionvon AcrA/MexA mit ihren jeweiligen Außenmembrankanälen (TolC/OprM), von “tip-to-tip”
Symington, Vicki F. "Structure and function of nitrate and nitrite transporters, NrtA and NitA, from Aspergillus nidulans." Thesis, University of St Andrews, 2009. http://hdl.handle.net/10023/748.
Bayro, Marvin J. "Protein MAS NMR methodology and structural analysis of protein assemblies." Thesis, Massachusetts Institute of Technology, 2010. http://hdl.handle.net/1721.1/57800.
Vita. Cataloged from PDF version of thesis.
Includes bibliographical references.
Methodological developments and applications of solid-state magic-angle spinning nuclear magnetic resonance (MAS NMR) spectroscopy, with particular emphasis on the analysis of protein structure, are described in this thesis. MAS NMR studies of biomolecules ranging from model peptides and proteins in crystalline form to amyloid fibrils and whole bacterial organelles are reported. The methods presented include novel pulse sequences and optimized pulse sequence elements, experimental approaches designed for multiple-spin systems, a protocol for efficient sequential resonance assignment of proteins in the solid state, and techniques to determine the inter-molecular organization of amyloid fibrils formed by moderately sized proteins. Notably, an efficient dipolar recoupling technique, bandselective radio frequency-driven recoupling (BASE RFDR), is introduced and combined with alternating 13C-12C labeling to yield highly sensitive 13C-13C correlation spectra between distant nuclei in proteins. Various applications of the BASE RFDR scheme are presented, including protein resonance assignment, determination of tertiary structure of amyloid fibrils, and variable-temperature studies of protein dynamics. The main biological systems analyzed are amyloid fibrils formed by the SH3 domain of P13 kinase (P13-SH3) and intact gas vesicles from anabaena flos-aquae, for which atomic-level structural information was previously unavailable. P13-SH3 (86 residues) is a system thoroughly studied as a model of protein misfolding and amyloid formation by a natively globular protein. Gas vesicles are bacterial buoyancy organelles, with walls composed almost entirely by a single protein (GvpA, 70 residues), whose formation and structure constitute a highly intriguing biophysical problem. Nearly complete 13C and 'IN resonance assignments and the molecular conformations of the polypeptide backbones of both P13-SH3 and GvpA have been obtained via MAS NMR spectroscopy, enabling the proposal of models for the structure of these two protein assembly systems. In addition, the tertiary structure of P13-SH3 amyloid fibrils has been elucidated by the application of novel methodology introduced in this thesis. Finally, investigations regarding the effects of temperature and protein dynamics on MAS NMR experiments and biomolecular dynamic nuclear polarization studies are presented.
by Marvin J. Bayro.
Ph.D.
Hunnewell, Mary E. "Probing for Conformational Changes in the Repair Enzyme Mfd Using Mutant Protein Constructs." Connect to this title, 2008. https://scholarworks.umass.edu/theses/154.
Agarwal, Vipin. "Development and application of MAS solid state NMR methodologies to biomolecules." Berlin mbv, 2009. http://d-nb.info/998718602/04.
Vahl, Martin [Verfasser]. "Identifizierung von Liganden des G-Protein gekoppelten Rezeptors Mas und Mas-Sequenz-ähnlicher Rezeptoren / Martin Vahl." Berlin : Medizinische Fakultät Charité - Universitätsmedizin Berlin, 2010. http://d-nb.info/102410494X/34.
Raynor, James E. Jr. "Characterization of the mas protein as an angiotensin ii receptor." DigitalCommons@Robert W. Woodruff Library, Atlanta University Center, 1994. http://digitalcommons.auctr.edu/dissertations/2831.
Jordan, Katherine Jo. "Guanidine-stable chymoelastase : a comparative study of its hydrolytic specificity in the presence and absence of denaturant." Virtual Press, 1987. http://liblink.bsu.edu/uhtbin/catkey/481688.
Shevelkov, Veniamin. "Development of MAS solid state NMR methods for structural and dynamical characterization of biomolecules." Doctoral thesis, Humboldt-Universität zu Berlin, Mathematisch-Naturwissenschaftliche Fakultät I, 2011. http://dx.doi.org/10.18452/16260.
Understanding the mechanisms how biological systems work is an important objective of current structural biology. Nuclear magnetic resonance (NMR) spectroscopy is a well suited technique to approach these goals and to study structure and dynamics of biomolecules in order to obtain complimentary information for understanding functionality of proteins. Recently, rapid progress has been made in the field of biological solid state NMR (ssNMR), which resulted in complete structure elucidation of several peptides and small proteins, the characterization of protein complex formation and the characterization of dynamic properties of small proteins. Solid state NMR is the method of choice for structural and dynamic characterization of membrane proteins and aggregated amyloidogenic systems, which are poorly soluble and can not be easily studied by solution state NMR and X-ray spectroscopy. Modern solid state NMR is still limited in resolution and sensitivity, and requires developments in sample preparation and pulse sequence design. In my thesis, I study the potential use of deuteration in protein solid state NMR for sensitivity, as well as for resolution enhancement in 15N-1H correlation experiments. Achieved progress in these fields allows to monitor backbone motion with high accuracy, which has not been available before. We show for the first time that TROSY type experiments can be beneficial for solid state NMR. In addition, a pulse sequence for 13C-13C J decoupling was developed to increase resolution in the carbon dimension.
Books on the topic "MFS proteins":
L, Burlingame A., ed. Biological mass spectrometry. Amsterdam: Elsevier Academic Press, 2005.
(Editor), Regina Murphy, and Amos Tsai (Editor), eds. Misbehaving Proteins: Protein (Mis)Folding, Aggregation, and Stability. Springer, 2006.
Hakim, Alan J., and Rodney Grahame. Hypermobility syndromes. Oxford University Press, 2013. http://dx.doi.org/10.1093/med/9780199642489.003.0159.
Perez, Carlos. Mis Recetas Paleovida: 100 Recetas Paleo para Recuperar una Vida Saludable / Paleo Recipes. Ediciones B, 2017.
Albo, Carmen. Adelgaza sin hambre y con humor con mis recetas proteicas / Lose weight without hunger and humor with my protein recipes: Guisándome la vida. Grijalbo Mondadori Sa, 2013.
Pérez Jiménez, María José. Caracterización del perfil de disfunción mitocondrial en fibroblastos de pacientes con enfermedad de Alzheimer. Universidad Autónoma de Chile, 2018. http://dx.doi.org/10.32457/20.500.12728/87492018dcbm9.
Jara Orellana,, Claudia. Efectos de la proteína Tau sobre la disfunción mitocondrial y el deterioro cognitivo en el envejecimiento. Universidad Autónoma de Chile, 2018. http://dx.doi.org/10.32457/20.500.12728/87452018dcbm6.
Joseph Correa (Nutricionista Deportivo Certificado). Barras de Proteina Caseras para Acelerar el Desarrollo de Musculo para Hockey: Aumente naturalmente el crecimiento de musculo y disminuya la grasa para ganar mas y durar mas tiempo. CreateSpace Independent Publishing Platform, 2015.
Armendano, Andrea, Alda González, and Sergio Roberto Martorelli. Conceptos claves en Biología. Editorial de la Universidad Nacional de La Plata (EDULP), 2016. http://dx.doi.org/10.35537/10915/54497.
Placencia López, Bárbara Miladys, Fernanda Vanessa Alcívar Macías, José Aníbal Sánchez Saltos, Mayra Alejandra Cedeño Mera, Silvia Beatriz Alarcón Barreiro, María Gabriela Pertuz Alarcón, Jacqueline Beatriz Delgado Molina, José Roberto Rodríguez Mera, Agustina Elizabeth Cedeño Casanova, and Christian Paúl Vera Zambrano. Covid 19. Mawil Publicaciones de Ecuador, 2022, 2022. http://dx.doi.org/10.26820/978-9942-602-37-4.
Book chapters on the topic "MFS proteins":
Saidijam, Massoud, Kim E. Bettaney, Dong Leng, Pikyee Ma, Zhiqiang Xu, Jeffrey N. Keen, Nicholas G. Rutherford, et al. "The MFS Efflux Proteins of Gram-Positive and Gram-Negative Bacteria." In Advances in Enzymology - and Related Areas of Molecular Biology, 147–66. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2011. http://dx.doi.org/10.1002/9780470920541.ch4.
Yang, Ziping, Wenkui Li, Harold T. Smith, and Francis L. S. Tse. "LC-MS Bioanalysis of Proteins." In Handbook of LC-MS Bioanalysis, 601–5. Hoboken, NJ, USA: John Wiley & Sons Inc., 2013. http://dx.doi.org/10.1002/9781118671276.ch47.
Hjernø, Karin, and Ole N. Jensen. "MALDI-MS in Protein Chemistry and Proteomics." In MALDI MS, 105–31. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2013. http://dx.doi.org/10.1002/9783527335961.ch3.
Pang, Yongle, Chuan Shi, and Wenying Jian. "Targeted Protein Biomarker Quantitation by LC-MS." In Targeted Biomarker Quantitation by LC-MS, 227–44. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2017. http://dx.doi.org/10.1002/9781119413073.ch15.
Popletaeva, Sofya, Denis Erokhin, and Vitaly Dzhavakhiya. "Comparison of the Protective Activity of Elicitor Proteins MF2 and MF3 Applied Individually or in Combination Against Tobacco Mosaic Virus on Tobacco Leaves." In Agriculture Digitalization and Organic Production, 225–34. Singapore: Springer Nature Singapore, 2023. http://dx.doi.org/10.1007/978-981-99-4165-0_21.
Haselberg, Rob, and Govert W. Somsen. "CE-MS for the analysis of intact proteins." In Capillary Electrophoresis-Mass Spectrometry (CE-MS): Principles and Applications, 159–92. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2016. http://dx.doi.org/10.1002/9783527693801.ch7.
Carter, J. Mark. "Conjugation of Peptide to Carrier Proteins via m-Maleimidobenzoyl-N-Hydroxysuccinimide Ester (MBS)." In Springer Protocols Handbooks, 689–92. Totowa, NJ: Humana Press, 1996. http://dx.doi.org/10.1007/978-1-60327-259-9_118.
Reif, Bernd. "Deuterated Peptides and Proteins: Structure and Dynamics Studies by MAS Solid-State NMR." In Methods in Molecular Biology, 279–301. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-480-3_16.
Tiwari, Vineeta, Vinod Tiwari, Shaoqiu He, Tong Zhang, Srinivasa N. Raja, Xinzhong Dong, and Yun Guan. "Mas-Related G Protein-Coupled Receptors Offer Potential New Targets for Pain Therapy." In Advances in Experimental Medicine and Biology, 87–103. Dordrecht: Springer Netherlands, 2016. http://dx.doi.org/10.1007/978-94-017-7537-3_7.
Van Remoortel, Samuel, and Jean-Pierre Timmermans. "Mas-Related G Protein-Coupled Receptors (Mrgprs) as Mediators of Gut Neuro-Immune Signaling." In Advances in Experimental Medicine and Biology, 259–69. Cham: Springer International Publishing, 2022. http://dx.doi.org/10.1007/978-3-031-05843-1_25.
Conference papers on the topic "MFS proteins":
Júnior, Nino Sérgio Lemos De Oliveira, Keilane Silva Farias, and Carlos Priminho Pirovani. "AVALIAÇÃO DO EFEITO DE UMA CANDIDATA A EFETORA EM ALPISTE (PHALARIS CANARIENSIS) E EM TOMATE (SOLANUM LYCOPERSICUM)." In II Congresso Brasileiro de Biotecnologia On-line. Revista Multidisciplinar de Educação e Meio Ambiente, 2022. http://dx.doi.org/10.51189/conbiotec/30.
Mukai, Masahiro, and Ayae Honda. "Analysis of promoter binding proteins of Ebp1 that is inhibitor protein of influenza virus RNA polymerase." In 2009 International Symposium on Micro-NanoMechatronics and Human Science (MHS). IEEE, 2009. http://dx.doi.org/10.1109/mhs.2009.5351934.
Dodge, Taylor N., Jeana L. Drake, Paul Falkowski, and Liesl Hotaling. "Evolution of biomineralization proteins in Cnidaria." In OCEANS 2015 - MTS/IEEE Washington. IEEE, 2015. http://dx.doi.org/10.23919/oceans.2015.7404525.
Athayde, Natália Merten, and Alzira Alves de Siqueira Carvalho. "The heart of myofibrillary myopathy." In XIII Congresso Paulista de Neurologia. Zeppelini Editorial e Comunicação, 2021. http://dx.doi.org/10.5327/1516-3180.457.
Sidhu, A. S., T. S. Dillon, B. S. Sidhu, and E. Chang. "Protein Ontology Project: 2006 updates." In DATA MINING AND MIS 2006. Southampton, UK: WIT Press, 2006. http://dx.doi.org/10.2495/data060301.
Sousa-Santos, Patrick, Tarcísio Alvarenga, Pedro Pozzobon, Ana Beatriz Baston, Ana Flavia Lemos, Maria C. Foloni, Itamar Andrade, Luis Lopes, and Igor Teixeira. "Miller-Fisher syndrome in puerperium." In XIV Congresso Paulista de Neurologia. Zeppelini Editorial e Comunicação, 2023. http://dx.doi.org/10.5327/1516-3180.141s1.703.
Nitta, Takahiro. "In silico design of guiding tracks for molecular shuttles powered by motor proteins." In 2011 International Symposium on Micro-NanoMechatronics and Human Science (MHS). IEEE, 2011. http://dx.doi.org/10.1109/mhs.2011.6102250.
Kuriki, Hiroki, Sou Takasawa, Shinya Sakuma, Genji Kurisu, Fumihito Arai, and Yoko Yamanishi. "Electrically-induced bubble knife for protein crystallization and processing." In 2013 International Symposium on Micro-NanoMechatronics and Human Science (MHS). IEEE, 2013. http://dx.doi.org/10.1109/mhs.2013.6710474.
XAVIER, WILLIAM, FRANCISCO ERNANI ALVES MAGALHãES, ANTONIO EUFRáSIO VIEIRA NETO, ANTONIO ROMáRIO COELHO ALCâNTARA, KALINA KELMA OLIVEIRA DE SOUSA, MICHELINE SOARES COSTA OLIVEIRA, and ANA CRISTINA DE OLIVEIRA MONTEIRO MOREIRA. "ESTUDO IN SILICO DAS BASES MOLECULARES DE INTERAÇÃO ENTRE O ÁCIDO OLEANÓLICO E O RECEPTOR TGR5." In II Brazilian Congress of Development. DEV2021, 2021. http://dx.doi.org/10.51162/brc.dev2021-0056.
Katayama, Yoshiki, Hirotaro Kitazaki, Jeong-Hun Kang, Xiaoming Han, Takeshi Mori, and Takuro Niidome. "High-throughput Detection of Protein Kinase Activities in Cell Lysate Based on the Aggregation of Gold Nanoparticles with Peptides." In 2009 MRS Spring Meet. Materials Research Society, 2009. http://dx.doi.org/10.1557/proc-1241-xx08-08.
Reports on the topic "MFS proteins":
Yalovsky, Shaul, and Julian Schroeder. The function of protein farnesylation in early events of ABA signal transduction in stomatal guard cells of Arabidopsis. United States Department of Agriculture, January 2002. http://dx.doi.org/10.32747/2002.7695873.bard.
Epel, Bernard, and Roger Beachy. Mechanisms of intra- and intercellular targeting and movement of tobacco mosaic virus. United States Department of Agriculture, November 2005. http://dx.doi.org/10.32747/2005.7695874.bard.
Czosnek, Henryk Hanokh, Dani Zamir, Robert L. Gilbertson, and Lucas J. William. Resistance to Tomato Yellow Leaf Curl Virus by Combining Expression of a Natural Tolerance Gene and a Dysfunctional Movement Protein in a Single Cultivar. United States Department of Agriculture, June 2000. http://dx.doi.org/10.32747/2000.7573079.bard.
Fluhr, Robert, and Maor Bar-Peled. Novel Lectin Controls Wound-responses in Arabidopsis. United States Department of Agriculture, January 2012. http://dx.doi.org/10.32747/2012.7697123.bard.
Tucker, Mark L., Shimon Meir, Amnon Lers, Sonia Philosoph-Hadas, and Cai-Zhong Jiang. Elucidation of signaling pathways that regulate ethylene-induced leaf and flower abscission of agriculturally important plants. United States Department of Agriculture, January 2012. http://dx.doi.org/10.32747/2012.7597929.bard.
Blumwald, Eduardo, and Avi Sadka. Citric acid metabolism and mobilization in citrus fruit. United States Department of Agriculture, October 2007. http://dx.doi.org/10.32747/2007.7587732.bard.
MARTÍNEZ LEAL, LAURA DE LA CRUZ, and Carlos Romá Mateo. Preliminary proteomics analysis of the potential use of HMGB1 as sepsis biomarker. Fundación Avanza, May 2023. http://dx.doi.org/10.60096/fundacionavanza/2312022.
Sengupta-Gopalan, Champa, Shmuel Galili, and Rachel Amir. Improving Methionine Content in Transgenic Forage Legumes. United States Department of Agriculture, February 2001. http://dx.doi.org/10.32747/2001.7580671.bard.
Whitham, Steven A., Amit Gal-On, and Victor Gaba. Post-transcriptional Regulation of Host Genes Involved with Symptom Expression in Potyviral Infections. United States Department of Agriculture, June 2012. http://dx.doi.org/10.32747/2012.7593391.bard.
Medrano, Juan, Adam Friedmann, Moshe (Morris) Soller, Ehud Lipkin, and Abraham Korol. High resolution linkage disequilibrium mapping of QTL affecting milk production traits in Israel Holstein dairy cattle. United States Department of Agriculture, March 2008. http://dx.doi.org/10.32747/2008.7696509.bard.