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1

The influence of epoxomicin, inhibitor of proteasomal proteolytic activity, on spermiogenesis in Chara vulgaris

100%
Kwiatkowska M., Wojtczak A., Poplonska K., Teodorczyk M.
Folia Histochemica et Cytobiologica
|
2003
|
tom 41
|
nr 1
2

On the spatial organization of ubiquitin-dependent proteolysis in HeLa cells

88%
Wojcik C.
Folia Histochemica et Cytobiologica
|
1997
|
tom 35
|
nr 2
3

Evaluation of the effects of DNA and protesaomes from Ascaris suum in mice infected with A.suum and Toxocara canis

88%
Derda M., Hadas E., Stankiewicz M., Wandurska-Nowak E.
Medycyna Weterynaryjna
|
2004
|
tom 60
|
nr 04
4

Ribophagy - the novel degradation system of the ribosome

75%
Bakowska-Zywicka K., Tyczewska A.
Biotechnologia
|
2009
|
nr 1
99-103
5

Localization of a proteasomal antigen in human spermatozoa: immunohistochemical electron microscopic study

75%
Bialy L. P., Ziemba H. T., Marianowski P., Fracki S., Bury M., Wojcik C.
Folia Histochemica et Cytobiologica
|
2001
|
tom 39
|
nr 2
6

Occurrence of ubiquitin during spermiogenesis in Chara vulgaris

75%
Kwiatkowska M., Wojtczak A., Poplonska K., Gosek A.
Folia Histochemica et Cytobiologica
|
2001
|
tom 39
|
nr 2
7

Anti-tumor chemotherapy utilizing peptide-based approaches - apoptotic pathways, kinases, and proteasome as targets

75%
Mendoza F. J., Espino P. S., Cann K. L., Bristow N., McCrea K., Los M.
Archivum Immunologiae et Therapiae Experimentalis
|
2005
|
tom 53
|
nr 1
8

Cathepsin A and chymotrypsin-like activity of the proteasome in human blood platelet

75%
Ostrowska H., Wojcik C., Worowski K.
Folia Histochemica et Cytobiologica
|
1999
|
tom 37
|
nr 2
9

The role of the ubiquitin/ 26S proteasome pathway in plant morphogenesis and embryogenesis

63%
Brukhin V., Thomann A., Dieterle M., Gheyselinck J., Genschik P., Grossniklaus U.
Acta Biologica Cracoviensia. Series Botanica. Supplement
|
2005
|
tom 47
|
nr 1
10
Content available remote

Celastrol overcomes Hsp72 gene silencing-mediated muscle atrophy and induces myofiber preservation

63%
Gwag T., Park K., Park J., Lee J.-H., Nikawa T., Choi I.
Journal of Physiology and Pharmacology
|
2015
|
tom 66
|
nr 2
11

Temporal regulation of embryonic M-phases

63%
Kubiak J. Z., Bazile F., Pascal A., Richard-Parpaillon L., Polanski Z., Ciemerych M. A., Chesnel F.
Folia Histochemica et Cytobiologica
|
2008
|
tom 46
|
nr 1
5-9
12

An inhibitor of the chymotrypsin-like activity of the proteasome [PSI] induces similar morphological changes in various cell lines

63%
Wojcik C.
Folia Histochemica et Cytobiologica
|
1997
|
tom 35
|
nr 4
13

Proteasomes, ubiquitin and the effects of epoxomicin, an inhibitor of proteasomal proteolytic activity, on the spermiogenesis of Chara vulgaris

63%
Kwiatkowska M., Poplonska K., Wojtczak A., Gosek A., Stepinski D.
Cellular and Molecular Biology Letters
|
2002
|
tom 07
|
nr Suppl.
14

Pioglitazone, a PPAR-gamma ligand, exerts cytostatic-cytotoxic effects against cancer cells, that do not result from inhibition of proteasome

63%
Mrowka P., Glodkowska E., Mlynarczuk-Bialy I., Bialy L., Kuckelkorn U., Nowis D., Makowski M., Legat M., Golab J.
Acta Biochimica Polonica
|
2008
|
tom 55
|
nr 1
Thiazolidinediones are oral antidiabetic agents that activate peroxisome proliferator-activated receptor-gamma (PPAR-γ) and exert potent antioxidant and anti-inflammatory properties. It has also been shown that PPAR-γ agonists induce G0/G1 arrest and apoptosis of malignant cells. Some of these effects have been suggested to result from inhibition of proteasome activity in target cells. The aim of our studies was to critically evaluate the cytostatic/cytotoxic effects of one of thiazolidinediones (pioglitazone) and its influence on proteasome activity. Pioglitazone exerted dose-dependent cytostatic/cytotoxic effects in MIA PaCa-2 cells. Incubation of tumor cells with pioglitazone resulted in increased levels of p53 and p27 and decreased levels of cyclin D1. Accumulation of polyubiquitinated proteins within cells incubated with pioglitazone suggested dysfunction of proteasome activity. However, we did not observe any influence of pioglitazone on the activity of isolated proteasome and on the proteolytic activity in lysates of pioglitazone-treated MIA PaCa-2 cells. Further, treatment with pioglitazone did not cause an accumulation of fluorescent proteasome substrates in transfected HeLa cells expressing unstable GFP variants. Our results indicate that pioglitazone does not act as a direct or indirect proteasome inhibitor.
15

Degradation and beyond: control of androgen receptor activity by the proteasome system

63%
Jaworski T.
Cellular and Molecular Biology Letters
|
2006
|
tom 11
|
nr 1
The androgen receptor (AR) is a transcription factor belonging to the family of nuclear receptors which mediates the action of androgens in the development of urogenital structures. AR expression is regulated post-translationally by the ubiquitin/proteasome system. This regulation involves more complex mechanisms than typical degradation. The ubiquitin/proteasome system may regulate AR via mechanisms that do not engage in receptor turnover. Given the critical role of AR in sexual development, this complex regulation is especially important. Deregulation of AR signalling may be a causal factor in prostate cancer development. AR is the main target in prostate cancer therapies. Due to the critical role of the ubiquitin/proteasome system in AR regulation, current research suggests that targeting AR degradation is a promising approach.
16

Synaptic protein UNC-13 interacts with an F-box protein that may target it for degradation by proteasomes

63%
Polinsky C., Houston C., Vado J., Shaikh A., Kohn R. E.
Acta Biochimica Polonica
|
2006
|
tom 53
|
nr 1
UNC-13 protein participates in regulating neurotransmitter release. In Drosophila melanogaster, proteasomal degradation controls UNC-13 levels at synapses. Function of the amino-terminal region of a 207 kDa form of Caenorhabditis elegans UNC-13 is unknown. Yeast two-hybrid and secondary yeast assays identified an F-box protein that interacts with this amino-terminal region. As F-box proteins bind proteins targeted for proteasomal degradation, this protein may participate in degrading a subset of UNC-13 proteins, suggesting that different forms of UNC-13 are regulated differently. Yeast assays also identified an exonuclease, a predicted splicing factor, and a protein with coiled-coil domains, indicating that UNC-13 may affect RNA function.
17

Proteasome localization and ultrastructure of spermatozoa from patients with varicocele - immunoelectron microscopic study

63%
Ziemba B., Bialy L. P., Fracki S., Bablok L., Wojcik C.
Folia Histochemica et Cytobiologica
|
2002
|
tom 40
|
nr 2
18

Slowing down aging from within: mechanistic aspects of anti-aging hormetic effects of mild heat stress on human cells

63%
Rattan S. I. S., Gonzalez-Dosal R., Nielsen E. R., Kraft D. C., Weibel J., Kahns S.
Acta Biochimica Polonica
|
2004
|
tom 51
|
nr 2
Since aging is primarily the result of a failure of maintenance and repair mecha­nisms, various approaches are being developed in order to stimulate these pathways and modulate the process of aging. One such approach, termed hormesis, involves challenging cells and organisms by mild stress that often results in anti-aging and life prolonging effects. In a series of experimental studies, we have reported that re­peated mild heat stress (RMHS) has anti-aging hormetic effects on growth and vari­ous cellular and biochemical characteristics of human skin fibroblasts undergoing aging in vitro. These beneficial effects of repeated challenge include the mainte­nance of stress protein profile, reduction in the accumulation of oxidatively and glycoxidatively damaged proteins, stimulation of the proteasomal activities for the degradation of abnormal proteins, improved cellular resistance to other stresses, and enhanced levels of cellular antioxidant ability. In order to elucidate the molecular mechanisms of hormetic effects of RMHS, we are now undertaking studies on signal transduction pathways, energy production and utilisation kinetics, and the proteomic analysis of patterns of proteins synthesised and their posttranslational modifications in various types of human cells undergoing cellular aging in vitro. Human applications of hormesis include early intervention and modulation of the aging process to prevent or delay the onset of age-related conditions, such as sarcopenia, Alzheimer’s disease, Parkinson’s disease, cataracts and osteoporosis.
19

Thymoproteasome: role in thymic selection and clinical significance as a diagnostic marker for thymic epithelial tumors

51%
Tomaru U., Kasahara M.
Archivum Immunologiae et Therapiae Experimentalis
|
2013
|
tom 61
|
nr 5
20
Content available remote

Emerging roles of proteasomes in ischemia-reperfusion injury of organs

51%
Kukan M.
Journal of Physiology and Pharmacology
|
2004
|
tom 55
|
nr 1,1
Proteasomes are the main non-lysosomal, multicatalytic proteinase complexes involved in the degradation of most intracellular proteins and in numerous cell processes. Studies from isolated cell models indicate that agents that induce oxidative stress may also damage proteasomes. Similarly, continuous oxidative stress during cell aging may impair proteasome activity. In ischemia-reperfusion models of organ injury, proteasomes may be involved in several ways. First, proteasomes were found to be targets of ischemia-reperfusion injury of the brain and heart. Second, proteasome activity increased in liver models of ischemia-reperfusion. Third, proteasome inhibition prevented ischemia-reperfusion injury of the brain, heart and kidney. A major mechanism by which proteasome inhibititors may confer tissue protection is inactivation of transcription activator nuclear factor-B resulting in a block of expression of cytokines and cell adhesion molecules during the reperfusion phase. Thus, proteasome inhibition represents a novel strategy for the treatment of pathologies such as stroke, infarction, and kidney failure.
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