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Book ; Thesis: Kohäsion in psychotherapeutischen Gruppen

Marquet, Andrea

Entwicklung und Anwendung einer Skala zur Messung von Gruppenkohäsion unter Berücksichtigung der Perspektiven Patient, Therapeut und Beobachter

(Schriften zur medizinischen Psychologie ; 20)

2008

Author's details	Andrea Marquet
Series title	Schriften zur medizinischen Psychologie ; 20
Collection
Keywords	Gruppentherapie ; Gruppenkohäsion ; Messung
Subject	Gruppenzusammenhalt ; Kohäsion ; Zusammenhalt ; Gruppenpsychotherapie ; Messen ; Messverfahren ; Messmethode ; Messkonzept
Language	German
Size	282 S., 51 schw.-w. Ill., 44 schw.-w. Tab., 210 mm x 148 mm, 355 gr.
Publisher	Kovac, J
Publishing place	Hamburg
Publishing country	Germany
Document type	Book ; Thesis
Thesis / German Habilitation thesis	Hamburg, Univ., Diss., 2007
HBZ-ID	HT015539398
ISBN	978-3-8300-3407-0 ; 3-8300-3407-5
Database	Catalogue ZB MED Medicine, Health

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2008 A 2792	order for loan	Magazin

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Book: Friedrich Wilhelm Wagner

Marquet, Andreas

1894–1971. Eine politische Biografie

(Politik- und Gesellschaftsgeschichte ; 100)

2015

Institution	Verlag J. H. W. Dietz Nachf
Author's details	Andreas Marquet
Series title	Politik- und Gesellschaftsgeschichte ; 100
Language	German
Size	485 S, Ill, 230 mm x 160 mm
Publisher	Dietz, J H
Publishing place	Bonn
Document type	Book
ISBN	9783801242312 ; 3801242312 ; 3801242315
Database	Former special subject collection: coastal and deep sea fishing

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Article: Iron-sulfur proteins as initiators of radical chemistry.

Marquet, Andrée / Bui, Bernadette Tse Sum / Smith, Alison G / Warren, Martin J

Natural product reports

2007 Volume 24, Issue 5, Page(s) 1027–1040

Abstract: Iron-sulfur proteins are very versatile biological entities for which many new functions are continuously being unravelled. This review focus on their role in the initiation of radical chemistry, with special emphasis on radical-SAM enzymes, since ... ...

Abstract	Iron-sulfur proteins are very versatile biological entities for which many new functions are continuously being unravelled. This review focus on their role in the initiation of radical chemistry, with special emphasis on radical-SAM enzymes, since several members of the family catalyse key steps in the biosynthetic pathways of cofactors such as biotin, lipoate, thiamine, heme and the molybdenum cofactor. It will also include other examples to show the chemical logic which is emerging from the presently available data on this family of enzymes. The common step in all the (quite different) reactions described here is the monoelectronic reductive cleavage of SAM by a reduced [4Fe-4S](1+) cluster, producing methionine and a highly oxidising deoxyadenosyl radical, which can initiate chemically difficult reactions. This set of enzymes, which represent a means to perform oxidation under reductive conditions, are often present in anaerobic organisms. Some other, non-SAM-dependent, radical reactions obeying the same chemical logic are also covered.
MeSH term(s)	Enzymes/metabolism ; Iron-Sulfur Proteins/chemistry ; Iron-Sulfur Proteins/metabolism ; Molecular Structure
Chemical Substances	Enzymes ; Iron-Sulfur Proteins
Language	English
Publishing date	2007-09-11
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2002546-4
ISSN	1460-4752 ; 0265-0568
ISSN (online)	1460-4752
ISSN	0265-0568
DOI	10.1039/b703109m
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Total synthesis of amiclenomycin, an inhibitor of biotin biosynthesis.

Mann, Stéphane / Carillon, Sophie / Breyne, Olivier / Marquet, Andrée

Chemistry (Weinheim an der Bergstrasse, Germany)

2002 Volume 8, Issue 2, Page(s) 439–450

Abstract: We describe the first synthesis of amiclenomycin, a natural product that has been found to inhibit biotin biosynthesis and, as a consequence, to exhibit antibiotic properties. Structure 1, with a trans relationship between the ring substituents. had ... ...

Abstract	We describe the first synthesis of amiclenomycin, a natural product that has been found to inhibit biotin biosynthesis and, as a consequence, to exhibit antibiotic properties. Structure 1, with a trans relationship between the ring substituents. had previously been proposed for amiclenomycin on the basis of its 1H NMR spectrum. We have prepared the trans and cis isomers 1 and 2 by unequivocal routes and we conclude that the natural product is in fact the cis isomer 2. The properly substituted cyclohexadienyl rings were constructed first. A cycloaddition reaction between 1,2-di(phenylsulfonyl)ethylene and the N-allyloxycarbonyl diene 13, followed by reductive elimination of the phenylsulfinyl groups, gave the cis isomer 15. To obtain the trans isomer, the O-trimethylsilyl diene was used to give the cis hydroxylated Diels-Alder adduct 33, which was transformed into the corresponding trans amino derivative by means of a Mitsunobu reaction. The L-alpha-amino acid functionality was introduced by means of a Strecker reaction on the aldehydes 16 and 42, followed by enzymatic hydrolysis with immobilised pronase.
MeSH term(s)	Aminobutyrates/chemical synthesis ; Aminobutyrates/chemistry ; Anti-Bacterial Agents/chemical synthesis ; Anti-Bacterial Agents/chemistry ; Biological Products/chemical synthesis ; Biological Products/chemistry ; Biotin/biosynthesis ; Molecular Structure
Chemical Substances	Aminobutyrates ; Anti-Bacterial Agents ; Biological Products ; amiclenomycin (53696-70-1) ; Biotin (6SO6U10H04)
Language	English
Publishing date	2002-01-18
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1478547-x
ISSN	1521-3765 ; 0947-6539
ISSN (online)	1521-3765
ISSN	0947-6539
DOI	10.1002/1521-3765(20020118)8:2<439::AID-CHEM439>3.0.CO;2-5
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Metal and cofactor insertion.

Mendel, Ralf R / Smith, Alison G / Marquet, Andree / Warren, Martin J

Natural product reports

2007 Volume 24, Issue 5, Page(s) 963–971

Abstract: Cells require metal ions as cofactors for the assembly of metalloproteins. Principally one has to distinguish between metal ions that are directly incorporated into their cognate sites on proteins and those metal ions that have to become part of ... ...

Abstract	Cells require metal ions as cofactors for the assembly of metalloproteins. Principally one has to distinguish between metal ions that are directly incorporated into their cognate sites on proteins and those metal ions that have to become part of prosthetic groups, cofactors or complexes prior to insertion of theses moieties into target proteins. Molybdenum is only active as part of the molybdenum cofactor, iron can be part of diverse Fe-S clusters or of the heme group, while copper ions are directly delivered to their targets. We will focus in greater detail on molybdenum metabolism because molybdenum metabolism is a good example for demonstrating the role and the network of metals in metabolism: each of the three steps in the pathway of molybdenum cofactor formation depends on a different metal (iron, copper, molybdenum) and also the enzymes finally harbouring the molybdenum cofactor need additional metal-containing groups to function (iron sulfur-clusters, heme-iron).
MeSH term(s)	Coenzymes/physiology ; Copper/physiology ; Iron/physiology ; Metalloproteins/physiology ; Molecular Structure ; Molybdenum/physiology ; Molybdenum Cofactors ; Pteridines
Chemical Substances	Coenzymes ; Metalloproteins ; Molybdenum Cofactors ; Pteridines ; Copper (789U1901C5) ; Molybdenum (81AH48963U) ; molybdenum cofactor (ATN6EG42UQ) ; Iron (E1UOL152H7)
Language	English
Publishing date	2007-09-12
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2002546-4
ISSN	1460-4752 ; 0265-0568
ISSN (online)	1460-4752
ISSN	0265-0568
DOI	10.1039/b703112m
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Iron–sulfur proteins as initiators of radical chemistry

Marquet, Andrée / Tse Sum Bui, Bernadette / Smith, Alison G. / Warren, Martin J.

Natural product reports. 2007 Sept. 26, v. 24, no. 5

2007

Abstract: Iron–sulfur proteins are very versatile biological entities for which many new functions are continuously being unravelled. This review focus on their role in the initiation of radical chemistry, with special emphasis on ‘radical-SAM’ enzymes, since ... ...

Abstract	Iron–sulfur proteins are very versatile biological entities for which many new functions are continuously being unravelled. This review focus on their role in the initiation of radical chemistry, with special emphasis on ‘radical-SAM’ enzymes, since several members of the family catalyse key steps in the biosynthetic pathways of cofactors such as biotin, lipoate, thiamine, heme and the molybdenum cofactor. It will also include other examples to show the chemical logic which is emerging from the presently available data on this family of enzymes. The common step in all the (quite different) reactions described here is the monoelectronic reductive cleavage of SAM by a reduced [4Fe–4S]¹⁺ cluster, producing methionine and a highly oxidising deoxyadenosyl radical, which can initiate chemically difficult reactions. This set of enzymes, which represent a means to perform oxidation under reductive conditions, are often present in anaerobic organisms. Some other, non-SAM-dependent, radical reactions obeying the same chemical logic are also covered.
Keywords	biosynthesis ; biotin ; heme ; methionine ; molybdenum ; oxidation ; thiamin
Language	English
Dates of publication	2007-0926
Size	p. 1027-1040.
Publishing place	The Royal Society of Chemistry
Document type	Article
ZDB-ID	2002546-4
ISSN	1460-4752 ; 0265-0568
ISSN (online)	1460-4752
ISSN	0265-0568
DOI	10.1039/b703109m
Database	NAL-Catalogue (AGRICOLA)

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Article: Elucidating biosynthetic pathways for vitamins and cofactors.

Webb, Michael E / Marquet, Andrée / Mendel, Ralf R / Rébeillé, Fabrice / Smith, Alison G

Natural product reports

2007 Volume 24, Issue 5, Page(s) 988–1008

Abstract: The elucidation of the pathways to the water-soluble vitamins and cofactors has provided many biochemical and chemical challenges. This is a reflection both of their complex chemical nature, and the fact that they are often made in small amounts, making ... ...

Abstract	The elucidation of the pathways to the water-soluble vitamins and cofactors has provided many biochemical and chemical challenges. This is a reflection both of their complex chemical nature, and the fact that they are often made in small amounts, making detection of the enzyme activities and intermediates difficult. Here we present an orthogonal review of how these challenges have been overcome using a combination of methods, which are often ingenious. We make particular reference to some recent developments in the study of biotin, pantothenate, folate, pyridoxol, cobalamin, thiamine, riboflavin and molybdopterin biosynthesis.
MeSH term(s)	Biosynthetic Pathways ; Coenzymes/biosynthesis ; Molecular Structure ; Vitamins/biosynthesis
Chemical Substances	Coenzymes ; Vitamins
Language	English
Publishing date	2007-10
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2002546-4
ISSN	1460-4752 ; 0265-0568
ISSN (online)	1460-4752
ISSN	0265-0568
DOI	10.1039/b703105j
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Structural basis for the inhibition of the biosynthesis of biotin by the antibiotic amiclenomycin.

Sandmark, Jenny / Mann, Stephane / Marquet, Andree / Schneider, Gunter

The Journal of biological chemistry

2002 Volume 277, Issue 45, Page(s) 43352–43358

Abstract: The antibiotic amiclenomycin blocks the biosynthesis of biotin by inhibiting the pyridoxal-phosphate-dependent enzyme diaminopelargonic acid synthase. Inactivation of the enzyme is stereoselective, i.e. the cis isomer of amiclenomycin is a potent ... ...

Abstract	The antibiotic amiclenomycin blocks the biosynthesis of biotin by inhibiting the pyridoxal-phosphate-dependent enzyme diaminopelargonic acid synthase. Inactivation of the enzyme is stereoselective, i.e. the cis isomer of amiclenomycin is a potent inhibitor, whereas the trans isomer is much less reactive. The crystal structure of the complex of the holoenzyme and amiclenomycin at 1.8 A resolution reveals that the internal aldimine linkage between the cofactor and the side chain of the catalytic residue Lys-274 is broken. Instead, a covalent bond is formed between the 4-amino nitrogen of amiclenomycin and the C4' carbon atom of pyridoxal-phosphate. The electron density for the bound inhibitor suggests that aromatization of the cyclohexadiene ring has occurred upon formation of the covalent adduct. This process could be initiated by proton abstraction at the C4 carbon atom of the cyclohexadiene ring, possibly by the proximal side chain of Lys-274, leading to the tautomer Schiff base followed by the removal of the second allylic hydrogen. The carboxyl tail of the amiclenomycin moiety forms a salt link to the conserved residue Arg-391 in the substrate-binding site. Modeling suggests steric hindrance at the active site as the determinant of the weak inhibiting potency of the trans isomer.
MeSH term(s)	Aminobutyrates/pharmacology ; Biotin/antagonists & inhibitors ; Biotin/biosynthesis ; Crystallography, X-Ray ; Escherichia coli/enzymology ; Kinetics ; Models, Molecular ; Molecular Conformation ; Transaminases/chemistry ; Transaminases/isolation & purification ; Transaminases/metabolism
Chemical Substances	Aminobutyrates ; amiclenomycin (53696-70-1) ; Biotin (6SO6U10H04) ; 7,8-diaminopelargonic acid aminotransferase (EC 2.6.1.-) ; Transaminases (EC 2.6.1.-)
Language	English
Publishing date	2002-09-05
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M207239200
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Escherichia coli biotin synthase produces selenobiotin. Further evidence of the involvement of the [2Fe-2S]2+ cluster in the sulfur insertion step.

Tse Sum Bui, Bernadette / Mattioli, Tony A / Florentin, Dominique / Bolbach, Gérard / Marquet, Andrée

Biochemistry

2006 Volume 45, Issue 11, Page(s) 3824–3834

Abstract: Biotin synthase, a member of the "radical SAM" family, catalyzes the final step of the biotin biosynthetic pathway, namely, the insertion of a sulfur atom into dethiobiotin. The as-isolated enzyme contains a [2Fe-2S](2+) cluster, but the active enzyme ... ...

Abstract	Biotin synthase, a member of the "radical SAM" family, catalyzes the final step of the biotin biosynthetic pathway, namely, the insertion of a sulfur atom into dethiobiotin. The as-isolated enzyme contains a [2Fe-2S](2+) cluster, but the active enzyme requires an additional [4Fe-4S](2+) cluster, which is formed in the presence of Fe(NH(4))(2)(SO(4))(2) and Na(2)S in the in vitro assay. The role of the [4Fe-4S](2+) cluster is to mediate the electron transfer to SAM, while the [2Fe-2S](2+) cluster is involved in the sulfur insertion step. To investigate the selenium version of the reaction, we have depleted the enzyme of its iron and sulfur and reconstituted the resulting apoprotein with FeCl(3) and Na(2)Se to yield a [2Fe-2Se](2+) cluster. This enzyme was assayed in vitro with Na(2)Se in place of Na(2)S to enable the formation of a [4Fe-4Se](2+) cluster. Selenobiotin was produced, but the activity was lower than that of the as-isolated [2Fe-2S](2+) enzyme in the presence of Na(2)S. The [2Fe-2Se](2+) enzyme was additionally assayed with Na(2)S, to reconstitute a [4Fe-4S](2+) cluster, in case the latter was more efficient than a [4Fe-4Se](2+) cluster for the electron transfer. Indeed, the activity was improved, but in that case, a mixture of biotin and selenobiotin was produced. This was unexpected if one considers the [2Fe-2S](2+) center as the sulfur source (either as the ultimate donor or via another intermediate), unless some exchange of the chalcogenide has taken place in the cluster. This latter point was seen in the resonance Raman spectrum of the reacted enzyme which clearly indicated the presence of both the [2Fe-2Se](2+) and [2Fe-2S](2+) clusters. No exchange was observed in the absence of reaction. These observations bring supplementary proof that the [2Fe-2S](2+) cluster is implicated in the sulfur insertion step.
MeSH term(s)	Biotin/analogs & derivatives ; Biotin/chemistry ; Biotin/metabolism ; Cell Fractionation ; Chalcogens/chemistry ; Chalcogens/metabolism ; Chromatography, High Pressure Liquid ; Enzyme Activation ; Escherichia coli Proteins/metabolism ; Iron/chemistry ; Iron/metabolism ; Organoselenium Compounds/chemistry ; Organoselenium Compounds/metabolism ; Selenium/chemistry ; Selenium/metabolism ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Spectrum Analysis, Raman ; Sulfides/chemistry ; Sulfides/metabolism ; Sulfur/chemistry ; Sulfur/metabolism ; Sulfurtransferases/chemistry ; Sulfurtransferases/metabolism
Chemical Substances	Chalcogens ; Escherichia coli Proteins ; Organoselenium Compounds ; Sulfides ; selenobiotin (57956-29-3) ; Biotin (6SO6U10H04) ; Sulfur (70FD1KFU70) ; Iron (E1UOL152H7) ; Sulfurtransferases (EC 2.8.1.-) ; biotin synthetase (EC 2.8.1.6) ; Selenium (H6241UJ22B) ; sodium sulfide (YGR27ZW0Y7)
Language	English
Publishing date	2006-03-21
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/bi052388m
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Elucidating biosynthetic pathways for vitamins and cofactors

Webb, Michael E. / Marquet, Andrée / Mendel, Ralf R. / Rébeillé, Fabrice / Smith, Alison G.

Natural product reports. 2007 Sept. 26, v. 24, no. 5

2007

Abstract	The elucidation of the pathways to the water-soluble vitamins and cofactors has provided many biochemical and chemical challenges. This is a reflection both of their complex chemical nature, and the fact that they are often made in small amounts, making detection of the enzyme activities and intermediates difficult. Here we present an orthogonal review of how these challenges have been overcome using a combination of methods, which are often ingenious. We make particular reference to some recent developments in the study of biotin, pantothenate, folate, pyridoxol, cobalamin, thiamine, riboflavin and molybdopterin biosynthesis.
Keywords	biosynthesis ; biotin ; enzymes ; folic acid ; riboflavin ; thiamin ; vitamin B12 ; water solubility
Language	English
Dates of publication	2007-0926
Size	p. 988-1008.
Publishing place	The Royal Society of Chemistry
Document type	Article
ZDB-ID	2002546-4
ISSN	1460-4752 ; 0265-0568
ISSN (online)	1460-4752
ISSN	0265-0568
DOI	10.1039/b703105j
Database	NAL-Catalogue (AGRICOLA)

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