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  1. Article ; Online ; Conference proceedings: Meeting report: 16(th) European Congress on Biotechnology.

    Cicchetti, Gregor / Peng, Judy

    Biotechnology journal

    2014  Volume 9, Issue 12, Page(s) 1470–1471

    MeSH term(s) Biotechnology/methods ; Biotechnology/organization & administration ; Humans
    Language English
    Publishing date 2014-12
    Publishing country Germany
    Document type Congresses
    ZDB-ID 2221885-3
    ISSN 1860-7314 ; 1860-6768
    ISSN (online) 1860-7314
    ISSN 1860-6768
    DOI 10.1002/biot.201400599
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    Zs.A 6349: Show issues Location:
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  2. Book ; Article ; Online: Viral and Microbial Threats - a joint position paper by Analytical Research Infrastructures of Europe (ARIE)

    Cicchetti, Gregor / van Daalen, Mirjam* / Gleizes, Pierre-Emmanuel / Leonard, Gordon / Redlich, Britta / Schertler, Gebhard / Toimil Morales, Maria Eugenia / Wacklin-Knecht, Hanna

    2020  

    Abstract: Analytical Research Infrastructures of Europe (ARIE) join forces to face threats such as COVID-19 and potential future crises. With this paper, the ARIE enhanced its cross-border, multidisciplinary collaboration to offer Europe a strong and valid weapon ... ...

    Abstract Analytical Research Infrastructures of Europe (ARIE) join forces to face threats such as COVID-19 and potential future crises. With this paper, the ARIE enhanced its cross-border, multidisciplinary collaboration to offer Europe a strong and valid weapon against the present COVID-19 challenge and other potential viral and microbial threats.
    Keywords viral threats ; COVID-19 ; Coronavirus ; research infrastructures ; electrons ; photons ; lasers ; protons ; ions ; high magnetic field ; neutrons ; LEAPS ; LENS ; DREAM ; Inspire Project ; EMFL ; RADIATE ; Laserlab ; microbial threats ; covid19
    Language English
    Publishing date 2020-09-16
    Publishing country eu
    Document type Book ; Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  3. Book ; Thesis: Ligand interactions of the Listeria monocytogenes protein, ActA

    Cicchetti, Gregor

    evidence of phosphoinositide association and actinbinding

    1999  

    Author's details vorgelegt von Gregor Cicchetti
    Keywords Wechselwirkung ; Listeria monocytogenes ; Phosphoinositide ; Actin-bindende Proteine
    Language English
    Size VI, 111 S, Ill., graph. Darst, 21 cm
    Document type Book ; Thesis
    Thesis / German Habilitation thesis Unv., Diss--Köln, 1999
    Database Former special subject collection: coastal and deep sea fishing

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  4. Book ; Thesis: Ligand interactions of the Listeria monocytogenes protein, ActA

    Cicchetti, Gregor

    evidence of phosphoinositide association and actinbinding

    1999  

    Author's details vorgelegt von Gregor Cicchetti
    Keywords Wechselwirkung ; Listeria monocytogenes ; Phosphoinositide ; Actin-bindende Proteine
    Language English
    Size VI, 111 S, Ill., graph. Darst, 21 cm
    Document type Book ; Thesis
    Thesis / German Habilitation thesis Unv., Diss--Köln, 1999
    Database Library catalogue of the German National Library of Science and Technology (TIB), Hannover

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  5. Article: Chemotactic signaling pathways in neutrophils: from receptor to actin assembly.

    Cicchetti, Gregor / Allen, Philip G / Glogauer, Michael

    Critical reviews in oral biology and medicine : an official publication of the American Association of Oral Biologists

    2002  Volume 13, Issue 3, Page(s) 220–228

    Abstract: In this review, we present an overview of the signaling elements between neutrophil chemotactic receptors and the actin cytoskeleton that drives cell motility. From receptor-ligand interactions, activation of heterotrimeric G-proteins, their downstream ... ...

    Abstract In this review, we present an overview of the signaling elements between neutrophil chemotactic receptors and the actin cytoskeleton that drives cell motility. From receptor-ligand interactions, activation of heterotrimeric G-proteins, their downstream effectors PLC and PI-3 kinase, the activation of small GTPases of the Rho family, and their regulation of particular cytoskeletal regulatory proteins, we describe pathways specific to the chemotaxing neutrophil and elements documented to be important for neutrophil function.
    MeSH term(s) Actins/metabolism ; Actins/physiology ; Chemotactic Factors/physiology ; Chemotaxis, Leukocyte/physiology ; Cytoskeleton/metabolism ; Cytoskeleton/physiology ; GTP Phosphohydrolases/physiology ; GTP-Binding Proteins/physiology ; Humans ; Neutrophil Activation/physiology ; Neutrophil Infiltration/physiology ; Neutrophils/physiology ; Phosphatidylinositol 3-Kinases/physiology ; Phosphatidylinositols/physiology ; Receptors, Cell Surface/physiology ; Signal Transduction/physiology ; Type C Phospholipases/physiology ; rho GTP-Binding Proteins/physiology
    Chemical Substances Actins ; Chemotactic Factors ; Phosphatidylinositols ; Receptors, Cell Surface ; Phosphatidylinositol 3-Kinases (EC 2.7.1.-) ; Type C Phospholipases (EC 3.1.4.-) ; GTP Phosphohydrolases (EC 3.6.1.-) ; GTP-Binding Proteins (EC 3.6.1.-) ; rho GTP-Binding Proteins (EC 3.6.5.2)
    Language English
    Publishing date 2002-06-28
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 1130962-3
    ISSN 1045-4411
    ISSN 1045-4411
    DOI 10.1177/154411130201300302
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 3504: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
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    Jg. 1995 - 2021: Lesesall (2.OG)
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  6. Article: Mechanisms of gelsolin-dependent and -independent EGF-stimulated cell motility in a human lung epithelial cell line.

    Lader, Alan S / Lee, Justin J / Cicchetti, Gregor / Kwiatkowski, David J

    Experimental cell research

    2005  Volume 307, Issue 1, Page(s) 153–163

    Abstract: Acquisition of motility is an important step in malignant progression of tumor cells and involves dynamic changes in actin filament architecture orchestrated by many actin binding proteins. A role for the actin-binding protein gelsolin has been ... ...

    Abstract Acquisition of motility is an important step in malignant progression of tumor cells and involves dynamic changes in actin filament architecture orchestrated by many actin binding proteins. A role for the actin-binding protein gelsolin has been demonstrated in fibroblast motility. In this report, we investigated the role of gelsolin in bronchial epithelial cell motility. The non-tumorigenic bronchial epithelial cell line, NL20 migrated towards EGF in a modified Boyden chamber cell motility assay. However, the tumorigenic NL20-TA cell line derived from the NL20 cells and lacking gelsolin, did not migrate towards EGF. Ectopic expression of gelsolin in NL20-TA cells restored the EGF response, while motility of NL20-TA derived cells towards serum, PDGF, and fibronectin was independent of gelsolin expression. PI3-kinase inhibition failed to block EGF-stimulated motility in gelsolin transfected NL20-TA cells. Furthermore, EGF stimulated a motility response in cells lacking gelsolin in the presence of fibronectin or fibrinogen that was blocked with PI3-kinase inhibition. Thus, EGF-stimulated motility in NL20 cells and its derivatives are gelsolin dependent and PI3-kinase independent, while fibronectin and fibrinogen enhances EGF-stimulated motility through a pathway independent of gelsolin and dependent upon PI3-kinase.
    MeSH term(s) Antibodies, Monoclonal/metabolism ; Calcium/metabolism ; Cell Line ; Cell Line, Tumor ; Cell Movement/drug effects ; Chromones/pharmacology ; Culture Media, Serum-Free ; Enzyme Inhibitors/pharmacology ; Epidermal Growth Factor/pharmacology ; Epithelial Cells/drug effects ; Epithelial Cells/metabolism ; Estrenes/pharmacology ; Fibrinogen/pharmacology ; Fibronectins/pharmacology ; Gelsolin/metabolism ; Humans ; Lung/cytology ; Models, Biological ; Morpholines/pharmacology ; Phosphatidylinositol 3-Kinases/metabolism ; Platelet-Derived Growth Factor/pharmacology ; Pyrrolidinones/pharmacology ; Serum/metabolism ; Transfection ; Type C Phospholipases/metabolism
    Chemical Substances Antibodies, Monoclonal ; Chromones ; Culture Media, Serum-Free ; Enzyme Inhibitors ; Estrenes ; Fibronectins ; Gelsolin ; Morpholines ; Platelet-Derived Growth Factor ; Pyrrolidinones ; 1-(6-((3-methoxyestra-1,3,5(10)-trien-17-yl)amino)hexyl)-1H-pyrrole-2,5-dione (112648-68-7) ; 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (31M2U1DVID) ; Epidermal Growth Factor (62229-50-9) ; Fibrinogen (9001-32-5) ; Phosphatidylinositol 3-Kinases (EC 2.7.1.-) ; Type C Phospholipases (EC 3.1.4.-) ; Calcium (SY7Q814VUP)
    Language English
    Publishing date 2005-07-01
    Publishing country United States
    Document type Comparative Study ; Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 1493-x
    ISSN 1090-2422 ; 0014-4827
    ISSN (online) 1090-2422
    ISSN 0014-4827
    DOI 10.1016/j.yexcr.2005.03.001
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 563: Show issues Location:
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  7. Article: A ratiometric expressible FRET sensor for phosphoinositides displays a signal change in highly dynamic membrane structures in fibroblasts.

    Cicchetti, Gregor / Biernacki, Melinda / Farquharson, Jessica / Allen, Philip G

    Biochemistry

    2004  Volume 43, Issue 7, Page(s) 1939–1949

    Abstract: Phosphoinositides are important signal transduction intermediates in cell growth, survival, and motility. We have invented a fluorescence sensor for polyphosphorylated phosphoinositides based on a peptide derived from the Listeria protein ActA that ... ...

    Abstract Phosphoinositides are important signal transduction intermediates in cell growth, survival, and motility. We have invented a fluorescence sensor for polyphosphorylated phosphoinositides based on a peptide derived from the Listeria protein ActA that undergoes a random coil to helix transition upon lipid binding. The sensor, termed CAY, is a fusion protein of cyan and yellow fluorescent proteins flanking the peptide at its N- and C-termini, respectively. CAY displays fluorescence resonance energy transfer in vitro in the absence of phosphorylated phosphoinositides, and this energy transfer is lost upon interaction with these phospholipids. These results demonstrate that a short peptide undergoing a coil to helix transition can be sufficient for the engineering of a FRET-based biosensor. CAY is predominantly localized to the cytoplasm in fibroblasts expressing the sensor but shows loss of fluorescence resonance energy transfer in regions of active actin dynamics such as ruffles that have previously been demonstrated to contain high levels of phosphoinositides.
    MeSH term(s) Amino Acid Sequence ; Animals ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Fibroblasts/chemistry ; Fibroblasts/metabolism ; Fluorescence Resonance Energy Transfer/methods ; Fluorescent Dyes/chemistry ; Green Fluorescent Proteins ; Luminescent Proteins/genetics ; Membrane Microdomains/chemistry ; Membrane Microdomains/genetics ; Membrane Microdomains/metabolism ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Mice ; Microinjections ; Molecular Sequence Data ; Phosphatidylinositols/chemistry ; Recombinant Fusion Proteins/biosynthesis ; Recombinant Fusion Proteins/chemistry ; Recombinant Fusion Proteins/genetics ; Signal Transduction/genetics ; Swiss 3T3 Cells ; Thermodynamics
    Chemical Substances Bacterial Proteins ; Fluorescent Dyes ; Luminescent Proteins ; Membrane Proteins ; Phosphatidylinositols ; Recombinant Fusion Proteins ; yellow fluorescent protein, Bacteria ; actA protein, Listeria monocytogenes (144430-05-7) ; Green Fluorescent Proteins (147336-22-9)
    Language English
    Publishing date 2004-02-24
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 1108-3
    ISSN 1520-4995 ; 0006-2960
    ISSN (online) 1520-4995
    ISSN 0006-2960
    DOI 10.1021/bi035480w
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    Zs.A 217: Show issues Location:
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  8. Article: Time-resolved structural studies with serial crystallography: A new light on retinal proteins.

    Panneels, Valérie / Wu, Wenting / Tsai, Ching-Ju / Nogly, Przemek / Rheinberger, Jan / Jaeger, Kathrin / Cicchetti, Gregor / Gati, Cornelius / Kick, Leonhard M / Sala, Leonardo / Capitani, Guido / Milne, Chris / Padeste, Celestino / Pedrini, Bill / Li, Xiao-Dan / Standfuss, Jörg / Abela, Rafael / Schertler, Gebhard

    Structural dynamics (Melville, N.Y.)

    2015  Volume 2, Issue 4, Page(s) 41718

    Abstract: Structural information of the different conformational states of the two prototypical light-sensitive membrane proteins, bacteriorhodopsin and rhodopsin, has been obtained in the past by X-ray cryo-crystallography and cryo-electron microscopy. However, ... ...

    Abstract Structural information of the different conformational states of the two prototypical light-sensitive membrane proteins, bacteriorhodopsin and rhodopsin, has been obtained in the past by X-ray cryo-crystallography and cryo-electron microscopy. However, these methods do not allow for the structure determination of most intermediate conformations. Recently, the potential of X-Ray Free Electron Lasers (X-FELs) for tracking the dynamics of light-triggered processes by pump-probe serial femtosecond crystallography has been demonstrated using 3D-micron-sized crystals. In addition, X-FELs provide new opportunities for protein 2D-crystal diffraction, which would allow to observe the course of conformational changes of membrane proteins in a close-to-physiological lipid bilayer environment. Here, we describe the strategies towards structural dynamic studies of retinal proteins at room temperature, using injector or fixed-target based serial femtosecond crystallography at X-FELs. Thanks to recent progress especially in sample delivery methods, serial crystallography is now also feasible at synchrotron X-ray sources, thus expanding the possibilities for time-resolved structure determination.
    Language English
    Publishing date 2015-06-29
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2758684-4
    ISSN 2329-7778
    ISSN 2329-7778
    DOI 10.1063/1.4922774
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  9. Article: Rac1-null mouse embryonic fibroblasts are motile and respond to platelet-derived growth factor.

    Vidali, Luis / Chen, Feng / Cicchetti, Gregor / Ohta, Yasutaka / Kwiatkowski, David J

    Molecular biology of the cell

    2006  Volume 17, Issue 5, Page(s) 2377–2390

    Abstract: Previous studies of Rac1 in fibroblasts have used dominant negative constructs, which may have nonspecific effects. We used a conditional Rac1 allele to critically examine Rac1 function in mouse fibroblasts. Lack of Rac1 had dramatic effects on ... ...

    Abstract Previous studies of Rac1 in fibroblasts have used dominant negative constructs, which may have nonspecific effects. We used a conditional Rac1 allele to critically examine Rac1 function in mouse fibroblasts. Lack of Rac1 had dramatic effects on nonconfluent cells, which were elongated and had extensive blebbing, but no lamellipodia or ruffle formation. However, Rac1-null fibroblasts translocated using pseudopodia-like protrusions without lamellipodia, migrating toward a platelet-derived growth factor (PDGF) gradient as efficiently as their wild-type counterparts. Rac1-null fibroblasts closed wounds in vitro and spread on a fibronectin substrate, although at a slower rate than wild-type cells. However, Rac1-null cells were markedly impaired in proliferation, with a defect in G1 to S transition, although they were capable of surviving in culture for more than 2 wk. These results refine our understanding of the functions of Rac1, indicate that lamellipodia formation is not required for cell motility, and show that PDGF-induced chemotaxis can occur in the absence of both lamellipodia and Rac1.
    MeSH term(s) Actins/analysis ; Actins/metabolism ; Animals ; Cell Cycle/genetics ; Cell Proliferation ; Cells, Cultured ; Chemotaxis/genetics ; Embryo, Mammalian/cytology ; Embryo, Mammalian/drug effects ; Fibroblasts/chemistry ; Fibroblasts/drug effects ; Fibroblasts/physiology ; Focal Adhesions/genetics ; Mice ; Mice, Mutant Strains ; Platelet-Derived Growth Factor/pharmacology ; Pseudopodia/genetics ; Pseudopodia/physiology ; Wound Healing/genetics ; rac1 GTP-Binding Protein/genetics ; rac1 GTP-Binding Protein/physiology
    Chemical Substances Actins ; Platelet-Derived Growth Factor ; rac1 GTP-Binding Protein (EC 3.6.5.2)
    Language English
    Publishing date 2006-03-08
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1098979-1
    ISSN 1939-4586 ; 1059-1524
    ISSN (online) 1939-4586
    ISSN 1059-1524
    DOI 10.1091/mbc.e05-10-0955
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2853: Show issues Location:
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    Zs.MO 410: Show issues

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  10. Article: Arp2/3 complex-deficient mouse fibroblasts are viable and have normal leading-edge actin structure and function.

    Di Nardo, Alessia / Cicchetti, Gregor / Falet, Hervé / Hartwig, John H / Stossel, Thomas P / Kwiatkowski, David J

    Proceedings of the National Academy of Sciences of the United States of America

    2005  Volume 102, Issue 45, Page(s) 16263–16268

    Abstract: RNA interference silencing of up to 90% of Arp3 protein expression, a major subunit of the Arp2/3 complex, proportionately decreases the intracellular motility of Listeria monocytogenes and actin nucleation activity ascribable to the Arp2/3 complex in ... ...

    Abstract RNA interference silencing of up to 90% of Arp3 protein expression, a major subunit of the Arp2/3 complex, proportionately decreases the intracellular motility of Listeria monocytogenes and actin nucleation activity ascribable to the Arp2/3 complex in mouse embryonic fibroblasts. However, the Arp2/3-deficient cells exhibit unimpaired lamellipodial actin network structure, translational locomotion, spreading, actin assembly, and ruffling responses. In addition, Arp3-silenced cells expressing neural Wiskott-Aldrich syndrome protein-derived peptides that inhibit Arp2/3 complex function in wild-type cells retained normal PDGF-induced ruffling. The Arp2/3 complex can be dispensable for leading-edge actin remodeling.
    MeSH term(s) Actin-Related Protein 2-3 Complex/genetics ; Actin-Related Protein 2-3 Complex/physiology ; Actins/chemistry ; Actins/physiology ; Animals ; Cells, Cultured ; Fibroblasts/physiology ; Gene Silencing ; Mice ; Platelet-Derived Growth Factor/pharmacology ; RNA Interference
    Chemical Substances Actin-Related Protein 2-3 Complex ; Actins ; Platelet-Derived Growth Factor
    Language English
    Publishing date 2005-11-08
    Publishing country United States
    Document type Journal Article
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.0508228102
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