Estimating Adaptacion of Dialogue Partners with Different Verbal Intelligence

This work investigates to what degree speakers with different verbal intelligence may adapt to each other. The work is based on a corpus consisting of 100 descriptions of a short film (monologues), 56 discussions about the same topic (dialogues), and verbal intelligence scores of the test participants. Adaptation between two dialogue partners was measured using cross-referencing, proportion of "I", "You" and "We" words, between-subject correlation and similarity of texts. It was shown that lower verbal intelligence speakers repeated more nouns and adjectives from the other and used the same linguistic categories more often than higher verbal intelligence speakers. In dialogues between strangers, participants with higher verbal intelligence showed a greater level of adaptation.

Med Capital Partners: plan de negocio de una EAFI

Med Capital Partners (MCP en adelante) es un empresa de asesoramiento financiero independiente (EAFI) que ofrecerá servicios de asesoramiento personalizado tanto a clientes particulares como a empresas, complementando su oferta con otros servicios auxiliares, que le permitan brindar a sus clientes una solución integral. MCP ha sido fundada por tres socios con formación y experiencia específica en el ámbito objeto del negocio, pero multidisciplinar para ofrecer un amplio espectro de servicios de calidad tanto en la Región de Murcia, donde va a establecer su sede, como en el resto de territorio nacional. MCP se crea con la firme misión de ofrecer servicios de asesoramiento y consulta financieros para la gestión y planificación patrimonial de calidad, de forma independiente y transparente y con la motivación de ser el médico de cabecera financiero de familias, particulares y empresas de todos los ámbitos, basándonos en arraigados valores entre los que predominan la transparencia, la independencia y la discreción. Una vez analizados los factores externos y haber realizado los planes de marketing, operaciones y financiero, nos encontramos en disposición de determinar que: 1.Existe un gran número de clientes potenciales. 2.Los factores político, social y legal favorecen la creación de este tipo de empresas. 3.Hay pocos competidores establecidos hasta la fecha. 4.No necesita complicadas infraestructuras ni requiere elevados gastos de aprovisionamiento. 5.Desde el año 2, se obtienen resultados positivos. La propuesta de valor de MCP está focalizada en ofrecer un servicio de calidad al menor precio posible, fijando una política de tarifas inferior a la media nacional y a la de nuestros competidores más cercanos, así como un esquema de precios descendentes para aquellos clientes que depositen su confianza en nosotros y renueven su contrato de asesoramiento continuado o contraten un combo de servicios. En términos operativos, el establecimiento de MCP requiere relativamente poco capital inicial, permitiendo ofrecer los primeros dividendos a los socios en un corto espacio temporal y teniendo desde el primer momento, un sueldo que les permita dedicarse plenamente al funcionamiento de MCP. En definitiva, creemos que MCP puede dar respuesta a una gran oportunidad de negocio existente en un sector en alza y en un mercado de arranque en el que hay una gran riqueza y poca cultura de inversión asesorada. ---ABSTRACT---Med Capital Partners (MCP) is an invest services company, which is established according to an EAFI structure. MCP will offer a custom-made service not only to individual clients but also to enterprises, with a wide range of supplementary services, including industrial strategy projects and all kind of financial processes demanded. MCP has been founded by three partners with proved training and specific experience based on the financial field but multitask and different between them, in order to offer various quality services in Región de Murcia, where it is going to be based, and also all around Spain. MCP is built with the firm mission of offering assessment and financial consulting quality services, helping with the patrimonial management and planning, doing it in an independent and transparent way, and always driving by the motivation of being the family doctor of individual and enterprise of sectors. To make it possible, MCP has deep values as excellence, wisdom and discretion. Once we have analyzed external factors and having made marketing, operations and financial plans, we are ready to determinate: 1.There is a big amount of potential customers. 2.Political, social and legal factors favor the formation of this type of business. 3.There are not many established competitors until now. 4.MCP does not need complex infrastructures either raised initial investment. 5.From year 2 and on, MCP is profitable. The value proposition of MCP is to focus on developing quality services with affordable fees, fixing a price policy under any other Spanish EAFI. MCP wants to build processes according to reality, working with reachable expectations and on real times. MCP is committed to the creation of stable, sustainable and consistent structures to adapt themselves to the individual risk profile of the customers, taking care of all of them. MCP wants to build a close relationship with clients and has developed a descending fee policy. MCP establishment does not require high initial resources and it is profitable in a short time, allowing investors to get their first dividends. Summarizing, we can say MCP is the answer of a big business opportunity within a rising and wealth market that only need a little help to emerge.

Large-scale identification of gibberellin-related transcription factor defines group VII ERFs as functional of DELLA partners

DELLA proteins are the master negative regulators in gibberellin (GA) signaling acting in the nucleus as transcriptional regulators. The current view of DELLA action indicates that their activity relies on the physical interaction with transcription factors (TFs). Therefore, the identification of TFs through which DELLAs regulate GA responses is key to understanding these responses from a mechanistic point of view. Here, we have determined the TF interactome of the Arabidopsis (Arabidopsis thaliana) DELLA protein GIBBERELLIN INSENSITIVE and screened a collection of conditional TF overexpressors in search of those that alter GA sensitivity. As a result, we have found RELATED TO APETALA2.3, an ethylene-induced TF belonging to the group VII ETHYLENE RESPONSE FACTOR of the APETALA2/ethylene responsive element binding protein superfamily, as a DELLA interactor with physiological relevance in the context of apical hook development. The combination of transactivation assays and chromatin immunoprecipitation indicates that the interaction with GIBBERELLIN INSENSITIVE impairs the activity of RELATED TO APETALA2.3 on the target promoters. This mechanism represents a unique node in the cross regulation between the GA and ethylene signaling pathways controlling differential growth during apical hook development.

Identification of the endophilins (SH3p4/p8/p13) as novel binding partners for the β1-adrenergic receptor

Several G-protein coupled receptors, such as the β1-adrenergic receptor (β1-AR), contain polyproline motifs within their intracellular domains. Such motifs in other proteins are known to mediate protein–protein interactions such as with Src homology (SH)3 domains. Accordingly, we used the proline-rich third intracellular loop of the β1-AR either as a glutathione S-transferase fusion protein in biochemical “pull-down” assays or as bait in the yeast two-hybrid system to search for interacting proteins. Both approaches identified SH3p4/p8/p13 (also referred to as endophilin 1/2/3), a SH3 domain-containing protein family, as binding partners for the β1-AR. In vitro and in human embryonic kidney (HEK) 293 cells, SH3p4 specifically binds to the third intracellular loop of the β1-AR but not to that of the β2-AR. Moreover, this interaction is mediated by the C-terminal SH3 domain of SH3p4. Functionally, overexpression of SH3p4 promotes agonist-induced internalization and modestly decreases the Gs coupling efficacy of β1-ARs in HEK293 cells while having no effect on β2-ARs. Thus, our studies demonstrate a role of the SH3p4/p8/p13 protein family in β1-AR signaling and suggest that interaction between proline-rich motifs and SH3-containing proteins may represent a previously underappreciated aspect of G-protein coupled receptor signaling.

The SH3p4/Sh3p8/SH3p13 protein family: Binding partners for synaptojanin and dynamin via a Grb2-like Src homology 3 domain

The GTPase dynamin I and the inositol 5-phosphatase synaptojanin are nerve terminal proteins implicated in synaptic vesicle recycling. Both proteins contain COOH-terminal proline-rich domains that can interact with a variety of Src homology 3 (SH3) domains. A major physiological binding partner for dynamin I and synaptojanin in the nervous system is amphiphysin I, an SH3 domain-containing protein also concentrated in nerve terminals. We have used the proline-rich tail of synaptojanin to screen a rat brain library by the two-hybrid method to identify additional interacting partners of synaptojanin. Three related proteins containing SH3 domains that are closely related to the SH3 domains of Grb2 were isolated: SH3p4, SH3p8, and SH3p13. Further biochemical studies demonstrated that the SH3p4/8/13 proteins bind to both synaptojanin and dynamin I. The SH3p4/8/13 transcripts are differentially expressed in tissues: SH3p4 mRNA was detected only in brain, SH3p13 mRNA was present in brain and testis, and the SH3p8 transcript was detected at similar levels in multiple tissues. Members of the SH3p4/8/13 protein family were found to be concentrated in nerve terminals, and pools of synaptojanin and dynamin I were coprecipitated from brain extracts with antibodies recognizing SH3p4/8/13. These findings underscore the important role of SH3-mediated interactions in synaptic vesicle recycling.

Copy Number Variations in DISC1 and DISC1-Interacting Partners in Major Mental Illness

Acknowledgements We would like to thank all of the patients, relatives and control individuals who participated in the study. We are indebted to the late Prof. Walter Muir, Chair of Developmental Psychiatry and Honorary Consultant in Learning Disability Psychiatry, University of Edinburgh, who initiated these studies and whose work was dedicated to the welfare of the patients who generously participated. We are also grateful to Mrs. Pat Malloy for her assistance with DNA collection and MAQ assays screening of the Scottish samples. The Scottish sample collection was supported by a grant from the Chief Scientist Office (CSO), part of the Scottish Government Health and Social Care Directorates. This research was funded by grants from the CSO to B.S.P. (grant CZB/4/610), The Academy of Medical Sciences/Wellcome Trust to M.J. (grant R41455) and The RS Macdonald Charitable Trust (grant D21419 together with J.H.), the Swedish Research Council (grants 2003-5158 and 2006-4472), the Medical Faculty, Umeå University, and the County Councils of Västerbotten and Norrbotten, Sweden, as well as by grants from the Fund for Scientific Research Flanders (FWO-F), the Industrial Research Fund (IWT) and the Special Research Fund of the University of Antwerp, Belgium. M.J. is funded by a Wellcome Trust Clinical Research Fellowship for MB PhD graduates (R42811). We acknowledge the contribution of the personnel of the VIB Genetic Service Facility (http://www.vibgeneticservicefacility.be/) for the genetic analysis of the Swedish samples. Research nurses Gunnel Johansson, Lotta Kronberg, Tage Johansson and Lisbeth Bertilsson are thankfully acknowledged for their help and expertise. The Betula Study was funded by the Swedish Research Council (grants 345-2003-3883 and 315-2004-6977). We also acknowledge the contribution by the staff in the Betula project

The α chain of laminin-1 is independently secreted and drives secretion of its β- and γ-chain partners

A mammalian recombinant strategy was established to dissect rules of basement membrane laminin assembly and secretion. The α-, β-, and γ-chain subunits of laminin-1 were expressed in all combinations, transiently and/or stably, in a near-null background. In the absence of its normal partners, the α chain was secreted as intact protein and protein that had been cleaved in the coiled-coil domain. In contrast, the β and γ chains, expressed separately or together, remained intracellular with formation of ββ or βγ, but not γγ, disulfide-linked dimers. Secretion of the β and γ chains required simultaneous expression of all three chains and their assembly into αβγ heterotrimers. Epitope-tagged recombinant α subunit and recombinant laminin were affinity-purified from the conditioned medium of αγ and αβγ clones. Rotary-shadow electron microscopy revealed that the free α subunit is a linear structure containing N-terminal and included globules with a foreshortened long arm, while the trimeric species has the typical four-arm morphology of native laminin. We conclude that the α chain can be delivered to the extracellular environment as a single subunit, whereas the β and γ chains cannot, and that the α chain drives the secretion of the trimeric molecule. Such an α-chain-dependent mechanism could allow for the regulation of laminin export into a nascent basement membrane, and might serve an important role in controlling basement membrane formation.

Leukemia-associated retinoic acid receptor α fusion partners, PML and PLZF, heterodimerize and colocalize to nuclear bodies

In acute promyelocytic leukemia (APL), the typical t(15;17) and the rare t(11;17) translocations express, respectively, the PML/RARα and PLZF/RARα fusion proteins (where RARα is retinoic acid receptor α). Herein, we demonstrate that the PLZF and PML proteins interact with each other and colocalize onto nuclear bodies (NBs). Furthermore, induction of PML expression by interferons leads to a recruitment of PLZF onto NBs without increase in the levels of the PLZF protein. PML/RARα and PLZF/RARα localize to the same microspeckled nuclear domains that appear to be common targets for the two fusion proteins in APL. Although PLZF/RARα does not affect the localization of PML, PML/RARα delocalizes the endogenous PLZF protein in t(15;17)-positive NB4 cells, pointing to a hierarchy in the nuclear targeting of these proteins. Thus, our results unify the molecular pathogenesis of APL with at least two different RARα gene translocations and stress the importance of alterations of PLZF and RARα nuclear localizations in this disease.

Erp1p and Erp2p, Partners for Emp24p and Erv25p in a Yeast p24 Complex

Six new members of the yeast p24 family have been identified and characterized. These six genes, named ERP1–ERP6 (for Emp24p- and Erv25p-related proteins) are not essential, but deletion of ERP1 or ERP2 causes defects in the transport of Gas1p, in the retention of BiP, and deletion of ERP1 results in the suppression of a temperature-sensitive mutation in SEC13 encoding a COPII vesicle coat protein. These phenotypes are similar to those caused by deletion of EMP24 or ERV25, two previously identified genes that encode related p24 proteins. Genetic and biochemical studies demonstrate that Erp1p and Erp2p function in a heteromeric complex with Emp24p and Erv25p.

Diminished degradation of yeast cytochrome c by interactions with its physiological partners.

The level and structure of yeast iso-1-cytochrome c and iso-2-cytochrome c, encoded by the nuclear genes CYC1 and CYC7, respectively, are normally not altered in rho- mutants, which completely lack the cytochromes a.a3 subunits and cytochrome b that are encoded by mitochondrial DNA. In contrast, iso-cytochromes c containing the amino acid change Thr-78-->Ile (T78I) were observed at the normal or near-normal wild-type level in rho+ strains but were completely absent in rho- mutants. We have demonstrated with the "global" suppressor mutation Asn-52-->Ile and by pulse-chase labeling that the T78I iso-1-cytochrome c undergoes rapid cellular degradation in rho- mutants. Furthermore, specific mutations revealed that the deficiency of T78I iso-1 cytochrome c can be caused by the lack of cytochrome a.a3 or cytochrome c1, but not by the lack of cytochrome b. Thus, this and certain other, but not all, labile forms of cytochrome c are protected from degradation by the interaction with its physiological partners.