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1.
PLoS One ; 12(9): e0185023, 2017.
Artículo en Inglés | MEDLINE | ID: mdl-28931079

RESUMEN

PhD recipients acquire discipline-specific knowledge and a range of relevant skills during their training in the life sciences, physical sciences, computational sciences, social sciences, and engineering. Empirically testing the applicability of these skills to various careers held by graduates will help assess the value of current training models. This report details results of an Internet survey of science PhDs (n = 8099) who provided ratings for fifteen transferrable skills. Indeed, analyses indicated that doctoral training develops these transferrable skills, crucial to success in a wide range of careers including research-intensive (RI) and non-research-intensive (NRI) careers. Notably, the vast majority of skills were transferrable across both RI and NRI careers, with the exception of three skills that favored RI careers (creativity/innovative thinking, career planning and awareness skills, and ability to work with people outside the organization) and three skills that favored NRI careers (time management, ability to learn quickly, ability to manage a project). High overall rankings suggested that graduate training imparted transferrable skills broadly. Nonetheless, we identified gaps between career skills needed and skills developed in PhD training that suggest potential areas for improvement in graduate training. Therefore, we suggest that a two-pronged approach is crucial to maximizing existing career opportunities for PhDs and developing a career-conscious training model: 1) encouraging trainees to recognize their existing individual skill sets, and 2) increasing resources and programmatic interventions at the institutional level to address skill gaps. Lastly, comparison of job satisfaction ratings between PhD-trained employees in both career categories indicated that those in NRI career paths were just as satisfied in their work as their RI counterparts. We conclude that PhD training prepares graduates for a broad range of satisfying careers, potentially more than trainees and program leaders currently appreciate.


Asunto(s)
Investigación Biomédica , Selección de Profesión , Educación de Postgrado/estadística & datos numéricos , Satisfacción en el Trabajo , Ciencia , Humanos , Apoyo a la Formación Profesional , Recursos Humanos
2.
CBE Life Sci Educ ; 15(3)2016.
Artículo en Inglés | MEDLINE | ID: mdl-27587854

RESUMEN

A national sample of PhD-trained scientists completed training, accepted subsequent employment in academic and nonacademic positions, and were queried about their previous graduate training and current employment. Respondents indicated factors contributing to their employment decision (e.g., working conditions, salary, job security). The data indicate the relative importance of deciding factors influencing career choice, controlling for gender, initial interest in faculty careers, and number of postgraduate publications. Among both well-represented (WR; n = 3444) and underrepresented minority (URM; n = 225) respondents, faculty career choice was positively associated with desire for autonomy and partner opportunity and negatively associated with desire for leadership opportunity. Differences between groups in reasons endorsed included: variety, prestige, salary, family influence, and faculty advisor influence. Furthermore, endorsement of faculty advisor or other mentor influence and family or peer influence were surprisingly rare across groups, suggesting that formal and informal support networks could provide a missed opportunity to provide support for trainees who want to stay in faculty career paths. Reasons requiring alteration of misperceptions (e.g., limited leadership opportunity for faculty) must be distinguished from reasons requiring removal of actual barriers. Further investigation into factors that affect PhDs' career decisions can help elucidate why URM candidates are disproportionately exiting the academy.


Asunto(s)
Academias e Institutos , Selección de Profesión , Personal de Laboratorio , Grupos Minoritarios , Docentes , Femenino , Humanos , Modelos Logísticos , Masculino
3.
J Bacteriol ; 193(18): 4709-18, 2011 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-21764922

RESUMEN

Two-component regulatory systems, in which phosphorylation controls the activity of a response regulator protein, provide signal transduction in bacteria. For example, the phosphorylated CheY response regulator (CheYp) controls swimming behavior. In Escherichia coli, the chemotaxis phosphatase CheZ stimulates the dephosphorylation of CheYp. CheYp apparently binds first to the C terminus of CheZ and then binds to the active site where dephosphorylation occurs. The phosphatase activity of the CheZ(2) dimer exhibits a positively cooperative dependence on CheYp concentration, apparently because the binding of the first CheYp to CheZ(2) is inhibited compared to the binding of the second CheYp. Thus, CheZ phosphatase activity is reduced at low CheYp concentrations. The CheZ21IT gain-of-function substitution, located far from either the CheZ active site or C-terminal CheY binding site, enhances CheYp binding and abolishes cooperativity. To further explore mechanisms regulating CheZ activity, we isolated 10 intragenic suppressor mutations of cheZ21IT that restored chemotaxis. The suppressor substitutions were located along the central portion of CheZ and were not allele specific. Five suppressor mutants tested biochemically diminished the binding of CheYp and/or the catalysis of dephosphorylation, even when the suppressor substitutions were distant from the active site. One suppressor mutant also restored cooperativity to CheZ21IT. Consideration of results from this and previous studies suggests that the binding of CheYp to the CheZ active site (not to the C terminus) is rate limiting and leads to cooperative phosphatase activity. Furthermore, amino acid substitutions distant from the active site can affect CheZ catalytic activity and CheYp binding, perhaps via the propagation of structural or dynamic perturbations through a helical bundle.


Asunto(s)
Sustitución de Aminoácidos/genética , Proteínas Bacterianas/genética , Proteínas Bacterianas/metabolismo , Escherichia coli/enzimología , Escherichia coli/fisiología , Locomoción , Proteínas de la Membrana/genética , Proteínas de la Membrana/metabolismo , Sitios de Unión , Dominio Catalítico , Proteínas de Escherichia coli , Proteínas Quimiotácticas Aceptoras de Metilo , Modelos Moleculares , Fosfatos/metabolismo , Monoéster Fosfórico Hidrolasas/genética , Monoéster Fosfórico Hidrolasas/metabolismo , Unión Proteica , Estructura Cuaternaria de Proteína , Supresión Genética
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