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Article ; Online: Magnesium Status and Stress: The Vicious Circle Concept Revisited.

Pickering, Gisèle / Mazur, André / Trousselard, Marion / Bienkowski, Przemyslaw / Yaltsewa, Natalia / Amessou, Mohamed / Noah, Lionel / Pouteau, Etienne

Nutrients

2020 Volume 12, Issue 12

Abstract: Magnesium deficiency and stress are both common conditions among the general population, which, over time, can increase the risk of health consequences. Numerous studies, both in pre-clinical and clinical settings, have investigated the interaction of ... ...

Abstract	Magnesium deficiency and stress are both common conditions among the general population, which, over time, can increase the risk of health consequences. Numerous studies, both in pre-clinical and clinical settings, have investigated the interaction of magnesium with key mediators of the physiological stress response, and demonstrated that magnesium plays an inhibitory key role in the regulation and neurotransmission of the normal stress response. Furthermore, low magnesium status has been reported in several studies assessing nutritional aspects in subjects suffering from psychological stress or associated symptoms. This overlap in the results suggests that stress could increase magnesium loss, causing a deficiency; and in turn, magnesium deficiency could enhance the body's susceptibility to stress, resulting in a magnesium and stress vicious circle. This review revisits the magnesium and stress vicious circle concept, first introduced in the early 1990s, in light of recent available data.
MeSH term(s)	Diet ; Homeostasis ; Humans ; Magnesium/administration & dosage ; Magnesium/metabolism ; Magnesium Deficiency/etiology ; Stress, Physiological
Chemical Substances	Magnesium (I38ZP9992A)
Language	English
Publishing date	2020-11-28
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2518386-2
ISSN	2072-6643 ; 2072-6643
ISSN (online)	2072-6643
ISSN	2072-6643
DOI	10.3390/nu12123672
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Article: Identification de mutations activatrices de gp130 dans la tumorigenèse hépatique.

Zucman-Rossi, Jessica / Amessou, Mohamed / Bioulac-Sage, Paulette / Rebouissou, Sandra

Medecine sciences : M/S

2008 Volume 24, Issue 12, Page(s) 1113–1114

Title translation	Gp130-activating mutations in inflammatory liver adenomas.
MeSH term(s)	Adenoma/chemically induced ; Adenoma/genetics ; Adult ; Carcinoma, Hepatocellular/genetics ; Chemical and Drug Induced Liver Injury/etiology ; Chemical and Drug Induced Liver Injury/genetics ; Contraceptives, Oral, Hormonal/adverse effects ; Cytokine Receptor gp130/genetics ; Cytokine Receptor gp130/physiology ; Disease Progression ; Female ; Gene Expression Regulation, Neoplastic ; Hepatocyte Nuclear Factor 1-alpha/physiology ; Humans ; Inflammation Mediators/metabolism ; Interleukin-6/physiology ; Liver Neoplasms/chemically induced ; Liver Neoplasms/genetics ; Mutation ; Neoplasm Proteins/genetics ; Neoplasm Proteins/physiology ; STAT3 Transcription Factor/physiology ; Sequence Deletion ; Wnt Proteins/physiology ; Young Adult ; beta Catenin/physiology
Chemical Substances	CTNNB1 protein, human ; Contraceptives, Oral, Hormonal ; Hepatocyte Nuclear Factor 1-alpha ; IL6 protein, human ; IL6ST protein, human ; Inflammation Mediators ; Interleukin-6 ; Neoplasm Proteins ; STAT3 Transcription Factor ; STAT3 protein, human ; Wnt Proteins ; beta Catenin ; Cytokine Receptor gp130 (133483-10-0)
Language	French
Publishing date	2008-12
Publishing country	France
Document type	News ; Research Support, Non-U.S. Gov't
ZDB-ID	632733-3
ISSN	1958-5381 ; 0767-0974
ISSN (online)	1958-5381
ISSN	0767-0974
DOI	10.1051/medsci/200824121113
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Article ; Online: Spatio-temporal regulation of EGFR signaling by the Eps15 homology domain-containing protein 3 (EHD3).

Amessou, Mohamed / Ebrahim, Abdul Shukkur / Dilly, Ashok / Joseph, Melvin / Tabolina, Marina / Chukkapalli, Sahiti / Meroueh, Louay / Syed, Joseph T / Liddane, Allison / Lang, Siera Lanae / Al-Katib, Ayad / Kandouz, Mustapha

Oncotarget

2016 Volume 7, Issue 48, Page(s) 79203–79216

Abstract: The epidermal growth factor (EGF) receptor EGFR is a major receptor tyrosine kinase whose role in gliomagenesis is well established. We have recently identified EHD3 [Eps15 homology (EH) domain-containing protein 3], an endocytic trafficking regulatory ... ...

Abstract	The epidermal growth factor (EGF) receptor EGFR is a major receptor tyrosine kinase whose role in gliomagenesis is well established. We have recently identified EHD3 [Eps15 homology (EH) domain-containing protein 3], an endocytic trafficking regulatory protein, as a putative brain tumor suppressor. Here, we investigate the underlying mechanisms, by establishing a novel mechanistic and functional connection between EHD3 and the EGFR signaling pathway. We show that, in response to stimulation with the EGF ligand, EHD3 accelerates the rate of EGFR degradation by dramatically increasing its ubiquitination. As part of this process, EHD3 also regulates EGFR endosomal trafficking by diverting it away from the recycling route into the degradative pathway. Moreover, we found that upon EGF activation, rather than affecting the total MAPK and AKT downstream signaling, EHD3 decreases endosome-based signaling of these two pathways, thus suggesting the contribution of EHD3 in the spatial regulation of EGFR signaling. This function explains the higher sensitivity of EHD3-expressing cells to the growth-inhibitory effects of EGF. In summary, this is the first report supporting a mechanism of EHD3-mediated tumor suppression that involves the attenuation of endosomal signaling of the EGFR oncogene.
Language	English
Publishing date	2016-11-29
Publishing country	United States
Document type	Journal Article
ZDB-ID	2560162-3
ISSN	1949-2553 ; 1949-2553
ISSN (online)	1949-2553
ISSN	1949-2553
DOI	10.18632/oncotarget.13008
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Article: Use of high affinity insulin analogues to assess the functional relationships between insulin receptor trafficking, mitogenic signaling and mRNA expression in rat liver.

Authier, François / Merlen, Clémence / Amessou, Mohamed / Danielsen, Gillian M

Biochimie

2004 Volume 86, Issue 3, Page(s) 157–166

Abstract: We have investigated the functional relationships between insulin receptor (IR) trafficking, mitogenic signaling and mRNA expression in rat liver and primary hepatocytes. The low-K(d) insulin analogues [His(A8),His(B4), Glu(B10),His(B27)]-human insulin (- ...

Abstract	We have investigated the functional relationships between insulin receptor (IR) trafficking, mitogenic signaling and mRNA expression in rat liver and primary hepatocytes. The low-K(d) insulin analogues [His(A8),His(B4), Glu(B10),His(B27)]-human insulin (-HI) (the H2-analogue), [Asp(B10)]HI and [Glu(A13),Glu(B10)]HI, were studied in liver parenchymal cells and compared with wild-type HI and epidermal growth factor (EGF), a mitogenic inducer. The extent and duration of IR endocytosis were markedly increased in response to the H2-analogue and [Asp(B10)]HI compared to wild-type HI, but similar to HI after [Glu(A13),Glu(B10)]HI administration. Importantly, the insulin analogues induced a higher and more prolonged tyrosine phosphorylation of the IR-beta subunit in endosomes compared to authentic HI. A low cell-free endosome-lysosome transfer of the internalized IR was only observed in response to HI and H2-analogue injection. Concomitant with the low endosome-lysosome transfer of the intact IR-beta subunit, 47 and 50 kDa fragments of the IR-beta subunit accumulated in lysosomal fractions. Neither HI nor the insulin analogues promoted the endosomal recruitment and tyrosine phosphorylation of Shc, whereas EGF accessed the Shc signaling pathway. Moreover, EGF induced a fast and prolonged activation of Raf-1 and MAP-kinase pathways whereas HI and insulin analogues displayed a moderate and transient effect. Finally, treatment of primary rat hepatocytes with HI and the protease-resistant H2-analogue did not affect the total level and relative expression of isotype A and B of IR mRNA regardless of time of exposure. These results suggest a lack of relationship between IR trafficking, endosomal tyrosine phosphorylation and mitogenic signaling in rat liver in vivo.
MeSH term(s)	Adaptor Proteins, Signal Transducing/metabolism ; Animals ; Cells, Cultured ; Epidermal Growth Factor/pharmacology ; Extracellular Signal-Regulated MAP Kinases/metabolism ; Gene Expression Regulation/drug effects ; Humans ; Insulin/administration & dosage ; Insulin/analogs & derivatives ; Insulin/pharmacology ; Kinetics ; Ligands ; Liver/drug effects ; Liver/metabolism ; MAP Kinase Signaling System/drug effects ; Phosphotyrosine/metabolism ; Protein Transport/drug effects ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Rats ; Rats, Sprague-Dawley ; Receptor, Insulin/genetics ; Receptor, Insulin/metabolism ; Shc Signaling Adaptor Proteins ; Src Homology 2 Domain-Containing, Transforming Protein 1
Chemical Substances	Adaptor Proteins, Signal Transducing ; Insulin ; Ligands ; RNA, Messenger ; SHC1 protein, human ; Shc Signaling Adaptor Proteins ; Shc1 protein, rat ; Src Homology 2 Domain-Containing, Transforming Protein 1 ; Phosphotyrosine (21820-51-9) ; Epidermal Growth Factor (62229-50-9) ; Receptor, Insulin (EC 2.7.10.1) ; Extracellular Signal-Regulated MAP Kinases (EC 2.7.11.24)
Language	English
Publishing date	2004-03
Publishing country	France
Document type	Journal Article
ZDB-ID	120345-9
ISSN	0300-9084
ISSN	0300-9084
DOI	10.1016/j.biochi.2004.03.005
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Article ; Online: Role of the EphB2 receptor in autophagy, apoptosis and invasion in human breast cancer cells.

Chukkapalli, Sahiti / Amessou, Mohamed / Dilly, Ashok K / Dekhil, Hafedh / Zhao, Jing / Liu, Qiang / Bejna, Alex / Thomas, Ron D / Bandyopadhyay, Sudeshna / Bismar, Tarek A / Neill, Daniel / Azoulay, Laurent / Batist, Gerald / Kandouz, Mustapha

Experimental cell research

2014 Volume 320, Issue 2, Page(s) 233–246

Abstract: The Eph and Ephrin proteins, which constitute the largest family of receptor tyrosine kinases, are involved in normal tissue development and cancer progression. Here, we examined the expression and role of the B-type Eph receptor EphB2 in breast cancers. ...

Abstract	The Eph and Ephrin proteins, which constitute the largest family of receptor tyrosine kinases, are involved in normal tissue development and cancer progression. Here, we examined the expression and role of the B-type Eph receptor EphB2 in breast cancers. By immunohistochemistry using a progression tissue microarray of human clinical samples, we found EphB2 to be expressed in benign tissues, but strongly increased in cancers particularly in invasive and metastatic carcinomas. Subsequently, we found evidence that EphB2, whose expression varies in established cell breast lines, possesses multiple functions. First, the use of a DOX-inducible system to restore EphB2 function to low expressers resulted in decreased tumor growth in vitro and in vivo, while its siRNA-mediated silencing in high expressers increased growth. This function involves the onset of apoptotic death paralleled by caspases 3 and 9 activation. Second, EphB2 was also found to induce autophagy, as assessed by immunofluorescence and/or immunoblotting examination of the LC3, ATG5 and ATG12 markers. Third, EphB2 also has a pro-invasive function in breast cancer cells that involves the regulation of MMP2 and MMP9 metalloproteases and can be blocked by treatment with respective neutralizing antibodies. Furthermore, EphB2-induced invasion is kinase-dependent and is impeded in cells expressing a kinase-dead mutant EphB2. In summary, we identified a mechanism involving a triple role for EphB2 in breast cancer progression, whereby it regulates apoptosis, autophagy, and invasion.
MeSH term(s)	Animals ; Apoptosis/genetics ; Autophagy/genetics ; Breast Neoplasms/genetics ; Breast Neoplasms/pathology ; Cells, Cultured ; Disease Progression ; Female ; Humans ; MCF-7 Cells ; Mice ; Mice, Nude ; Neoplasm Invasiveness ; Receptor, EphB2/genetics ; Receptor, EphB2/physiology ; Tumor Cells, Cultured
Chemical Substances	EPHB2 protein, human (EC 2.7.10.1) ; Receptor, EphB2 (EC 2.7.10.1)
Language	English
Publishing date	2014-01-15
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	1493-x
ISSN	1090-2422 ; 0014-4827
ISSN (online)	1090-2422
ISSN	0014-4827
DOI	10.1016/j.yexcr.2013.10.022
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Article ; Online: Ehd3, a regulator of vesicular trafficking, is silenced in gliomas and functions as a tumor suppressor by controlling cell cycle arrest and apoptosis.

Chukkapalli, Sahiti / Amessou, Mohamed / Dekhil, Hafedh / Dilly, Ashok Kumar / Liu, Qiang / Bandyopadhyay, Sudeshna / Thomas, Ron Dan / Bejna, Alex / Batist, Gerald / Kandouz, Mustapha

Carcinogenesis

2014 Volume 35, Issue 4, Page(s) 877–885

Abstract: EHD3 [Eps15 homology (EH) domain-containing protein 3] is a protein that resides in tubular and vesicular membrane structures and participates in endocytic recycling, although all its functions are unknown. Since Ehd3 is most abundantly expressed in ... ...

Abstract	EHD3 [Eps15 homology (EH) domain-containing protein 3] is a protein that resides in tubular and vesicular membrane structures and participates in endocytic recycling, although all its functions are unknown. Since Ehd3 is most abundantly expressed in brain tissues, we examined its role in brain cancer progression. Using immunohistochemistry, we report loss of EHD3 expression in gliomas, including low-grade astrocytomas, suggesting that this is an early event in gliomagenesis. EHD3 expression is also very low in most of glioma cell lines tested. In two cell lines, a bisulfite sequencing method identifies promoter hypermethylation as a mechanism of Ehd3 silencing, and its expression was restored by the demethylating agent 5-Azacytidine. Doxycycline-inducible restoration of EHD3 expression to glioma cells decreases their growth and invasiveness and induces cell cycle arrest and apoptosis. Furthermore, shRNA-mediated Ehd3 silencing increases cell growth. Using a xenograft model, we demonstrate Ehd3 growth inhibitory functions in glioma cells in vivo. We suggest that Ehd3 functions as a tumor suppressor gene and loss of its expression is a very common event in gliomas. This is the first study to highlight the importance of a member of the C-terminal EHD proteins in cancer and to link their functions to the cell cycle and apoptosis.
MeSH term(s)	Apoptosis/genetics ; Base Sequence ; Brain Neoplasms/genetics ; Brain Neoplasms/pathology ; Carrier Proteins/genetics ; Cell Cycle/genetics ; Cell Division ; Cell Line, Tumor ; DNA Methylation ; DNA Primers ; Gene Silencing ; Genes, Tumor Suppressor ; Glioma/genetics ; Glioma/pathology ; Humans ; Neoplasm Invasiveness ; Polymerase Chain Reaction ; Promoter Regions, Genetic ; Tissue Array Analysis
Chemical Substances	Carrier Proteins ; DNA Primers ; EHD3 protein, human
Language	English
Publishing date	2014-04
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	603134-1
ISSN	1460-2180 ; 0143-3334
ISSN (online)	1460-2180
ISSN	0143-3334
DOI	10.1093/carcin/bgt399
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Article ; Online: Chemistry-based protein modification strategy for endocytic pathway analysis.

Christiano, Romain / Amessou, Mohamed / Shi, Getao / Azoulay, Michel / Blanpain, Annick / Drobecq, Hervé / Melnyk, Oleg / Florent, Jean-Claude / Johannes, Ludger

Biology of the cell

2010 Volume 102, Issue 6, Page(s) 351–359

Abstract: Background information: The integrated analysis of intracellular trafficking pathways is one of the current challenges in the field of cell biology, and functional proteomics has become a powerful technique for the large-scale identification of proteins ...

Abstract	Background information: The integrated analysis of intracellular trafficking pathways is one of the current challenges in the field of cell biology, and functional proteomics has become a powerful technique for the large-scale identification of proteins or lipids and the elucidation of biological processes in their natural contexts. For this, new dynamic strategies must be devised to trace proteins that follow a specific pathway such that their initial and final destinations can be detected by automated means. Results: Here, we report a novel vectorial strategy for trafficking pathway analysis. This strategy is based on a chemical modification of plasma membrane proteins with a bSuPeR (biotinylated sulfation site peptide reagent) and metabolic labelling in the Golgi apparatus, such that plasma membrane proteins that traffic via the retrograde route become detectable in complex mixtures. Efficient synthesis schemes are presented for tailor-made chemical tools that are then applied to the step-by-step validation of the strategy, using a known retrograde cargo protein: the STxB (Shiga toxin B-subunit). bSuPeR modification at the plasma membrane does not affect STxB transport to the Golgi apparatus, where the protein is metabolically labelled, allowing its detection in cell lysates. Conclusions: Our vectorial concept proposes a new chemical approach for traffic-based profiling of proteins that may prove to be applicable to the analysis of diverse endocytic pathways.
MeSH term(s)	Cell Membrane/metabolism ; Endocytosis/physiology ; Fluorescent Antibody Technique, Indirect ; Golgi Apparatus/metabolism ; HeLa Cells ; Humans ; Protein Transport/physiology ; Proteomics/methods
Language	English
Publishing date	2010-03-25
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	245745-3
ISSN	1768-322X ; 0399-0311 ; 0248-4900
ISSN (online)	1768-322X
ISSN	0399-0311 ; 0248-4900
DOI	10.1042/BC20100008
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Article: Synthesis of globo- and isoglobotriosides bearing a cinnamoylphenyl tag as novel electrophilic thiol-specific carbohydrate reagents.

Aly, Mohamed R E / Rochaix, Pascal / Amessou, Mohamed / Johannes, Ludger / Florent, Jean-Claude

Carbohydrate research

2006 Volume 341, Issue 12, Page(s) 2026–2036

Abstract: The galactosyl donor, 4,6-di-O-acetyl-2,3-di-O-benzyl-D-galactopyranosyl trichloroacetimidate, was efficiently coupled with regioselectively benzylated lactoside acceptors under standard conditions to stereoselectively afford the corresponding ... ...

Abstract	The galactosyl donor, 4,6-di-O-acetyl-2,3-di-O-benzyl-D-galactopyranosyl trichloroacetimidate, was efficiently coupled with regioselectively benzylated lactoside acceptors under standard conditions to stereoselectively afford the corresponding globotrioside and isoglobotrioside derivatives in very good yields. These glycosides were smoothly functionalized with a 6-(p-cinnamoylphenoxy)-hexyl tether tag as novel electrophilic thiol-specific carbohydrate reagents. Immobilization of the globotrioside conjugate to Thiopropyl Sepharose 6B for purification of B-subunit of Shiga toxin (StxB) and coupling of a model cysteine-containing protein (StxB-Z(n)-Cys) to the isoglobotrioside conjugate were both performed with high efficiency.
MeSH term(s)	Carbohydrate Sequence ; Chalcone/chemistry ; Cinnamates/chemistry ; Molecular Sequence Data ; Molecular Structure ; Oligosaccharides/chemical synthesis ; Oligosaccharides/chemistry ; Phenols/chemistry ; Sepharose/analogs & derivatives ; Sepharose/chemistry ; Shiga Toxin/chemistry ; Shiga Toxin/isolation & purification ; Sulfhydryl Reagents/chemical synthesis ; Sulfhydryl Reagents/chemistry ; Trioses/chemical synthesis ; Trioses/chemistry
Chemical Substances	Cinnamates ; Oligosaccharides ; Phenols ; Sulfhydryl Reagents ; Trioses ; Chalcone (5S5A2Q39HX) ; sepharose CL 6B (62610-50-8) ; Shiga Toxin (75757-64-1) ; Sepharose (9012-36-6)
Language	English
Publishing date	2006-09-04
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1435-7
ISSN	1873-426X ; 0008-6215
ISSN (online)	1873-426X
ISSN	0008-6215
DOI	10.1016/j.carres.2006.03.044
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Article ; Online: Measuring retrograde transport to the trans-Golgi network.

Amessou, Mohamed / Popoff, Vincent / Yelamos, Belèn / Saint-Pol, Agnès / Johannes, Ludger

Current protocols in cell biology

2006 Volume Chapter 15, Page(s) Unit 15.10

Abstract: The recently described retrograde transport route is a highly selective pathway that allows some internalized molecules to reach the trans-Golgi network from early/recycling endosomes, bypassing the recycling route to the plasma membrane and the late ... ...

Abstract	The recently described retrograde transport route is a highly selective pathway that allows some internalized molecules to reach the trans-Golgi network from early/recycling endosomes, bypassing the recycling route to the plasma membrane and the late endocytic pathway. The non-toxic receptor-binding B-subunit of bacterial Shiga toxin has played an important role in the discovery and molecular dissection of membrane trafficking at the early/recycling endosomes-TGN interface. This unit describes several recent methods for quantitative biochemical and morphological analysis of retrograde transport. The sulfation assay permits the detection and quantification of cargo protein transport from endosomes to the TGN, describing how sulfation-site peptides can be chemically coupled to cargo proteins. Furthermore, a variant of the sulfation assay on permeabilized cells is presented. The chemical crosslinking theme is extended to horseradish peroxidase for the ultrastructural study of the Shiga toxin-containing early/recycling endosomes by whole mount analysis. Finally, an endocytosis assay describes concomitant analysis of cellular uptake of Shiga toxin and transferrin.
MeSH term(s)	Biological Assay ; HeLa Cells ; Humans ; Protein Transport/physiology ; Shiga Toxins/metabolism ; trans-Golgi Network/metabolism
Chemical Substances	Shiga Toxins ; stxB toxin
Language	English
Publishing date	2006-10
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1934-2616
ISSN (online)	1934-2616
DOI	10.1002/0471143030.cb1510s32
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Article: Shiga Toxin-Mediated Retrograde Delivery of a Topoisomerase I Inhibitor Prodrug

El Alaoui, Abdessamad / Schmidt, Frédéric / Amessou, Mohamed / Sarr, Marianne / Decaudin, Didier / Florent, Jean-Claude / Johannes, Ludger

Angewandte Chemie. 2007 Aug. 27, v. 46, no. 34

2007

Language	English
Dates of publication	2007-0827
Size	p. 6469-6472.
Publishing place	Wiley-VCH Verlag
Document type	Article
ZDB-ID	2011836-3
ISSN	1521-3773 ; 1433-7851
ISSN (online)	1521-3773
ISSN	1433-7851
DOI	10.1002/anie.200701270
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