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  1. Article ; Online: Occupational Safety of Municipal Police Officers: Assessing the Vulnerability and Riskiness of Police Officers' Work.

    Soltes, Viktor / Kubas, Jozef / Velas, Andrej / Michalík, David

    International journal of environmental research and public health

    2021  Volume 18, Issue 11

    Abstract: The municipal police agencies increase the safety of a municipality's citizens and thus increase their quality of life. When performing interventions, municipal police officers may endanger their safety and health. This paper deals with the analysis of ... ...

    Abstract The municipal police agencies increase the safety of a municipality's citizens and thus increase their quality of life. When performing interventions, municipal police officers may endanger their safety and health. This paper deals with the analysis of the riskiness of municipal police officers working in the Slovak Republic and the Czech Republic from 2004 to 2019 and the assessment of their occupational safety. The risk analysis was carried out on the basis of a risk matrix and calculations of the probability of attack and injury to municipal police officers. Using the Pearson correlation coefficient, the dependence between the selected variables was investigated. The reliability of this dependence was examined by the determination coefficient. The main result of the paper is the determination of the riskiness category of municipal police officer work based on the assessment of the occupational health protection of officers through statistical indicators of their activities and risk matrix. The results will serve as part of the explanatory memorandum for the proposal of legislative changes in order to increase the occupational health protection of municipal police officers.
    MeSH term(s) Czech Republic ; Humans ; Occupational Health ; Police ; Quality of Life ; Reproducibility of Results ; Slovakia
    Language English
    Publishing date 2021-05-24
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1660-4601
    ISSN (online) 1660-4601
    DOI 10.3390/ijerph18115605
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  2. Article ; Online: Occupational Safety of Municipal Police Officers

    Viktor Soltes / Jozef Kubas / Andrej Velas / David Michalík

    International Journal of Environmental Research and Public Health, Vol 18, Iss 5605, p

    Assessing the Vulnerability and Riskiness of Police Officers’ Work

    2021  Volume 5605

    Abstract: The municipal police agencies increase the safety of a municipality’s citizens and thus increase their quality of life. When performing interventions, municipal police officers may endanger their safety and health. This paper deals with the analysis of ... ...

    Abstract The municipal police agencies increase the safety of a municipality’s citizens and thus increase their quality of life. When performing interventions, municipal police officers may endanger their safety and health. This paper deals with the analysis of the riskiness of municipal police officers working in the Slovak Republic and the Czech Republic from 2004 to 2019 and the assessment of their occupational safety. The risk analysis was carried out on the basis of a risk matrix and calculations of the probability of attack and injury to municipal police officers. Using the Pearson correlation coefficient, the dependence between the selected variables was investigated. The reliability of this dependence was examined by the determination coefficient. The main result of the paper is the determination of the riskiness category of municipal police officer work based on the assessment of the occupational health protection of officers through statistical indicators of their activities and risk matrix. The results will serve as part of the explanatory memorandum for the proposal of legislative changes in order to increase the occupational health protection of municipal police officers.
    Keywords occupational health ; municipal police ; police ; risk assessment ; vulnerability ; Medicine ; R
    Language English
    Publishing date 2021-05-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  3. Article: Proteasome degrades soluble expanded polyglutamine completely and efficiently.

    Michalik, Andrej / Van Broeckhoven, Christine

    Neurobiology of disease

    2004  Volume 16, Issue 1, Page(s) 202–211

    Abstract: To date, nine progressive neurodegenerative diseases are caused by expansion of the CAG repeat coding for polyglutamine, including Huntington's disease and several forms of spinocerebellar ataxia. Expanded polyglutamine causes dominant toxic gain-of- ... ...

    Abstract To date, nine progressive neurodegenerative diseases are caused by expansion of the CAG repeat coding for polyglutamine, including Huntington's disease and several forms of spinocerebellar ataxia. Expanded polyglutamine causes dominant toxic gain-of-function related to its ability to aggregate. Polyglutamine aggregates inhibit the proteasome, suggesting that reduced degradation of misfolded proteins might contribute to polyglutamine toxicity. Moreover, several observations indicate that soluble proteins harboring expanded polyglutamine display altered turnover. To examine whether soluble polyglutamine interfered with proteasome-mediated degradation, we analyzed degradation of model proteasome substrates carrying either 103 or 25 glutamines in transfected cells. Expanded and normal size polyglutamine were degraded to completion and with similar efficiency. Moreover, targeting of expanded polyglutamine for proteasome-mediated degradation did not compromise proteasome activity. Thus, we propose that polyglutamine-containing disease proteins can be readily digested by the proteasome if they carried a degradation signal.
    MeSH term(s) Amino Acid Sequence ; Animals ; COS Cells ; Cercopithecus aethiops ; Cysteine Endopeptidases/genetics ; Cysteine Endopeptidases/metabolism ; Hydrolysis ; Multienzyme Complexes/genetics ; Multienzyme Complexes/metabolism ; Peptides/genetics ; Peptides/metabolism ; Proteasome Endopeptidase Complex ; Recombinant Fusion Proteins/metabolism ; Repetitive Sequences, Amino Acid ; Solubility ; Trinucleotide Repeat Expansion/genetics ; Trinucleotide Repeat Expansion/physiology
    Chemical Substances Multienzyme Complexes ; Peptides ; Recombinant Fusion Proteins ; polyglutamine (26700-71-0) ; Cysteine Endopeptidases (EC 3.4.22.-) ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
    Language English
    Publishing date 2004-06
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1211786-9
    ISSN 1095-953X ; 0969-9961
    ISSN (online) 1095-953X
    ISSN 0969-9961
    DOI 10.1016/j.nbd.2003.12.020
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  4. Article: Pathogenesis of polyglutamine disorders: aggregation revisited.

    Michalik, Andrej / Van Broeckhoven, Christine

    Human molecular genetics

    2003  Volume 12 Spec No 2, Page(s) R173–86

    Abstract: Expansion of CAG trinucleotide repeats coding for polyglutamine in unrelated proteins causes at least nine late-onset progressive neurodegenerative disorders, including Huntington's disease and a number of spinocerebellar ataxias. Expanded polyglutamine ... ...

    Abstract Expansion of CAG trinucleotide repeats coding for polyglutamine in unrelated proteins causes at least nine late-onset progressive neurodegenerative disorders, including Huntington's disease and a number of spinocerebellar ataxias. Expanded polyglutamine provokes a dominant gain-of-function neurotoxicity, regardless of the specific protein context within which it resides. Nevertheless, the protein context does modulate polyglutamine toxicity, as evidenced by the distinct clinical and pathological features of the various disorders. Importantly, polyglutamine toxicity might derive from its ability to aggregate. Indeed, aggregation probably underlies some defining attributes of the polyglutamine disorders, such as their late onset, progressive nature, and the dependence of onset age on polyglutamine length. However, the central role of aggregation in polyglutamine pathogenesis has been challenged by several studies, which instead argued that the soluble form of the disease proteins is responsible for neuronal damage. Thus, the question whether polyglutamine aggregates are deleterious, harmless or protective remains the most passionately disputed issue in the study of these diseases. In this review, we attempt to reconcile some of these controversies.
    MeSH term(s) Animals ; Humans ; Huntington Disease/genetics ; Peptides/physiology ; Spinocerebellar Ataxias/genetics
    Chemical Substances Peptides ; polyglutamine (26700-71-0)
    Language English
    Publishing date 2003-10-15
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1108742-0
    ISSN 1460-2083 ; 0964-6906
    ISSN (online) 1460-2083
    ISSN 0964-6906
    DOI 10.1093/hmg/ddg295
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  5. Article ; Online: Method to Introduce Stable, Expanded, Polyglutamine-Encoding CAG/CAA Trinucleotide Repeats into CAG Repeat-Containing Genes

    Andrej Michalik / Aleksey Kazantsev / Christine Van Broeckhoven

    BioTechniques, Vol 31, Iss 2, Pp 250-

    2001  Volume 254

    Keywords Biology (General) ; QH301-705.5
    Language English
    Publishing date 2001-08-01T00:00:00Z
    Publisher Future Science Ltd
    Document type Article ; Online
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  6. Article: Ataxin-7 aggregation and ubiquitination in infantile SCA7 with 180 CAG repeats.

    Ansorge, Olaf / Giunti, Paola / Michalik, Andrej / Van Broeckhoven, Christine / Harding, Brian / Wood, Nicholas / Scaravilli, Francesco

    Annals of neurology

    2004  Volume 56, Issue 3, Page(s) 448–452

    Abstract: Extremely long (>150) CAG repeats are often used to create models of polyglutamine diseases yet are very rare in humans where they manifest as pediatric multisystem syndromes of little specificity. Here, we describe an infant with 180 CAG repeats in the ... ...

    Abstract Extremely long (>150) CAG repeats are often used to create models of polyglutamine diseases yet are very rare in humans where they manifest as pediatric multisystem syndromes of little specificity. Here, we describe an infant with 180 CAG repeats in the spinocerebellar ataxia type 7 gene and focus on systemic ataxin-7 aggregation. This was found in many organs, including the cardiovascular system. In the brain, the hippocampus emerged as a principal site of ataxin-7 aggregation without cell loss. We note differential ubiquitination of aggregates and discuss how this may relate to selective vulnerability.
    MeSH term(s) Ataxin-7 ; Child, Preschool ; Female ; Humans ; Male ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/metabolism ; Neurons/metabolism ; Neurons/pathology ; Pedigree ; Spinocerebellar Ataxias/genetics ; Spinocerebellar Ataxias/metabolism ; Spinocerebellar Ataxias/pathology ; Trinucleotide Repeats/genetics ; Ubiquitin/genetics ; Ubiquitin/metabolism
    Chemical Substances ATXN7 protein, human ; Ataxin-7 ; Nerve Tissue Proteins ; Ubiquitin
    Language English
    Publishing date 2004-09
    Publishing country United States
    Document type Case Reports ; Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 80362-5
    ISSN 1531-8249 ; 0364-5134
    ISSN (online) 1531-8249
    ISSN 0364-5134
    DOI 10.1002/ana.20230
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  7. Article ; Online: Intraneuronal amyloid beta and reduced brain volume in a novel APP T714I mouse model for Alzheimer's disease.

    Van Broeck, Bianca / Vanhoutte, Greet / Pirici, Daniel / Van Dam, Debby / Wils, Hans / Cuijt, Ivy / Vennekens, Krist'l / Zabielski, Monika / Michalik, Andrej / Theuns, Jessie / De Deyn, Peter Paul / Van der Linden, Annemie / Van Broeckhoven, Christine / Kumar-Singh, Samir

    Neurobiology of aging

    2008  Volume 29, Issue 2, Page(s) 241–252

    Abstract: Transgenic mouse models of Alzheimer's disease (AD) expressing high levels of amyloid precursor protein (APP) with familial AD (FAD) mutations have proven to be extremely useful in understanding pathogenic processes of AD especially those that involve ... ...

    Abstract Transgenic mouse models of Alzheimer's disease (AD) expressing high levels of amyloid precursor protein (APP) with familial AD (FAD) mutations have proven to be extremely useful in understanding pathogenic processes of AD especially those that involve amyloidogenesis. We earlier described Austrian APP T714I pathology that leads to one of the earliest AD age-at-onsets with abundant intracellular and extracellular amyloid deposits in brain. The latter strikingly was non-fibrillar diffuse amyloid, composed of N-truncated A beta 42 in absence of A beta 40. In vitro, this mutation leads to one of the highest A beta 42/A beta 40 ratios among all FAD mutations. We generated an APP T714I transgenic mouse model that despite having 10 times lower transgene than endogenous murine APP deposited intraneuronal A beta in brain by 6 months of age. Accumulations increased with age, and this was paralleled by decreased brain sizes on volumetric MRI, compared to age-matched and similar transgene-expressing APP wild-type mice, although, with these levels of transgenic expression we did not detect neuronal loss or significant memory impairment. Immunohistochemical studies revealed that the majority of the intraneuronal A beta deposits colocalized with late endosomal markers, although some A beta inclusions were also positive for lysosomal and Golgi markers. These data support earlier observations of A beta accumulation in the endosomal-lysosomal pathway and the hypothesis that intraneuronal accumulation of A beta could be an important factor in the AD pathogenesis.
    MeSH term(s) Alzheimer Disease/genetics ; Alzheimer Disease/pathology ; Alzheimer Disease/physiopathology ; Amyloid beta-Peptides/metabolism ; Amyloid beta-Protein Precursor/genetics ; Analysis of Variance ; Animals ; Behavior, Animal/physiology ; Brain/pathology ; Disease Models, Animal ; Enzyme-Linked Immunosorbent Assay ; Humans ; Isoleucine/genetics ; Magnetic Resonance Imaging ; Maze Learning/physiology ; Mice ; Mice, Transgenic ; Neurons/cytology ; Peptide Fragments/metabolism ; Psychomotor Performance/physiology ; Tyrosine/genetics
    Chemical Substances Amyloid beta-Peptides ; Amyloid beta-Protein Precursor ; Peptide Fragments ; amyloid beta-protein (1-40) ; amyloid beta-protein (1-42) ; Isoleucine (04Y7590D77) ; Tyrosine (42HK56048U)
    Language English
    Publishing date 2008-02
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 604505-4
    ISSN 1558-1497 ; 0197-4580
    ISSN (online) 1558-1497
    ISSN 0197-4580
    DOI 10.1016/j.neurobiolaging.2006.10.016
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  8. Article: Hot-spot residue in small heat-shock protein 22 causes distal motor neuropathy.

    Irobi, Joy / Van Impe, Katrien / Seeman, Pavel / Jordanova, Albena / Dierick, Ines / Verpoorten, Nathalie / Michalik, Andrej / De Vriendt, Els / Jacobs, An / Van Gerwen, Veerle / Vennekens, Krist'l / Mazanec, Radim / Tournev, Ivailo / Hilton-Jones, David / Talbot, Kevin / Kremensky, Ivo / Van Den Bosch, Ludo / Robberecht, Wim / Van Vandekerckhove, Joël /
    Van Broeckhoven, Christine / Gettemans, Jan / De Jonghe, Peter / Timmerman, Vincent

    Nature genetics

    2004  Volume 36, Issue 6, Page(s) 597–601

    Abstract: Distal hereditary motor neuropathies are pure motor disorders of the peripheral nervous system resulting in severe atrophy and wasting of distal limb muscles. In two pedigrees with distal hereditary motor neuropathy type II linked to chromosome 12q24.3, ... ...

    Abstract Distal hereditary motor neuropathies are pure motor disorders of the peripheral nervous system resulting in severe atrophy and wasting of distal limb muscles. In two pedigrees with distal hereditary motor neuropathy type II linked to chromosome 12q24.3, we identified the same mutation (K141N) in small heat-shock 22-kDa protein 8 (encoded by HSPB8; also called HSP22). We found a second mutation (K141E) in two smaller families. Both mutations target the same amino acid, which is essential to the structural and functional integrity of the small heat-shock protein alphaA-crystallin. This positively charged residue, when mutated in other small heat-shock proteins, results in various human disorders. Coimmunoprecipitation experiments showed greater binding of both HSPB8 mutants to the interacting partner HSPB1. Expression of mutant HSPB8 in cultured cells promoted formation of intracellular aggregates. Our findings provide further evidence that mutations in heat-shock proteins have an important role in neurodegenerative disorders.
    MeSH term(s) Amino Acid Sequence ; Animals ; COS Cells ; Cell Line ; Charcot-Marie-Tooth Disease/genetics ; Charcot-Marie-Tooth Disease/metabolism ; Female ; Heat-Shock Proteins/chemistry ; Heat-Shock Proteins/genetics ; Heat-Shock Proteins/metabolism ; Humans ; Male ; Molecular Sequence Data ; Pedigree ; Point Mutation ; Protein-Serine-Threonine Kinases ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Sequence Homology, Amino Acid ; Transfection
    Chemical Substances HSPB8 protein, human ; Heat-Shock Proteins ; Recombinant Proteins ; Protein-Serine-Threonine Kinases (EC 2.7.11.1)
    Language English
    Publishing date 2004-05-02
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1108734-1
    ISSN 1546-1718 ; 1061-4036
    ISSN (online) 1546-1718
    ISSN 1061-4036
    DOI 10.1038/ng1328
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