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Institution

University of Seville

EducationSeville, Andalucía, Spain
About: University of Seville is a education organization based out in Seville, Andalucía, Spain. It is known for research contribution in the topics: Population & Context (language use). The organization has 20098 authors who have published 47317 publications receiving 947007 citations. The organization is also known as: Universidad de Sevilla.


Papers
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Journal ArticleDOI
TL;DR: It is shown that HPR1 is not required for transcription activation and that the previously reported effects of hpr1Delta on the activation of different promoters is a consequence of the incapacity of hPR1Delta cells to elongate transcription through lacZ, used as reporter.
Abstract: The yeast HPR1 gene plays an important role in genome stability, as indicated by the observation that hpr1 mutants have high frequencies of DNA repeat recombination and chromosome loss. Here we report that HPR1 is required for transcriptional elongation. Transcription driven from constitutive and regulated yeast promoters cannot elongate through the bacterial lacZ coding region in hpr1D cells, but progresses efficiently through other sequences such as yeast PHO5. We show that HPR1 is not required for transcription activation and that the previously reported effects of hpr1D on the activation of different promoters is a consequence of the incapacity of hpr1D cells to elongate transcription through lacZ, used as reporter. Transcriptional defects are also observed in yeast DNA sequences of hpr1D cells in the presence of the transcription elongation inhibitor 6-azauracil. In all cases, the blockage of transcription elongation in hpr1D is associated with both the high frequency of deletions and the increase in plasmid instability that we report here. Therefore, in addition to the identification of a new element involved in transcriptional elongation, our work provides evidence for a new source of genomic instability.

173 citations

Journal ArticleDOI
TL;DR: OmpK35 from Klebsiella pneumoniae is the homologue of Escherichia coli OmpF porin and decreased the MICs of imipenem, ciprofloxacin, and chloramphenicol ≥8-fold and was similar or 1 dilution lower for other evaluated agents.
Abstract: OmpK35 from Klebsiella pneumoniae is the homologue of Escherichia coli OmpF porin. Expression of OmpK35 in K. pneumoniae strain CSUB10R (lacking both OmpK35 and OmpK36) decreased the MICs of cephalosporins and meropenem > or = 128-fold and decreased the MICs of imipenem, ciprofloxacin, and chloramphenicol > or = 8-fold. MIC reductions by OmpK35 were 4 times (cefepime), 8 times (cefotetan, cefotaxime, and cefpirome), or 128 times (ceftazidime) higher than those caused by OmpK36, but the MICs were similar or 1 dilution lower for other evaluated agents.

172 citations

Journal ArticleDOI
TL;DR: This study showed that digitoxin (1) was the most active compound and revealed some structural features that may play a role in the growth inhibition activity of these drugs.
Abstract: The cardiac glycosides digitoxin (1) and digoxin (3) have been used in cardiac diseases for many years. During this time several reports have suggested the possible use of digitalis in medical oncology. Several analogues of digitoxin (1) were evaluated for growth inhibition activity in three human cancer cell lines; this study showed that digitoxin (1) was the most active compound and revealed some structural features that may play a role in the growth inhibition activity of these drugs. The IC50 values for 1 (3-33 nM) were within or below the concentration range seen in the plasma of patients with cardiac disease receiving this glycoside (20-33 nM). A renal adenocarcinoma cancer cell line (TK-10) was hypersensitive to this drug, and digitoxin toxicity on these cells was mediated by apoptosis. In vitro experiments showed that 1 at 30 nM induced levels of DNA-topoisomerase II cleavable complexes similar to etoposide, a topoisomerase II poison widely used in cancer chemotherapy. Using the individual cell assay TARDIS, cells exposed to 1 for 30 min showed low but statistically significant levels of DNA-topoisomerase II cleavable complexes; however these complexes disappeared after 24 h exposure.

172 citations

Journal ArticleDOI
TL;DR: Data support the view that GMAP-210 serves to link the cis-Golgi network to the minus ends of centrosome-nucleated microtubules, and appears essential for ensuring the proper morphology and size of the Golgi apparatus.
Abstract: We report that a peripheral Golgi protein with a molecular mass of 210 kD localized at the cis-Golgi network (Rios, R.M., A.M. Tassin, C. Celati, C. Antony, M.C. Boissier, J.C. Homberg, and M. Bornens. 1994. J. Cell Biol. 125:997-1013) is a microtubule-binding protein that associates in situ with a subpopulation of stable microtubules. Interaction of this protein, now called GMAP-210, for Golgi microtubule-associated protein 210, with microtubules in vitro is direct, tight and nucleotide-independent. Biochemical analysis further suggests that GMAP-210 specifically binds to microtubule ends. The full-length cDNA encoding GMAP-210 predicts a protein of 1, 979 amino acids with a very long central coiled-coil domain. Deletion analyses in vitro show that the COOH terminus of GMAP-210 binds to microtubules whereas the NH2 terminus binds to Golgi membranes. Overexpression of GMAP-210-encoding cDNA induced a dramatic enlargement of the Golgi apparatus and perturbations in the microtubule network. These effects did not occur when a mutant lacking the COOH-terminal domain was expressed. When transfected in fusion with the green fluorescent protein, the NH2-terminal domain associated with the cis-Golgi network whereas the COOH-terminal microtubule-binding domain localized at the centrosome. Altogether these data support the view that GMAP-210 serves to link the cis-Golgi network to the minus ends of centrosome-nucleated microtubules. In addition, this interaction appears essential for ensuring the proper morphology and size of the Golgi apparatus.

172 citations

Journal ArticleDOI
TL;DR: In this article, the authors make a profound revision of the basic underlying physics of generic cone jets from thousands of experimental measurements, most of them reported in the literature, and the boundaries of the stability region of steady jetting are calculated.
Abstract: Capillary cone jets are natural microfluidic structures arising in steady capillary tip streaming, whose paradigms are electrospray and flow focusing phenomena. In this work, we make a profound revision of the basic underlying physics of generic cone jets from thousands of experimental measurements, most of them reported in the literature. First, the boundaries of the stability region of steady jetting are calculated. We describe these limitations by instability mechanisms associated with the local flow structure in the tip and the issuing jet and with the global behavior of the meniscus. Second, to undertake a general physical treatment of cone jets in steady regime, we analyze the energy balance taking place in the tips of both flow focusing and electrospray. This analysis yields a fundamental result: if the electrospray data are expressed in terms of an effective pressure drop, both phenomena satisfy the same scaling law for the droplet size, which exhibits nearly complete similarity in the parameter window where quasimonodisperse sprays are produced. That effective pressure drop is a function of the liquid properties exclusively, i.e., it does not depend on the operational parameters (flow rate and applied voltage). Moreover, the stability limits of the operational regimes are analyzed in detail, finding fundamental coincidences between flow focusing and electrospray as well. These results provide most useful general description and predictive scaling laws for nearly monodisperse microspraying or nanospraying based on steady cone jets, of immediate applicability in analytical chemistry, chemical engineering, biochemistry, pharmaceutical and food technologies, painting, and many other technological fields.

172 citations


Authors

Showing all 20465 results

NameH-indexPapersCitations
Russel J. Reiter1691646121010
Aaron Dominguez1471968113224
Jose M. Ordovas123102470978
Detlef Lohse104107542787
Miroslav Krstic9595542886
María Vallet-Regí9571141641
John S. Sperry9316035602
Jose Rodriguez9380358176
Shun-ichi Amari9049540383
Michael Ortiz8746731582
Bruce J. Paster8426128661
Floyd E. Dewhirst8122942613
Joan Montaner8048922413
Francisco B. Ortega7950326069
Luis Paz-Ares7759231496
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Performance
Metrics
No. of papers from the Institution in previous years
YearPapers
2023143
2022568
20213,358
20203,480
20193,032
20182,766