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1

Alpinarium. Cz.2. - Elementy ogrodów skalnych

100%
Pudelska K., Rojek K.
Teka Komisji Architektury, Urbanistyki i Studiów Krajobrazowych
|
2011
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tom 07
2

Kwiatowe elementy roślinne w XIX-wiecznych polskich ogrodach krajobrazowych w świetle literatury ogrodowej

100%
Pudelska K., Rojek K.
Teka Komisji Architektury, Urbanistyki i Studiów Krajobrazowych
|
2011
|
tom 07
3

Alpinarium. Cz.1. - Istota ogrodu skalnego

100%
Pudelska K., Rojek K.
Teka Komisji Architektury, Urbanistyki i Studiów Krajobrazowych
|
2010
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tom 06
4

Zmiany w strukturze drzewostanu w XIX-wiecznym parku w Czesławicach

100%
Pudelska K., Rojek K.
Teka Komisji Architektury, Urbanistyki i Studiów Krajobrazowych
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2013
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tom 9
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nr 3
5

Ogrody krajobrazowe, naturalistyczne czy ekologiczne

81%
Pudelska K., Rojek K., Chylewska R.
Teka Komisji Architektury, Urbanistyki i Studiów Krajobrazowych
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2013
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tom 9
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nr 4
6

Wpływ dogrzewania bezświetlnym grzejnikiem ceramicznym na odchów i zachowanie się prosiąt ssących

81%
Pilarczyk A., Jenike R., Rojek K.
Roczniki Naukowe Zootechniki
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1982
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tom 09
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nr 1
7

Drzewa pomnikowe w przestrzeni miejskiej na przykładzie Lublina

81%
Pudelska K., Rojek K., Chyzewska R.
Nauka Przyroda Technologie. Uniwersytet Przyrodniczy w Poznaniu
|
2017
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tom 11
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nr 1
8
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The influence of Bio-algeen S90 on the growth of multiflora rose seedlings (Rosa multiflora Thunb.)

71%
Szmagara M., Pudelska K., Durlak W., Marcinek B., Rojek K.
Acta Scientiarum Polonorum. Hortorum Cultus
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2019
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tom 18
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nr 3
Striving to intensify horticultural production, new and more effective bio-preparations are being sought to stimulate plant growth and development. Bio-algeen S90 is a natural agent based on sea algae, the high biological activity of which results from the high content of natural growth regulators. The aim of the study was to verify the influence of Bio-algeen S90 on the growth, morphological characteristics and chlorophyll fluorescence of Rosa multiflora seedlings. The bio-preparation was applied one, two and three times at concentrations: 0.1, 0.2, 0.4 and 0.6 mg.dm−3. Following parameters were measured to evaluate the response of plants to the bio-preparation: F0 – initial fluorescence, Fm – maximal fluorescence in the dark-adapted state, Fv/Fm – maximum photochemical efficiency of PSII. All concentrations of the bio-preparation and frequency of its application stimulated the number of shoots in a bush, the length of shoots and the diameter of the root crown of plants intended for budding. The most beneficial was the two-fold bio-preparation application at a concentration of 0.4 mg.dm–3. Bio-algeen also positively influenced the chlorophyll fluorescence parameters. The highest mean F0 and Fm values were recorded with the two-fold preparation treatment. There was no significant effect of the bio-preparation on the Fv/Fm index, which was within the range of 0.75–0.66.
9

Amotl1: a novel synaptic protein important for mice social behavior and brain organization

61%
Krzemien J., Rojek K., Winiarski M., Boguszewski P. M., Knapska E., Proszynski T. J.
Acta Neurobiologiae Experimentalis
|
2019
|
tom 79
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nr Suppl.1
INTRODUCTION: The angiomotin family comprises of three scaffold proteins – Amot, Amotl1, and Amotl2 – that have been implicated in the regulation of cell polarity, migration, and proliferation. Recent in vitro studies have reported that Amot localizes to the synapses in mature neurons and regulates dendritic spine maturation. AIM(S): We have found that Amot, together with Yap1, the Hippo pathway transcription co‑activator, are critical for proper dendritic arborization and mice locomotor coordination. However, to date the function of the two other Angiomotins, Amotl1 and Amotl2, in neurons has not been investigated. METHOD(S): To study Amotl1 function in the mouse brain, we generated systemic and neuron-specific knock‑out (KO) mice. To assess general locomotion, we performed an open field test. Amotl1 KO mice sociability was evaluated with the three-chamber task, automatic Eco‑Hab approach, and nesting test. To record the animal’s anxiety response, we used the marble burying test. RESULTS: In the present study, we show that Amotl1 localizes to the synaptic compartments in neurons. Deletion of Amotl1 leads to hyperlocomotion, decreased anxiety-like behavior, and alteration in mice sociability. Amotl1 ablation causes an increase in volume of lateral ventricles in the mouse brain by 50%. These features have been previously observed in animal models of various psychiatric disorders, such as schizophrenia or autism. Interestingly, mass spectrometry analysis of neuron‑specific interactors demonstrated that Amotl1 binds to FMR1 and FXR1, mutations of which cause Fragile X syndrome. CONCLUSIONS: We identified a novel synaptic protein, Amotl1, the deletion of which causes behavioral deficits and that it could be a potential molecular target for the development of new therapeutics for neurological disorders. FINANCIAL SUPPORT: This research was supported by National Science Center (NCN) grants: UMO- ‑2018/29/B/NZ3/02675, UMO-2018/29/N/NZ3/02682.
10

Role of Amot12, Rast8 and Homer1 in the organization of postsynaptic machinery

61%
Gawor M., Niewiadomski P., Bernadzki K., Jozwiak J., Rojek K., Redowicz M. J., Proswzynski T. J.
Acta Neurobiologiae Experimentalis
|
2015
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tom 75
|
nr Supl.
BACKGROUND AND AIMS: Vertebrate neuromuscular junction (NMJ) undergoes a series of topological rearrangements in order to achieve its mature complex shape resembling pretzels. We have previously reported that podosomes, actin-rich dynamic adhesive organelles are implicated in the NMJ developmental remodeling. The main aim of this study was to understand molecular mechanisms regulating formation of podosomes and/or remodeling of the postsynaptic machinery with a special focus on the role of Amotl2 scaffold protein in these processes. METHODS: To identify Amotl2-binding proteins we used TAP-tag affinity purification and mass spectrometry. Localization of proteins to NMJ subsynaptic compartments was performed using standard cytochemical procedures and confocal microscopy. We performed RNAi-based knockdown experiments on cultured C21C12 myotubes to assess the importance of proteins in the organization of postsynaptic AChR clusters. RESULTS: We identified several novel Amotl2-binding proteins and subsequently focused our experiments on two of them, Rassf8 and Homer1, that remain uncharacterized at the NMJ. Amotl2, Rassf8 and Homer1 are concentrated at postsynaptic areas of NMJs in the indentations between the AChR-rich branches. Our results suggest that Rassf8 and Homer1 may be involved in AChR organization and development of the neuromuscular synapses. CONCLUSIONS: We identified novel components of the muscle postsynaptic machinery that specifically localize to the sites of NMJ remodeling. Our results suggest that Amotl2 may be involved in the developmental remodeling of the postsynaptic machinery through the interactions with Rassf8 and Homer1. This research was supported by the NCN grant 2012/05/E/ NZ3/00487.
11

The role of Amot and Yap1 in the regulation of dendritic tree morphogenesis and cerebellar functions

61%
Rojek K., Krzemien J., Dolezyczek H., Rylski M., Kaczmarek L., Jaworski J., Proszynski T. J.
Acta Neurobiologiae Experimentalis
|
2019
|
tom 79
|
nr Suppl.1
INTRODUCTION: The Amot‑Yap1 complex plays a major role in the regulation of cell contact inhibition, cellular polarity and growth in many cell types. However, the function of the Amot and Hippo pathway transcription co‑activator Yap1 in the CNS remains unclear. Recent studies have demonstrated that, in mature hippocampal neurons, Amot localizes to dendritic spines where it associates with synaptic protein and regulates actin cytoskeleton. However, its function during neuronal development has not been studied. METHOD(S): Cultured primary neurons were used for RNAi experiments. For in vivo functional analysis, we used Amot and Yap1 conditional KO mice. For deletion in single sparse neurons, mice were injected with low doses of AAV‑CRE. For behavioral analysis, we used rotarod, catwalk, and foot fault tests. RESULTS: We demonstrate that Amot is a critical mediator of dendritogenesis in cultured hippocampal cells and Purkinje cells in the brain. Amot function in developing neurons depends on interactions with Yap1, which is also indispensable for dendrite growth and arborization in vitro. Conditional deletion of Amot or Yap1 in neurons leads to decreased Purkinje cell dendritic tree complexity, abnormal cerebellar morphology, and impaired motor coordination. The ability of Amot and Yap1 to regulate dendritic growth depends on regulation of S6 kinase activity and phosphorylation of S6 ribosomal protein. Hence, we suggest that Amot and Yap1 control dendritic tree morphogenesis through a cross‑talk with the PI3K/mTOR pathway, a known regulator of dendritogenesis. CONCLUSIONS: We identify a novel role for the scaffold protein Amot and the Hippo pathway transcription co‑activator Yap1 in dendritic morphogenesis. FINANCIAL SUPPORT: This research was supported by National Science Center grants 2012/05/E/ NZ3/00487 and 2015/19/N/NZ3/02346.
12

Expression and function of angiomotin family proteins in the brain

51%
Proszynski T., Rojek K., Niewiadomski P., Bernadzki K., Dolezyczek H., Rylski M., Kaczmarek L., Jaworski J.
Acta Neurobiologiae Experimentalis
|
2015
|
tom 75
|
nr Supl.
BACKGROUND AND AIMS: Proper organization of synaptic connections is important for the transmission of information in the central and peripheral nervous systems (CNS and PNS). Synaptic remodeling is a process whereby synapses are rewired to form functional neuronal networks. The molecular mechanisms underlying this process are still poorly understood. We have recently identified the scaffold protein Amotl2 as a potential regulator of neuromuscular junction (NMJ) plasticity. Interestingly, many proteins involved in NMJ remodeling are also implicated in the plasticity of synapses in the brain. Therefore, we investigated the expression and function of Amotl2 and closely related proteins Amot and Amotl1, collectively called Angiomotins, in CNS neurons. METHODS: Primary neuronal cultures were prepared from embryonic day 19 rat brains and transfected using Lipofectamine2000 or Amaxa nucleofection. Cells and mouse brain slices were immunostained to visualize Amot, Amotl1 and Amotl2. To assess the function of Amot in CNS, we knocked down its expression in hippocampal neurons using shRNA, and analyzed neuronal morphology using confocal microscopy. RESULTS: All three angiomotins are widely expressed in the brain. In cultured rat hippocampal neurons and mouse brain slices Amotl2 and Amotl1 localize to the synaptic compartment, whereas Amot is distributed in neurites. Amot depletion in neurons leads to reduced dendritic tree arborization and malfunction of the axon initial segment as reflected by aberrant localization of its main components ankyrin G and neurofascin. CONCLUSIONS: Our experiments identify a novel group of proteins that play a critical role in the organization of neurons and may regulate synaptogenesis both in the CNS and PNS. Amot may play a role in dendrite outgrowth and is critical for the establishment of the axon initial segment, suggesting a role in the maintenance of polarity in neurons. This research was supported by the NCN grant 2012/05/E/ NZ3/00487.
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