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I. Corbacho
Departamento de Didáctica de las Ciencias Experimentales y Matemáticas, Facultad de Educación, Universidad de Extremadura, 06006 Badajoz, Spain

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Journal article
Published: 18 March 2021 in Sustainability
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Enhancing the emotional dimension of prospective teachers in science subjects—which has become increasingly important in recent decades—is a responsibility of higher education institutions. The implementation of active methodologies has the potential to modify the traditional student-teacher roles that are encouraged by the educational policies implemented in the Bologna Process. Simultaneously, it is possible to promote knowledge of sustainability, as well as the attitudes and behaviors required by UNESCO. The main aim of this work is to describe a project-based learning methodology with a transversal sustainability approach (low-cost and eco-friendly) and to introduce this as a potential resource for the emotional and cognitive improvement of 19 prospective primary teachers enrolled in scientific subjects. This is a qualitative study in the context of a research line focused on higher education for sustainable development. A questionnaire was designed and filled in by students at two different stages, before and after implementation of the activity. The initial feedback from students was surprisingly enthusiastic due to the fact that they were working with rockets, despite this not being considered a common emotion expressed by students in science lessons. The results show the emotional improvement of prospective teachers after implementation of the activity. It is concluded that a good science education, with implementation of sustainable approaches is necessary during the training of teachers, taking into account their emotional dimensions and social repercussions as a consequence of future transmission.

ACS Style

Míriam Hernández-Barco; Jesús Sánchez-Martín; Isaac Corbacho-Cuello; Florentina Cañada-Cañada. Emotional Performance of a Low-Cost Eco-Friendly Project Based Learning Methodology for Science Education: An Approach in Prospective Teachers. Sustainability 2021, 13, 3385 .

AMA Style

Míriam Hernández-Barco, Jesús Sánchez-Martín, Isaac Corbacho-Cuello, Florentina Cañada-Cañada. Emotional Performance of a Low-Cost Eco-Friendly Project Based Learning Methodology for Science Education: An Approach in Prospective Teachers. Sustainability. 2021; 13 (6):3385.

Chicago/Turabian Style

Míriam Hernández-Barco; Jesús Sánchez-Martín; Isaac Corbacho-Cuello; Florentina Cañada-Cañada. 2021. "Emotional Performance of a Low-Cost Eco-Friendly Project Based Learning Methodology for Science Education: An Approach in Prospective Teachers." Sustainability 13, no. 6: 3385.

Journal article
Published: 10 September 2020 in Sustainability
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In the context of climatic emergency, teaching for sustainability is crucial to transform damaging behavioral social paths into sustainable ones. In this contribution, we focus on the relevance of the Degree in Primary Education to reach this change, assessing through the Sustainability Consciousness Questionnaire (SCQ) the sustainability awareness of a sample of 151 students of this bachelor’s degree. SPSS and JASP statistical programs were used for data analyses and graphical representations. The results support that this test is appropriate to estimate the different dimensions of sustainability consciousness of Spanish pre-service primary teachers. Specifically, we found that these students assign higher scores to items of sustainability knowingness and sustainability attitudes above all in the social dimension. Some gender differences are found in sustainability behavior, which is higher in the male subset for the economic dimension. Correlation analysis reveals positive associations between sustainability knowingness and sustainability attitudes, whereas sustainability behavior is positively related to both constructs but only in the social dimension. These results highlight the necessity of teaching sustainability looking for behavioral changes in the Degree of Primary Education.

ACS Style

José María Marcos-Merino; Isaac Corbacho-Cuello; Míriam Hernández-Barco. Analysis of Sustainability Knowingness, Attitudes and Behavior of a Spanish Pre-Service Primary Teachers Sample. Sustainability 2020, 12, 7445 .

AMA Style

José María Marcos-Merino, Isaac Corbacho-Cuello, Míriam Hernández-Barco. Analysis of Sustainability Knowingness, Attitudes and Behavior of a Spanish Pre-Service Primary Teachers Sample. Sustainability. 2020; 12 (18):7445.

Chicago/Turabian Style

José María Marcos-Merino; Isaac Corbacho-Cuello; Míriam Hernández-Barco. 2020. "Analysis of Sustainability Knowingness, Attitudes and Behavior of a Spanish Pre-Service Primary Teachers Sample." Sustainability 12, no. 18: 7445.

Conference paper
Published: 17 June 2020 in Proceedings of SOCIOINT 2020- 7th International Conference on Education and Education of Social Sciences
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ACS Style

Miriam Hernández Del Barco; Florentina Cañada; Isaac Corbacho-Cuello; Jesús Sánchez-Martín. “HARD SCIENCES” AND “SOFT SCIENCES”: A NECESSARY DIFFERENTIATION IN TEACHING SCIENCES TO PRIMARY PRE-SERVICE TEACHERS. Proceedings of SOCIOINT 2020- 7th International Conference on Education and Education of Social Sciences 2020, 1 .

AMA Style

Miriam Hernández Del Barco, Florentina Cañada, Isaac Corbacho-Cuello, Jesús Sánchez-Martín. “HARD SCIENCES” AND “SOFT SCIENCES”: A NECESSARY DIFFERENTIATION IN TEACHING SCIENCES TO PRIMARY PRE-SERVICE TEACHERS. Proceedings of SOCIOINT 2020- 7th International Conference on Education and Education of Social Sciences. 2020; ():1.

Chicago/Turabian Style

Miriam Hernández Del Barco; Florentina Cañada; Isaac Corbacho-Cuello; Jesús Sánchez-Martín. 2020. "“HARD SCIENCES” AND “SOFT SCIENCES”: A NECESSARY DIFFERENTIATION IN TEACHING SCIENCES TO PRIMARY PRE-SERVICE TEACHERS." Proceedings of SOCIOINT 2020- 7th International Conference on Education and Education of Social Sciences , no. : 1.

Conference paper
Published: 17 June 2020 in Proceedings of SOCIOINT 2020- 7th International Conference on Education and Education of Social Sciences
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ACS Style

Miriam Hernández Del Barco; Florentina Cañada; Isaac Corbacho-Cuello; Jesús Sánchez-Martín. RELATIONSHIP BETWEEN AFFECTIVE DOMAIN AND MULTIPLE INTELLIGENCES OF SCIENCE PRIMARY PRE-SERVICE TEACHER. Proceedings of SOCIOINT 2020- 7th International Conference on Education and Education of Social Sciences 2020, 1 .

AMA Style

Miriam Hernández Del Barco, Florentina Cañada, Isaac Corbacho-Cuello, Jesús Sánchez-Martín. RELATIONSHIP BETWEEN AFFECTIVE DOMAIN AND MULTIPLE INTELLIGENCES OF SCIENCE PRIMARY PRE-SERVICE TEACHER. Proceedings of SOCIOINT 2020- 7th International Conference on Education and Education of Social Sciences. 2020; ():1.

Chicago/Turabian Style

Miriam Hernández Del Barco; Florentina Cañada; Isaac Corbacho-Cuello; Jesús Sánchez-Martín. 2020. "RELATIONSHIP BETWEEN AFFECTIVE DOMAIN AND MULTIPLE INTELLIGENCES OF SCIENCE PRIMARY PRE-SERVICE TEACHER." Proceedings of SOCIOINT 2020- 7th International Conference on Education and Education of Social Sciences , no. : 1.

Journal article
Published: 09 July 2018 in Neuropharmacology
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The phenothiazine methylene blue (MB) is attracting increasing attention because it seems to have beneficial effects in the pathogenesis of Alzheimer's disease (AD). Among other factors, the presence of neuritic plaques of amyloid-β peptide (Aβ) aggregates, neurofibrilar tangles of tau and perturbation of cytosolic Ca2+ are important players of the disease. It has been proposed that MB decreases the formation of neuritic plaques due to Aβ aggregation. However, the molecular mechanism underlying this effect is far from clear. In this work, we show that MB stimulates the Ca2+-ATPase activity of the plasma membrane Ca2+-ATPase (PMCA) in human tissues from AD-affected brain and age-matched controls and also from pig brain and cell cultures. In addition, MB prevents and even blocks the inhibitory effect of Aβ on PMCA activity. Functional analysis with mutants and fluorescence experiments strongly suggest that MB binds to PMCA, at the C-terminal tail, in a site located close to the last transmembrane helix and also that MB binds to the peptide. Besides, Aβ increases PMCA affinity for MB. These results point out a novel molecular basis of MB action on Aβ and PMCA as mediator of its beneficial effect on AD.

ACS Style

Maria Berrocal; Isaac Corbacho; Carlos Gutierrez-Merino; Ana M. Mata. Methylene blue activates the PMCA activity and cross-interacts with amyloid β-peptide, blocking Aβ-mediated PMCA inhibition. Neuropharmacology 2018, 139, 163 -172.

AMA Style

Maria Berrocal, Isaac Corbacho, Carlos Gutierrez-Merino, Ana M. Mata. Methylene blue activates the PMCA activity and cross-interacts with amyloid β-peptide, blocking Aβ-mediated PMCA inhibition. Neuropharmacology. 2018; 139 ():163-172.

Chicago/Turabian Style

Maria Berrocal; Isaac Corbacho; Carlos Gutierrez-Merino; Ana M. Mata. 2018. "Methylene blue activates the PMCA activity and cross-interacts with amyloid β-peptide, blocking Aβ-mediated PMCA inhibition." Neuropharmacology 139, no. : 163-172.

Journal article
Published: 01 June 2017 in Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
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The disruption of Ca2 + signaling in neurons, together with a failure to keep optimal intracellular Ca2 + concentrations, have been proposed as significant factors for neuronal dysfunction in the Ca2 + hypothesis of Alzheimer's disease (AD). Tau is a protein that plays an essential role in axonal transport and can form abnormal structures such as neurofibrillary tangles that constitute one of the hallmarks of AD. We have recently shown that plasma membrane Ca2 +-ATPase (PMCA), a key enzyme in the maintenance of optimal cytosolic Ca2 + levels in cells, is inhibited by tau in membrane vesicles. In the present study we show that tau inhibits synaptosomal PMCA purified from pig cerebrum, and reconstituted in phosphatidylserine-containing lipid bilayers, with a Ki value of 1.5 ± 0.2 nM tau. Noteworthy, the inhibitory effect of tau is dependent on the charge of the phospholipid used for PMCA reconstitution. In addition, nanomolar concentrations of calmodulin, the major endogenous activator of PMCA, protects against inhibition of the Ca2 +-ATPase activity by tau. Our results in a cellular model such as SH-SY5Y human neuroblastoma cells yielded an inhibition of PMCA by nanomolar tau concentrations and protection by calmodulin against this inhibition similar to those obtained with purified synaptosomal PMCA. Functional studies were also performed with native and truncated versions of human cerebral PMCA4b, an isoform that has been showed to be functionally regulated by amyloid peptides, whose aggregates constitutes another hallmark of AD. Kinetic assays point out that tau binds to the C-terminal tail of PMCA, at a site distinct but close to the calmodulin binding domain. In conclusion, PMCA can be seen as a molecular target for tau-induced cytosolic calcium dysregulation in synaptic terminals.

ACS Style

María Berrocal; Isaac Corbacho; M. Rosario Sepulveda; Carlos Gutierrez-Merino; Ana M. Mata. Phospholipids and calmodulin modulate the inhibition of PMCA activity by tau. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 2017, 1864, 1028 -1035.

AMA Style

María Berrocal, Isaac Corbacho, M. Rosario Sepulveda, Carlos Gutierrez-Merino, Ana M. Mata. Phospholipids and calmodulin modulate the inhibition of PMCA activity by tau. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 2017; 1864 (6):1028-1035.

Chicago/Turabian Style

María Berrocal; Isaac Corbacho; M. Rosario Sepulveda; Carlos Gutierrez-Merino; Ana M. Mata. 2017. "Phospholipids and calmodulin modulate the inhibition of PMCA activity by tau." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1864, no. 6: 1028-1035.

Journal article
Published: 01 May 2017 in Biochemical and Biophysical Research Communications
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Amyloid β-peptides (Aβ) are a major hallmark of Alzheimer's disease (AD) and their neurotoxicity develop with cytosolic calcium dysregulation. On the other hand, calmodulin (CaM), a protein which plays a major multifunctional role in neuronal calcium signaling, has been shown to be involved in the regulation of non-amyloidogenic processing of amyloid β precursor protein (APP). Using fluorescent 6-bromoacetyl-2-dimethylaminonaphthalene derivatives of CaM, Badan-CaM, and human amyloid β(1-42) HiLyte™-Fluor555, we show in this work that Aβ binds with high affinity to CaM through the neurotoxic Aβ25-35 domain. In addition, the affinity of Aβ for calcium-saturated CaM conformation is approximately 20-fold higher than for CaM conformation in the absence of calcium (apo-CaM). Moreover, the value of Kd of 0.98 ± 0.11 nM obtained for Aβ1-42 dissociation from CaM saturated by calcium points out that CaM is one of the cellular targets with highest affinity for neurotoxic Aβ peptides. A major functional consequence of Aβ-CaM interaction is that it slowdowns Aβ fibrillation. The novel and high affinity interaction between calmodulin and Aβ shown in this work opens a yet-unexplored gateway to further understand the neurotoxic effect of Aβ in different neural cells and also to address the potential of calmodulin and calmodulin-derived peptides as therapeutic agents in AD.

ACS Style

Isaac Corbacho; María Berrocal; Katalin Török; Ana M. Mata; Carlos Gutierrez-Merino. High affinity binding of amyloid β -peptide to calmodulin: Structural and functional implications. Biochemical and Biophysical Research Communications 2017, 486, 992 -997.

AMA Style

Isaac Corbacho, María Berrocal, Katalin Török, Ana M. Mata, Carlos Gutierrez-Merino. High affinity binding of amyloid β -peptide to calmodulin: Structural and functional implications. Biochemical and Biophysical Research Communications. 2017; 486 (4):992-997.

Chicago/Turabian Style

Isaac Corbacho; María Berrocal; Katalin Török; Ana M. Mata; Carlos Gutierrez-Merino. 2017. "High affinity binding of amyloid β -peptide to calmodulin: Structural and functional implications." Biochemical and Biophysical Research Communications 486, no. 4: 992-997.

Journal article
Published: 01 April 2016 in Protein Expression and Purification
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Human plasma membrane calcium ATPases (PMCAs) are highly regulated transporters responsible for the extrusion of calcium out of the cell. Since calcium homeostasis is implicated in several diseases and neurodegenerative disorders, understanding PMCAs activity is crucial. One of the major hindrances is the availability of these proteins for functional and structural analysis. Here, using the yeast Saccharomyces cerevisiae system, we show a new and enhanced method for the expression of the full-length human PMCA isoform 4b (hPMCA4b) and a truncated form lacking its auto-inhibitory domain. We have also improved a method for the purification of the native isoform by calmodulin-agarose affinity chromatography, and developed a new method to purify the truncated isoform by glutathione-Sepharose affinity chromatography. One of the most relevant features of this work is that, when compared to PMCAs purification from pig brain, our method provides a pure single isoform instead of a mixture of isoforms, essential for fine-tuning the activity of PMCA4b. Another relevant feature is that the method described in this work has a superior yield of protein than previously established methods to purify PMCA proteins expressed in yeasts.

ACS Style

Isaac Corbacho; Francisco Fernández García-Prieto; Ara E. Hinojosa; María Berrocal; Ana M. Mata. An improved method for expression and purification of functional human Ca2+ transporter PMCA4b in Saccharomyces cerevisiae. Protein Expression and Purification 2016, 120, 51 -58.

AMA Style

Isaac Corbacho, Francisco Fernández García-Prieto, Ara E. Hinojosa, María Berrocal, Ana M. Mata. An improved method for expression and purification of functional human Ca2+ transporter PMCA4b in Saccharomyces cerevisiae. Protein Expression and Purification. 2016; 120 ():51-58.

Chicago/Turabian Style

Isaac Corbacho; Francisco Fernández García-Prieto; Ara E. Hinojosa; María Berrocal; Ana M. Mata. 2016. "An improved method for expression and purification of functional human Ca2+ transporter PMCA4b in Saccharomyces cerevisiae." Protein Expression and Purification 120, no. : 51-58.

Journal article
Published: 01 July 2015 in Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease
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Ca(2+)-ATPases are plasma membrane and intracellular membrane transporters that use the energy of ATP hydrolysis to pump cytosolic Ca(2+) out of the cell (PMCA) or into internal stores. These pumps are the main high-affinity Ca(2+) systems involved in the maintenance of intracellular free Ca(2+) at the properly low level in eukaryotic cells. The failure of neurons to keep optimal intracellular Ca(2+) concentrations is a common feature of neurodegeneration by aging and aging-linked neuropathologies, such as Alzheimer's disease (AD). This disease is characterized by the accumulation of β-amyloid senile plaques and neurofibrillary tangles of tau, a protein that plays a key role in axonal transport. Here we show a novel inhibition of PMCA activity by tau which is concentration-dependent. The extent of inhibition significantly decreases with aging in mice and control human brain membranes, but inhibition profiles were similar in AD-affected brain membrane preparations, independently of age. No significant changes in PMCA expression and localization with aging or neuropathology were found. These results point out a link between Ca(2+)-transporters, aging and neurodegeneration mediated by tau protein.

ACS Style

María Berrocal; Isaac Corbacho; María Vázquez-Hernández; Jesus Avila; M. Rosario Sepulveda; Ana M. Mata. Inhibition of PMCA activity by tau as a function of aging and Alzheimer's neuropathology. Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease 2015, 1852, 1465 -1476.

AMA Style

María Berrocal, Isaac Corbacho, María Vázquez-Hernández, Jesus Avila, M. Rosario Sepulveda, Ana M. Mata. Inhibition of PMCA activity by tau as a function of aging and Alzheimer's neuropathology. Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 2015; 1852 (7):1465-1476.

Chicago/Turabian Style

María Berrocal; Isaac Corbacho; María Vázquez-Hernández; Jesus Avila; M. Rosario Sepulveda; Ana M. Mata. 2015. "Inhibition of PMCA activity by tau as a function of aging and Alzheimer's neuropathology." Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease 1852, no. 7: 1465-1476.

Journal article
Published: 01 December 2014 in Journal of Biological Chemistry
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Fast inhibitory glycinergic transmission occurs in spinal cord, brainstem and retina to modulate the processing of motor and sensory information. After synaptic vesicle fusion, glycine is recovered back to the presynaptic terminal by the neuronal glycine transporter GlyT2 to maintain quantal glycine content in synaptic vesicles. The loss of presynaptic GlyT2 drastically impairs the refilling of glycinergic synaptic vesicles and severely disrupts neurotransmission. Indeed, mutations in the gene encoding GlyT2 are the main presynaptic cause of hyperekplexia in humans. Here we show a novel endogenous regulatory mechanism that can modulate GlyT2 activity based on a compartmentalized interaction between GlyT2, neuronal PMCA isoforms 2 and 3 and Na+/Ca2+- exchanger 1 (NCX1). This GlyT2/PMCA2-3/NCX1 complex is found in lipid raft subdomains where GlyT2 has been previously found to be fully active. We show that endogenous PMCA and NCX activities are necessary for GlyT2 activity and that this modulation depends on lipid raft integrity. Besides, we propose a model in which GlyT2/PMCA2-3/NCX complex would help Na+/K+‐ATPase in controlling local Na+ increases derived from GlyT2 activity after neurotransmitter release.

ACS Style

Jaime de Juan-Sanz; Enrique Núñez; Francisco Zafra; María Berrocal; Isaac Corbacho; Ignacio Ibáñez; Esther Arribas Gonzalez; Daniel Marcos; Beatriz Lopez Corcuera; Ana M. Mata; Carmen Aragón. Presynaptic Control of Glycine Transporter 2 (GlyT2) by Physical and Functional Association with Plasma Membrane Ca2+-ATPase (PMCA) and Na+-Ca2+ Exchanger (NCX). Journal of Biological Chemistry 2014, 289, 34308 -34324.

AMA Style

Jaime de Juan-Sanz, Enrique Núñez, Francisco Zafra, María Berrocal, Isaac Corbacho, Ignacio Ibáñez, Esther Arribas Gonzalez, Daniel Marcos, Beatriz Lopez Corcuera, Ana M. Mata, Carmen Aragón. Presynaptic Control of Glycine Transporter 2 (GlyT2) by Physical and Functional Association with Plasma Membrane Ca2+-ATPase (PMCA) and Na+-Ca2+ Exchanger (NCX). Journal of Biological Chemistry. 2014; 289 (49):34308-34324.

Chicago/Turabian Style

Jaime de Juan-Sanz; Enrique Núñez; Francisco Zafra; María Berrocal; Isaac Corbacho; Ignacio Ibáñez; Esther Arribas Gonzalez; Daniel Marcos; Beatriz Lopez Corcuera; Ana M. Mata; Carmen Aragón. 2014. "Presynaptic Control of Glycine Transporter 2 (GlyT2) by Physical and Functional Association with Plasma Membrane Ca2+-ATPase (PMCA) and Na+-Ca2+ Exchanger (NCX)." Journal of Biological Chemistry 289, no. 49: 34308-34324.

Journal article
Published: 18 January 2012 in FEMS Yeast Research
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The V-ATPase of Saccharomyces cerevisiae is an ATP-dependent proton pump responsible for acidification of the vacuole and other internal compartments including the whole secretory pathway. We have studied the behavior of several glycoprotein processing reactions occurring in different Golgi compartments of representative vmaΔ mutants. We found that outer chain initiation is not altered in the mutants while mannosylphosphate transfer, α(1, 3)-linked mannoses addition, and α factor maturation seem to be affected. The results suggest a gradation in the dependence of Golgi functions on V-ATPase activity, from early Golgi (unaffected) to late Golgi (significantly reduced). These findings are in agreement with the internal pH of Golgi cisternae measured in mammalian cells, which is more acidic in the late region. The mutant defects can be partially restored by buffering the external medium to pH 6.0, which supports the existence of a mechanism that, in the absence of a functional V-ATPase, could contribute to pH regulation at least in the late Golgi.

ACS Style

Isaac Corbacho; Francisco Teixidó; Isabel Olivero; Luis M Hernandez. Dependence of Saccharomyces cerevisiae Golgi functions on V-ATPase activity. FEMS Yeast Research 2012, 12, 341 -350.

AMA Style

Isaac Corbacho, Francisco Teixidó, Isabel Olivero, Luis M Hernandez. Dependence of Saccharomyces cerevisiae Golgi functions on V-ATPase activity. FEMS Yeast Research. 2012; 12 (3):341-350.

Chicago/Turabian Style

Isaac Corbacho; Francisco Teixidó; Isabel Olivero; Luis M Hernandez. 2012. "Dependence of Saccharomyces cerevisiae Golgi functions on V-ATPase activity." FEMS Yeast Research 12, no. 3: 341-350.

Journal article
Published: 01 December 2010 in Antonie van Leeuwenhoek
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Conventional complex media are routinely used to grow auxotrophic strains under the assumption that they can compensate the latter’s nutritional deficiencies. We here demonstrate that this is not always true. This study compares the growth parameters of Saccharomyces cerevisiae (S288C) and its derived auxotrophic strains FY1679-14C and BY4741 in synthetic minimal medium (SD), standard YPD medium from two of the most commonly used suppliers, or modified YPD medium. Maximum specific growth rates of auxotrophic strains were slightly lower than the prototrophic case in all growth conditions tested. Also, the biomass production of auxotrophic strains in synthetic medium was slightly less than the prototrophic case. However in both of the two standard YPD media used, the biomass production of both auxotrophic strains was markedly lower than that of the prototrophic one. The extent of the differences depended on the medium used. Indeed in one of the two YPD media, the lower biomass production of auxotrophic strains was evident even at the diauxic shift. Uracil seems to be the main limiting growth factor for both auxotrophic strains growing in the two standard YPD medium tested. No YPD media or specific supplement was able to compensate for the effect of the auxotrophic mutations in the multiple auxotrophic marker strain BY4741. The fact that auxotrophic strains grew poorly on YPD when compared to their prototrophic counterpart indicates that standard YPD medium is not sufficient to overcome the effect of auxotrophic mutations.

ACS Style

Isaac Corbacho; Francisco Teixidó; Rocío Velázquez; Luis M. Hernández; Isabel Olivero. Standard YPD, even supplemented with extra nutrients, does not always compensate growth defects of Saccharomyces cerevisiae auxotrophic strains. Antonie van Leeuwenhoek 2010, 99, 591 -600.

AMA Style

Isaac Corbacho, Francisco Teixidó, Rocío Velázquez, Luis M. Hernández, Isabel Olivero. Standard YPD, even supplemented with extra nutrients, does not always compensate growth defects of Saccharomyces cerevisiae auxotrophic strains. Antonie van Leeuwenhoek. 2010; 99 (3):591-600.

Chicago/Turabian Style

Isaac Corbacho; Francisco Teixidó; Rocío Velázquez; Luis M. Hernández; Isabel Olivero. 2010. "Standard YPD, even supplemented with extra nutrients, does not always compensate growth defects of Saccharomyces cerevisiae auxotrophic strains." Antonie van Leeuwenhoek 99, no. 3: 591-600.

Conference paper
Published: 01 December 2010 in Microorganisms in Industry and Environment
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We describe a group of experiments designed to set up a reproducible and reliable method for in vivo vacuole staining in Saccharomyces cerevisiae using neutral red, a vital dye previously used to stain intracellular organelles from plants and animals. In addition, we have compared the usage of neutral red with the use of quinacrine, a fluorescent dye that can accumulate in acidic compartments too. Advantages and disadvantages of both methods in vacuole acidification assays are discussed.

ACS Style

Isaac Corbacho; F. Teixidó; R. Velázquez; L.M. Hernández; I. Olivero; A Mendez-Vilas. Yeast vacuole staining using quinacrine and neutral red. Microorganisms in Industry and Environment 2010, 659 -661.

AMA Style

Isaac Corbacho, F. Teixidó, R. Velázquez, L.M. Hernández, I. Olivero, A Mendez-Vilas. Yeast vacuole staining using quinacrine and neutral red. Microorganisms in Industry and Environment. 2010; ():659-661.

Chicago/Turabian Style

Isaac Corbacho; F. Teixidó; R. Velázquez; L.M. Hernández; I. Olivero; A Mendez-Vilas. 2010. "Yeast vacuole staining using quinacrine and neutral red." Microorganisms in Industry and Environment , no. : 659-661.

Journal article
Published: 27 July 2010 in Glycobiology
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The MNN3 gene of Saccharomyces cerevisiae has been identified as a synonym of VPS74. We have compared phenotype characteristics of the original mnn3 mutant, including low dye binding phenotype, size of external invertase, clump formation, and sodium orthovanadate resistance and found these to be identical to those shown by vps74Δ. Mating of both haploid strains resulted in non-complementation of mutant phenotypes. Finally, a vector containing wild-type VPS74 complemented the defects of both vps74Δ and mnn3. This work completes the identification of the entire collection of genes that are defective in mnn mutants. In addition, we have identified the mnn3 mutation by sequencing the VPS74 gene from the original mnn3 strain. We found a single amino acid change of Arg97 to Cys. This unique alteration seems to be sufficient to account for the phenotype of mnn3.

ACS Style

Isaac Corbacho; Isabel Olivero; Luis M Hernández. Identification of the MNN3 gene of Saccharomyces cerevisiae. Glycobiology 2010, 20, 1336 -1340.

AMA Style

Isaac Corbacho, Isabel Olivero, Luis M Hernández. Identification of the MNN3 gene of Saccharomyces cerevisiae. Glycobiology. 2010; 20 (11):1336-1340.

Chicago/Turabian Style

Isaac Corbacho; Isabel Olivero; Luis M Hernández. 2010. "Identification of the MNN3 gene of Saccharomyces cerevisiae." Glycobiology 20, no. 11: 1336-1340.

Books
Published: 31 October 2007 in Environmental Forensics
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ACS Style

A. Méndez-Vilas; Isaac Corbacho; M. L. González-Martín; M. J. Nuevo. Physical characterization of wild type and mnn9 mutant cells of Saccharomyces cerevisiae by Atomic force microscopy (AFM). Environmental Forensics 2007, 50 -57.

AMA Style

A. Méndez-Vilas, Isaac Corbacho, M. L. González-Martín, M. J. Nuevo. Physical characterization of wild type and mnn9 mutant cells of Saccharomyces cerevisiae by Atomic force microscopy (AFM). Environmental Forensics. 2007; ():50-57.

Chicago/Turabian Style

A. Méndez-Vilas; Isaac Corbacho; M. L. González-Martín; M. J. Nuevo. 2007. "Physical characterization of wild type and mnn9 mutant cells of Saccharomyces cerevisiae by Atomic force microscopy (AFM)." Environmental Forensics , no. : 50-57.

Journal article
Published: 19 April 2006 in Antonie van Leeuwenhoek
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The MNN2 gene of S. cerevisiae encodes an alpha (1,2) mannosyl transferase required for branching the outer chain of N-linked oligosaccharides (Rayner J.C. and Munro S. 1998. J. Biol. Chem. 273: 26836-26843) and it also seems to have some effect on the transfer of mannosyl phosphate groups to the inner core (Olivero I. et al. 2000. FEBS Lett. 475: 111-116). In order to reveal possible interactions of MNN2 expression with other cellular pathways, we analyzed the transcriptome of the deletion mutant S. cerevisiae mnn2 Delta using cDNA microarrays. We found 151 genes that showed an altered expression level of > or =2-fold, 58 of them up-regulated and 93 down-regulated. Quite a high proportion of these genes (29%) encode unclassified proteins. In contrast to other defects affecting the integrity of the cell wall, deletion of MNN2 does not stimulate the expression of any of the genes included in the previously defined 'cell wall compensatory cluster' (Lagorce et al. 2003. J. Biol. Chem. 278: 20345-20357). We also found that 15% of the selected genes are related to central metabolic pathways. In addition, the mnn2 Delta strain seems to have a certain level of stimulation of DNA processing reactions while some genes involved in intracellular transport pathways are under-regulated.

ACS Style

Isaac Corbacho; Isabel Olivero; Stefan Hohmann; Per Sunnerhagen; Luis M. Hernández. Genome-wide expression profile of the mnn2Δ mutant of Saccharomyces cerevisiae. Antonie van Leeuwenhoek 2006, 89, 485 -494.

AMA Style

Isaac Corbacho, Isabel Olivero, Stefan Hohmann, Per Sunnerhagen, Luis M. Hernández. Genome-wide expression profile of the mnn2Δ mutant of Saccharomyces cerevisiae. Antonie van Leeuwenhoek. 2006; 89 (3-4):485-494.

Chicago/Turabian Style

Isaac Corbacho; Isabel Olivero; Stefan Hohmann; Per Sunnerhagen; Luis M. Hernández. 2006. "Genome-wide expression profile of the mnn2Δ mutant of Saccharomyces cerevisiae." Antonie van Leeuwenhoek 89, no. 3-4: 485-494.

Journal article
Published: 30 September 2005 in Fungal Genetics and Biology
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A collection of haploid Saccharomyces cerevisiae deletion strains—both MAT a and α—was screened for mutants that exhibit low dye binding (ldb) phenotype. This phenotype has previously been associated with reduced incorporation of mannosyl phosphate groups into the mannoprotein-linked oligosaccharides. We identified 199 nonessential genes whose deletion resulted in a detectable ldb phenotype. They fell into diverse functional categories, including those involved in protein glycosylation, vacuolar function, intracellular transport, cytoskeleton organization, transcription, signal transduction, among others. The study extends the number of known genes that affect mannosyl phosphorylation of mannoprotein-linked oligosaccharides, and establishes a link with other relevant pathways in the cell, especially vacuolar function. We have assigned an LDB name to four uncharacterized ORFs identified in this study: YCL005W, LDB16; YDL146W, LDB17; YLL049W, LDB18; and YOR322C, LDB19.

ACS Style

Isaac Corbacho; Isabel Olivero; Luis M. Hernández. A genome-wide screen for Saccharomyces cerevisiae nonessential genes involved in mannosyl phosphate transfer to mannoprotein-linked oligosaccharides. Fungal Genetics and Biology 2005, 42, 773 -790.

AMA Style

Isaac Corbacho, Isabel Olivero, Luis M. Hernández. A genome-wide screen for Saccharomyces cerevisiae nonessential genes involved in mannosyl phosphate transfer to mannoprotein-linked oligosaccharides. Fungal Genetics and Biology. 2005; 42 (9):773-790.

Chicago/Turabian Style

Isaac Corbacho; Isabel Olivero; Luis M. Hernández. 2005. "A genome-wide screen for Saccharomyces cerevisiae nonessential genes involved in mannosyl phosphate transfer to mannoprotein-linked oligosaccharides." Fungal Genetics and Biology 42, no. 9: 773-790.

Journal article
Published: 15 November 2004 in Applied Surface Science
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Contact and non-contact atomic force microscopy (AFM) has been used for analyzing the influence of the defects in N-glycosidic process in mnn9 mutants of S. cerevisiae in the cell wall physical properties. High-resolution non-contact AFM image have shown the mutant cell surface to present large highly rough areas (compared with wild type ones) and also some irregular but compact structures usually associated to the former areas. Since no crater-like rings (scars) were observed on the surface of mutant cells (unlike high-resolution imaging of these surface features in wild type cells), these structures are suggested to be deformed scars. These results would also confirm a critical influence of mannoproteins in the zone of the septum, which was already suggested in previous works. Force curves obtained on the irregular and rough areas have shown them to be physically softer than other parts of the cell surface and than wild type cells, and were easily deformed by the AFM tip while scanning in the contact mode. These results could be taken as a direct verification of the known highly osmotic fragility of these mutants. This is at our knowledge the first time defects on cell wall on mnn9 mutants have been directly probed and observed at nanometer scale.

ACS Style

A. Méndez-Vilas; I. Corbacho; M.L. González-Martı́n; M.J. Nuevo. Direct surface probing of cell wall-defective mutants of Saccharomyces cerevisiae by atomic force microscopy. Applied Surface Science 2004, 238, 51 -63.

AMA Style

A. Méndez-Vilas, I. Corbacho, M.L. González-Martı́n, M.J. Nuevo. Direct surface probing of cell wall-defective mutants of Saccharomyces cerevisiae by atomic force microscopy. Applied Surface Science. 2004; 238 (1-4):51-63.

Chicago/Turabian Style

A. Méndez-Vilas; I. Corbacho; M.L. González-Martı́n; M.J. Nuevo. 2004. "Direct surface probing of cell wall-defective mutants of Saccharomyces cerevisiae by atomic force microscopy." Applied Surface Science 238, no. 1-4: 51-63.

Journal article
Published: 31 January 2004 in FEMS Yeast Research
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We have completed the identification of Saccharomyces cerevisiae genes that are defective in previously isolated ldb (low-dye-binding) mutants. This was done by complementation of the mutant's phenotype with DNA fragments from a genomic library and by running standard tests of allelism with single-gene deletion mutants of similar phenotype. The results were as follows: LDB2 is allelic to ERD1; LDB4 to SPC72; LDB5 to RLR1; LDB6 to GON7/YJL184W; LDB7 to YBL006C; LDB9 to ELM1; LDB10 to CWH36; LDB11 to COG1; LDB12 to OCH1; LDB13 to VAN1; LDB14 to BUD32; and LDB15 to PHO85. Since the precise function of some of the genes is not known, these data may contribute to the functional characterization of the S. cerevisiae genome.

ACS Style

Isaac Corbacho; Isabel Olivero; Luis M Hernandez. Identification of low-dye-binding (ldb) mutants of Saccharomyces cerevisiae. FEMS Yeast Research 2004, 4, 437 -444.

AMA Style

Isaac Corbacho, Isabel Olivero, Luis M Hernandez. Identification of low-dye-binding (ldb) mutants of Saccharomyces cerevisiae. FEMS Yeast Research. 2004; 4 (4-5):437-444.

Chicago/Turabian Style

Isaac Corbacho; Isabel Olivero; Luis M Hernandez. 2004. "Identification of low-dye-binding (ldb) mutants of Saccharomyces cerevisiae." FEMS Yeast Research 4, no. 4-5: 437-444.

Journal article
Published: 01 February 2003 in FEMS Microbiology Letters
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The LDB1 gene of Saccharomyces cerevisiae was identified by complementation of the ldb1 mutant phenotype with a genomic library. We found that the ldb1 defect is complemented by PMR1 which codes for the yeast secretory pathway/Golgi Ca2+/Mn2+-ATPase. Besides that, the analysis of a null mutation of the PMR1 gene revealed a phenotype identical to that of ldb1 mutant. Thus, LDB1 must be considered a synonym of PMR1.

ACS Style

Isabel Olivero; Isaac Corbacho; Luis M Hernã¡ndez. Theldb1mutant ofSaccharomyces cerevisiaeis defective in Pmr1p, the yeast secretory pathway/Golgi Ca2+/Mn2+-ATPase. FEMS Microbiology Letters 2003, 219, 137 -142.

AMA Style

Isabel Olivero, Isaac Corbacho, Luis M Hernã¡ndez. Theldb1mutant ofSaccharomyces cerevisiaeis defective in Pmr1p, the yeast secretory pathway/Golgi Ca2+/Mn2+-ATPase. FEMS Microbiology Letters. 2003; 219 (1):137-142.

Chicago/Turabian Style

Isabel Olivero; Isaac Corbacho; Luis M Hernã¡ndez. 2003. "Theldb1mutant ofSaccharomyces cerevisiaeis defective in Pmr1p, the yeast secretory pathway/Golgi Ca2+/Mn2+-ATPase." FEMS Microbiology Letters 219, no. 1: 137-142.