830 resultados para Employee turnover
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"11.4.1889 Franz Trolldenier geb. 5.12.1866"
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"15.4.1889 Georg Heinrich geb. 12.5.1863. pens. 31.12.1927"
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"25.7.1891 Friedrich Brandes geb. 11.4.1867 pens. 31.12.1927"
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"1.10.1891 Moritz Romberg geb. 4.6.1870"
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"1.10.1891 August Rothschild geb. 14.11.1870"
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"1.10.1893 Otto Pieper geb. 11.2.1868"
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"15.11.1893 Heinrich Ruhrmann geb. 1.1.1863 pens. 31.12.1927"
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"2.12.1895 Richard Mueller geb. 1.3.1853 pens. 31.12.1927"
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"15.8.1896 Franz Koch geb. 14.9.1860 gest. 21.10.1927"
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"1.6.1897 Max Fonrobert geb. 5.12.1866"
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"1.12.1897 Otto Pfeiffer geb. 23.10.1873"
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We propose a conceptual model based on person–environment interaction, job performance, and motivational theories to structure a multilevel review of the employee green behavior (EGB) literature and agenda for future research. We differentiate between required EGB prescribed by the organization and voluntary EGB performed at the employees’ discretion. The review investigates institutional-, organizational-, leader-, team-, and employee-level antecedents and outcomes of EGB and factors that mediate and moderate these relationships. We offer suggestions to facilitate the development of the field, and call for future research to adopt a multilevel perspective and to investigate the outcomes of EGB.
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Ambidextrous leadership involves a combination of behaviours that stimulate employee exploration (‘opening behaviour’) and behaviours that facilitate exploitation of ideas (‘closing behaviour’). We hypothesized that the interaction between leaders’ daily opening and closing behaviours (i.e., ambidextrous leadership) predicts employees’ daily self-reported innovative performance. Results based on diary data provided by 113 employees across five work days supported this hypothesis: daily self-reported innovative performance was highest when both daily opening and closing behaviours were high.
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The striated muscle sarcomere is a force generating and transducing unit as well as an important sensor of extracellular cues and a coordinator of cellular signals. The borders of individual sarcomeres are formed by the Z-disks. The Z-disk component myotilin interacts with Z-disk core structural proteins and with regulators of signaling cascades. Missense mutations in the gene encoding myotilin cause dominantly inherited muscle disorders, myotilinopathies, by an unknown mechanism. In this thesis the functions of myotilin were further characterized to clarify the molecular biological basis and the pathogenetic mechanisms of inherited muscle disorders, mainly caused by mutated myotilin. Myotilin has an important function in the assembly and maintenance of the Z-disks probably through its actin-organizing properties. Our results show that the Ig-domains of myotilin are needed for both binding and bundling actin and define the Ig domains as actin-binding modules. The disease-causing mutations appear not to change the interplay between actin and myotilin. Interactions between Z-disk proteins regulate muscle functions and disruption of these interactions results in muscle disorders. Mutations in Z-disk components myotilin, ZASP/Cypher and FATZ-2 (calsarcin-1/myozenin-2) are associated with myopathies. We showed that proteins from the myotilin and FATZ families interact via a novel and unique type of class III PDZ binding motif with the PDZ domains of ZASP and other Enigma family members and that the interactions can be modulated by phosphorylation. The morphological findings typical of myotilinopathies include Z-disk alterations and aggregation of dense filamentous material. The causes and mechanisms of protein aggregation in myotilinopathy patients are unknown, but impaired degradation might explain in part the abnormal protein accumulation. We showed that myotilin is degraded by the calcium-dependent, non-lysosomal cysteine protease calpain and by the proteasome pathway, and that wild type and mutant myotilin differ in their sensitivity to degradation. These studies identify the first functional difference between mutated and wild type myotilin. Furthermore, if degradation of myotilin is disturbed, it accumulates in cells in a manner resembling that seen in myotilinopathy patients. Based on the results, we propose a model where mutant myotilin escapes proteolytic breakdown and forms protein aggregates, leading to disruption of myofibrils and muscular dystrophy. In conclusion, the main results of this study demonstrate that myotilin is a Z-disk structural protein interacting with several Z-disk components. The turnover of myotilin is regulated by calpain and the ubiquitin proteasome system and mutations in myotilin seem to affect the degradation of myotilin, leading to protein accumulations in cells. These findings are important for understanding myotilin-linked muscle diseases and designing treatments for these disorders.