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Article ; Online: Correction to Mitochondrial ADP/ATP Carrier: Preventing Conformational Changes by Point Mutations Inactivates Nucleotide Transport Activity.

Babot, Marion / Blancard, Corinne / Zeman, Igor / Lauquin, Guy J-M / Trézéguet, Véronique

2016 Volume 55, Issue 16, Page(s) 2422

Language	English
Publishing date	2016-04-26
Publishing country	United States
Document type	Journal Article
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/acs.biochem.6b00310
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Article ; Online: Mitochondrial ADP/ATP carrier: preventing conformational changes by point mutations inactivates nucleotide transport activity.

Babot, Marion / Blancard, Corinne / Zeman, Igor / Lauquin, Guy J-M / Trézéguet, Véronique

Biochemistry

2012 Volume 51, Issue 37, Page(s) 7348–7356

Abstract: The mitochondrial ADP/ATP carrier (Ancp) is a paradigm of the mitochondrial carrier family (MCF); its members allow metabolic fluxes between mitochondria and the cytosol. The members of the MCF share numerous structural and functional characteristics. ... ...

Abstract	The mitochondrial ADP/ATP carrier (Ancp) is a paradigm of the mitochondrial carrier family (MCF); its members allow metabolic fluxes between mitochondria and the cytosol. The members of the MCF share numerous structural and functional characteristics. Ancp is very specifically inhibited by two classes of compounds, which stabilize the carrier in two different conformations involved in nucleotide transport. Resolution of the atomic structure of the bovine Ancp, in complex with one of its specific inhibitors, is that of the carrier open toward the intermembrane space. To gain insights into the interconversion from one conformation to the other, we introduced point mutations in the yeast carrier at positions Cys73 in the first matrix loop and Tyr97 and Gly298 in transmembrane helices 2 and 6. We demonstrate in this paper that they impair stabilization of the carrier in one conformation or the other, resulting in an almost complete inactivation of nucleotide transport in both cases. The results are discussed on the basis of the atomic structure of the conformation open to the cytosol. These mutant proteins could afford convenient tools for undertaking structural studies of both conformations of the yeast carrier.
MeSH term(s)	Animals ; Biological Transport/genetics ; Cattle ; Crystallography, X-Ray ; Mitochondrial ADP, ATP Translocases/chemistry ; Mitochondrial ADP, ATP Translocases/genetics ; Mitochondrial ADP, ATP Translocases/metabolism ; Point Mutation ; Protein Stability ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae Proteins/chemistry ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Structure-Activity Relationship
Chemical Substances	Saccharomyces cerevisiae Proteins ; Mitochondrial ADP, ATP Translocases (9068-80-8)
Language	English
Publishing date	2012-09-18
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/bi300978z
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Article ; Online: The transmembrane prolines of the mitochondrial ADP/ATP carrier are involved in nucleotide binding and transport and its biogenesis.

Babot, Marion / Blancard, Corinne / Pelosi, Ludovic / Lauquin, Guy J-M / Trézéguet, Véronique

The Journal of biological chemistry

2012 Volume 287, Issue 13, Page(s) 10368–10378

Abstract: The mitochondrial ADP/ATP carrier (Ancp) is a paradigm of the mitochondrial carrier family, which allows cross-talk between mitochondria, where cell energy is mainly produced, and cytosol, where cell energy is mainly consumed. The members of this family ... ...

Abstract	The mitochondrial ADP/ATP carrier (Ancp) is a paradigm of the mitochondrial carrier family, which allows cross-talk between mitochondria, where cell energy is mainly produced, and cytosol, where cell energy is mainly consumed. The members of this family share numerous structural and functional characteristics. Resolution of the atomic structure of the bovine Ancp, in a complex with one of its specific inhibitors, revealed interesting features and suggested the involvement of some particular residues in the movements of the protein to perform translocation of nucleotides from one side of the membrane to the other. They correspond to three prolines located in the odd-numbered transmembrane helices (TMH), Pro-27, Pro-132, and Pro-229. The corresponding residues of the yeast Ancp (Pro-43, Ser-147, and Pro-247) were mutated into alanine or leucine, one at a time and analysis of the various mutants evidenced a crucial role of Pro-43 and Pro-247 during nucleotide transport. Beside, replacement of Ser-147 with proline does not inactivate Ancp and this is discussed in view of the conservation of the three prolines at equivalent positions in the Ancp sequences. These prolines belong to the signature sequences of the mitochondrial carriers and we propose they play a dual role in the mitochondrial ADP/ATP carrier function and biogenesis. Unexpectedly their mutations cause more general effects on mitochondrial biogenesis and morphology, as evidenced by measurements of respiratory rates, cytochrome contents, and also clearly highlighted by fluorescence microscopy.
MeSH term(s)	Amino Acid Substitution ; Animals ; Biological Transport ; Cattle ; Mitochondrial ADP, ATP Translocases/chemistry ; Mitochondrial ADP, ATP Translocases/genetics ; Mitochondrial ADP, ATP Translocases/metabolism ; Mutation, Missense ; Proline/chemistry ; Proline/genetics ; Proline/metabolism ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Saccharomyces cerevisiae/chemistry ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/chemistry ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism
Chemical Substances	Saccharomyces cerevisiae Proteins ; Mitochondrial ADP, ATP Translocases (9068-80-8) ; Proline (9DLQ4CIU6V)
Language	English
Publishing date	2012-02-09
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.M111.320697
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Article: Mitochondrial ADP/ATP Carrier: Preventing Conformational Changes by Point Mutations Inactivates Nucleotide Transport Activity

Babot, Marion / Blancard Corinne / Zeman Igor / Lauquin Guy J.-M / TreÌzeÌguet VeÌronique

Biochemistry. 2012 Sept. 18, v. 51, no. 37

2012

Abstract	The mitochondrial ADP/ATP carrier (Ancp) is a paradigm of the mitochondrial carrier family (MCF); its members allow metabolic fluxes between mitochondria and the cytosol. The members of the MCF share numerous structural and functional characteristics. Ancp is very specifically inhibited by two classes of compounds, which stabilize the carrier in two different conformations involved in nucleotide transport. Resolution of the atomic structure of the bovine Ancp, in complex with one of its specific inhibitors, is that of the carrier open toward the intermembrane space. To gain insights into the interconversion from one conformation to the other, we introduced point mutations in the yeast carrier at positions Cys73 in the first matrix loop and Tyr97 and Gly298 in transmembrane helices 2 and 6. We demonstrate in this paper that they impair stabilization of the carrier in one conformation or the other, resulting in an almost complete inactivation of nucleotide transport in both cases. The results are discussed on the basis of the atomic structure of the conformation open to the cytosol. These mutant proteins could afford convenient tools for undertaking structural studies of both conformations of the yeast carrier.
Keywords	adenosine diphosphate ; adenosine triphosphate ; cattle ; cytosol ; functional properties ; mitochondria ; mutants ; physiological transport ; point mutation ; transport proteins ; yeasts
Language	English
Dates of publication	2012-0918
Size	p. 7348-7356.
Publishing place	American Chemical Society
Document type	Article
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021%2Fbi300978z
Database	NAL-Catalogue (AGRICOLA)

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Article: Unambiguous structure of atractyloside and carboxyatractyloside

Sanchez, Jean-Frédéric / Kauffmann, Brice / Grélard, Axelle / Sanchez, Corinne / Trézéguet, Véronique / Huc, Ivan / Lauquin, Guy J.-M

Bioorganic & medicinal chemistry letters. 2012 Apr. 15, v. 22, no. 8

2012

Abstract: Atractyloside (ATR) was characterized in 1868 and until now structural studies on diterpenic moiety had been done through the characterization of ATR derivatives; while the glycosidic moiety seemed to be a β-d-glucopyranose a recent crystal structure of ... ...

Abstract	Atractyloside (ATR) was characterized in 1868 and until now structural studies on diterpenic moiety had been done through the characterization of ATR derivatives; while the glycosidic moiety seemed to be a β-d-glucopyranose a recent crystal structure of the mitochondrial ATP/ADP carrier in complex with CATR showed an α-d-glucopyranose. We decided to re-examine the ATR and CATR structures by crystallographic study of ATR.
Keywords	adenosine diphosphate ; adenosine triphosphate ; crystal structure
Language	English
Dates of publication	2012-0415
Size	p. 2973-2975.
Publishing place	Elsevier Ltd
Document type	Article
ZDB-ID	1063195-1
ISSN	1464-3405 ; 0960-894X
ISSN (online)	1464-3405
ISSN	0960-894X
DOI	10.1016/j.bmcl.2012.02.040
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Article: The mitochondrial ADP/ATP carrier: functional and structural studies in the route of elucidating pathophysiological aspects.

Trézéguet, Véronique / Pélosi, Ludovic / Lauquin, Guy J M / Brandolin, Gérard

Journal of bioenergetics and biomembranes

2008 Volume 40, Issue 5, Page(s) 435–443

Abstract: The mitochondrial ADP/ATP carrier plays a central role in aerobic cell energetics by providing to the cytosol the ATP generated by oxidative phosphorylation. Though discovered around 40 years ago owing to the existence of unique inhibitors and in spite ... ...

Abstract	The mitochondrial ADP/ATP carrier plays a central role in aerobic cell energetics by providing to the cytosol the ATP generated by oxidative phosphorylation. Though discovered around 40 years ago owing to the existence of unique inhibitors and in spite of numerous experimental approaches, this carrier, which stands as a model of the mitochondrial solute carriers keeps some long-standing mystery. There are still open challenging questions among them the precise ADP/ATP transport mechanism, the functional oligomeric state of the carrier and relationships between human ADP/ATP carrier dysfunctioning and pathologies. Deciphering the 3D structure of this carrier afforded a considerable progress of the knowledge but requires now additional data focused on molecular dynamics from this static picture. State of the art in this topic is reviewed and debated in this paper in view of better comprehending origin of the discrepancies in these questions and, finally, the multiple physiological roles of this carrier in eukaryotic cell economy.
MeSH term(s)	Animals ; Conserved Sequence ; Evolution, Molecular ; Humans ; Mitochondria/enzymology ; Mitochondria/genetics ; Mitochondrial ADP, ATP Translocases/chemistry ; Mitochondrial ADP, ATP Translocases/deficiency ; Mitochondrial ADP, ATP Translocases/genetics ; Mitochondrial ADP, ATP Translocases/physiology ; Mitochondrial Diseases/enzymology ; Mitochondrial Diseases/genetics ; Models, Molecular ; Mutation ; Oxidative Phosphorylation ; Protein Structure, Quaternary
Chemical Substances	Mitochondrial ADP, ATP Translocases (9068-80-8)
Language	English
Publishing date	2008-11-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	198499-8
ISSN	1573-6881 ; 0145-479X ; 0449-5705
ISSN (online)	1573-6881
ISSN	0145-479X ; 0449-5705
DOI	10.1007/s10863-008-9178-2
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Article ; Online: Native membrane proteins vs. yeast recombinant: an example: the mitochondrial ADP/ATP carrier.

Arnou, Bertrand / Dahout-Gonzalez, Cécile / Pelosi, Ludovic / Lauquin, Guy J-M / Brandolin, Gérard / Trézéguet, Véronique

Methods in molecular biology (Clifton, N.J.)

2010 Volume 654, Page(s) 19–28

Abstract: The mitochondrial ADP/ATP carrier (Ancp) has long been a paradigm for studies of the mitochondrial carrier family due to, among other properties, its natural abundance and the existence of specific inhibitors, namely, carboxyatractyloside (CATR) and ... ...

Abstract	The mitochondrial ADP/ATP carrier (Ancp) has long been a paradigm for studies of the mitochondrial carrier family due to, among other properties, its natural abundance and the existence of specific inhibitors, namely, carboxyatractyloside (CATR) and bongkrekic acid (BA), which lock the carrier under distinct and stable conformations. Bovine Anc1p isolated in complex with CATR in the presence of an aminoxyde detergent (LAPAO) was crystallized and its 3D structure determined. It is the first mitochondrial carrier structure resolved at high resolution (2.2 A, as reported by Pebay-Peyroula et al. (Nature 426:39-44, 2003)). Analyses revealed a monomer while most of the biochemical studies led to hypothesize Ancp functions as a dimer. To address the structural organization issue, we engineered a mutant of the yeast Ancp that corresponds to a covalent homodimer in view of 3D structure determination. We compare in this chapter the purification yield and quality of the chimera tagged either with six histidines at its C-ter end or nine histidines at its N-ter. We show that, as expected, length and position of the tag are important criteria for qualitative purification. We also discuss the advantages and drawbacks of purifying Ancp either from a natural source or from engineered yeast cells.
MeSH term(s)	Animals ; Atractyloside/analogs & derivatives ; Atractyloside/chemistry ; Atractyloside/pharmacology ; Bongkrekic Acid/chemistry ; Bongkrekic Acid/pharmacology ; Cattle ; Membrane Proteins/antagonists & inhibitors ; Membrane Proteins/chemistry ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Mitochondrial ADP, ATP Translocases/antagonists & inhibitors ; Mitochondrial ADP, ATP Translocases/chemistry ; Mitochondrial ADP, ATP Translocases/genetics ; Mitochondrial ADP, ATP Translocases/metabolism ; Recombinant Proteins/antagonists & inhibitors ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism
Chemical Substances	Membrane Proteins ; Recombinant Proteins ; Bongkrekic Acid (11076-19-0) ; Atractyloside (17754-44-8) ; Mitochondrial ADP, ATP Translocases (9068-80-8) ; carboxyatractyloside (SNP1XL23E6)
Language	English
Publishing date	2010
Publishing country	United States
Document type	Journal Article
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-60761-762-4_2
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Article: The mitochondrial ADP/ATP carrier: functional and structural studies in the route of elucidating pathophysiological aspects

Trézéguet, Véronique / Pélosi, Ludovic / Lauquin, Guy J. M / Brandolin, Gérard

Journal of bioenergetics and biomembranes. 2008 Oct., v. 40, no. 5

2008

Abstract	The mitochondrial ADP/ATP carrier plays a central role in aerobic cell energetics by providing to the cytosol the ATP generated by oxidative phosphorylation. Though discovered around 40 years ago owing to the existence of unique inhibitors and in spite of numerous experimental approaches, this carrier, which stands as a model of the mitochondrial solute carriers keeps some long-standing mystery. There are still open challenging questions among them the precise ADP/ATP transport mechanism, the functional oligomeric state of the carrier and relationships between human ADP/ATP carrier dysfunctioning and pathologies. Deciphering the 3D structure of this carrier afforded a considerable progress of the knowledge but requires now additional data focused on molecular dynamics from this static picture. State of the art in this topic is reviewed and debated in this paper in view of better comprehending origin of the discrepancies in these questions and, finally, the multiple physiological roles of this carrier in eukaryotic cell economy.
Keywords	mitochondria ; pathophysiology
Language	English
Dates of publication	2008-10
Size	p. 435-443.
Publisher	Springer US
Publishing place	Boston
Document type	Article
ZDB-ID	198499-8
ISSN	1573-6881 ; 0145-479X ; 0449-5705
ISSN (online)	1573-6881
ISSN	0145-479X ; 0449-5705
DOI	10.1007/s10863-008-9178-2
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Unambiguous structure of atractyloside and carboxyatractyloside.

Sanchez, Jean-Frédéric / Kauffmann, Brice / Grélard, Axelle / Sanchez, Corinne / Trézéguet, Véronique / Huc, Ivan / Lauquin, Guy J-M

Bioorganic & medicinal chemistry letters

2012 Volume 22, Issue 8, Page(s) 2973–2975

Abstract: Atractyloside (ATR) was characterized in 1868 and until now structural studies on diterpenic moiety had been done through the characterization of ATR derivatives; while the glycosidic moiety seemed to be a β-D-glucopyranose a recent crystal structure of ... ...

Abstract	Atractyloside (ATR) was characterized in 1868 and until now structural studies on diterpenic moiety had been done through the characterization of ATR derivatives; while the glycosidic moiety seemed to be a β-D-glucopyranose a recent crystal structure of the mitochondrial ATP/ADP carrier in complex with CATR showed an α-D-glucopyranose. We decided to re-examine the ATR and CATR structures by crystallographic study of ATR.
MeSH term(s)	Atractyloside/analogs & derivatives ; Atractyloside/chemistry ; Crystallography, X-Ray ; Models, Molecular ; Multiprotein Complexes/chemistry
Chemical Substances	Multiprotein Complexes ; Atractyloside (17754-44-8) ; carboxyatractyloside (SNP1XL23E6)
Language	English
Publishing date	2012-04-15
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1063195-1
ISSN	1464-3405 ; 0960-894X
ISSN (online)	1464-3405
ISSN	0960-894X
DOI	10.1016/j.bmcl.2012.02.040
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Structure-Function Relationships of the C-Terminal End of the Saccharomyces cerevisiae ADP/ATP Carrier Isoform 2

Clémençon, Benjamin / Rey, Martial / Dianoux, Anne-Christine / Trézéguet, Véronique / Lauquin, Guy J.-M / Brandolin, Gérard / Pelosi, Ludovic

Journal of biological chemistry. 2008 Apr. 25, v. 283, no. 17

2008

Abstract: The adenine nucleotide carrier (Ancp) catalyzes the transport of ADP and ATP across the mitochondrial inner membrane, thus playing an essential role in the cellular energy metabolism. Two regions of Anc2p from Saccharomyces cerevisiae are specifically ... ...

Abstract	The adenine nucleotide carrier (Ancp) catalyzes the transport of ADP and ATP across the mitochondrial inner membrane, thus playing an essential role in the cellular energy metabolism. Two regions of Anc2p from Saccharomyces cerevisiae are specifically photolabeled using a photoactivable ADP derivative; they are the central matrix loop, m2, and the C-terminal end. To get more insights into the structure-function relationships of the C-terminal region during nucleotide transport, we have developed two independent approaches. In the first we have deleted the last eight amino acids of Anc2p (Anc2pΔCter) and demonstrated that the C-terminal end of Anc2p plays an essential role in yeast growth on a non-fermentable carbon source. This resulted from impaired nucleotide binding properties of the Anc2pΔCter variant in line with conversion of ADP binding sites from high to low affinity. In the second we probed the ligand-induced conformational changes of Anc2p C-terminal end (i) by assessing its accessibility to anti-C-terminal antibodies and (ii) by measuring intrinsic fluorescence changes of an Anc2p mutant containing only one tryptophan residue located at its C-terminal end (Anc2p3Y-u). We show that the C-terminal region is no further accessible to antibodies when Anc2p binds non-transportable analogues of ADP. Besides, Trp-316 fluorescence is highly increased upon ligand binding, suggesting large conformational changes. Taken together, our results highlight the involvement of the Anc2p C-terminal region in nucleotide recognition, binding, and transport.
Language	English
Dates of publication	2008-0425
Size	p. 11218-11225.
Publishing place	American Society for Biochemistry and Molecular Biology
Document type	Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
Database	NAL-Catalogue (AGRICOLA)

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