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Article ; Online: A moonlighting role for LysM peptidoglycan binding domains underpins Enterococcus faecalis daughter cell separation.

Salamaga, Bartłomiej / Turner, Robert D / Elsarmane, Fathe / Galley, Nicola F / Kulakauskas, Saulius / Mesnage, Stéphane

Communications biology

2023 Volume 6, Issue 1, Page(s) 428

Abstract: Control of cell size and morphology is of paramount importance for bacterial fitness. In the opportunistic pathogen Enterococcus faecalis, the formation of diplococci and short cell chains facilitates innate immune evasion and dissemination in the host. ... ...

Abstract	Control of cell size and morphology is of paramount importance for bacterial fitness. In the opportunistic pathogen Enterococcus faecalis, the formation of diplococci and short cell chains facilitates innate immune evasion and dissemination in the host. Minimisation of cell chain size relies on the activity of a peptidoglycan hydrolase called AtlA, dedicated to septum cleavage. To prevent autolysis, AtlA activity is tightly controlled, both temporally and spatially. Here, we show that the restricted localization of AtlA at the septum occurs via an unexpected mechanism. We demonstrate that the C-terminal LysM domain that allows the enzyme to bind peptidoglycan is essential to target this enzyme to the septum inside the cell before its translocation across the membrane. We identify a membrane-bound cytoplasmic protein partner (called AdmA) involved in the recruitment of AtlA via its LysM domains. This work reveals a moonlighting role for LysM domains, and a mechanism evolved to restrict the subcellular localization of a potentially lethal autolysin to its site of action.
MeSH term(s)	Enterococcus faecalis/metabolism ; Peptidoglycan/metabolism ; Bacterial Proteins/metabolism ; Cell Wall/metabolism ; N-Acetylmuramoyl-L-alanine Amidase/genetics ; N-Acetylmuramoyl-L-alanine Amidase/metabolism ; Cell Separation
Chemical Substances	Peptidoglycan ; Bacterial Proteins ; N-Acetylmuramoyl-L-alanine Amidase (EC 3.5.1.28)
Language	English
Publishing date	2023-04-18
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2399-3642
ISSN (online)	2399-3642
DOI	10.1038/s42003-023-04808-z
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Clostridioides difficile canonical L,D-transpeptidases catalyze a novel type of peptidoglycan cross-links and are not required for beta-lactam resistance.

Galley, Nicola F / Greetham, Darren / Alamán-Zárate, Marcel G / Williamson, Mike P / Evans, Caroline A / Spittal, William D / Buddle, Jessica E / Freeman, Jane / Davis, Georgina L / Dickman, Mark J / Wilcox, Mark H / Lovering, Andrew L / Fagan, Robert P / Mesnage, Stéphane

The Journal of biological chemistry

2023 Volume 300, Issue 1, Page(s) 105529

Abstract: Clostridioides difficile is the leading cause of antibiotic-associated diarrhea worldwide with significant morbidity and mortality. This organism is naturally resistant to several beta-lactam antibiotics that inhibit the polymerization of peptidoglycan, ... ...

Abstract	Clostridioides difficile is the leading cause of antibiotic-associated diarrhea worldwide with significant morbidity and mortality. This organism is naturally resistant to several beta-lactam antibiotics that inhibit the polymerization of peptidoglycan, an essential component of the bacteria cell envelope. Previous work has revealed that C. difficile peptidoglycan has an unusual composition. It mostly contains 3-3 cross-links, catalyzed by enzymes called L,D-transpeptidases (Ldts) that are poorly inhibited by beta-lactams. It was therefore hypothesized that peptidoglycan polymerization by these enzymes could underpin antibiotic resistance. Here, we investigated the catalytic activity of the three canonical Ldts encoded by C. difficile (Ldt
MeSH term(s)	Bacterial Proteins/chemistry ; beta-Lactam Resistance ; beta-Lactams/pharmacology ; Catalysis ; Clostridioides difficile/enzymology ; Clostridioides difficile/genetics ; Peptidoglycan/chemistry ; Peptidyl Transferases/chemistry ; Peptidyl Transferases/genetics
Chemical Substances	Bacterial Proteins ; beta-Lactams ; Peptidoglycan ; Peptidyl Transferases (EC 2.3.2.12)
Language	English
Publishing date	2023-12-01
Publishing country	United States
Document type	Journal Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2023.105529
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Article ; Online: Molecular basis for substrate recognition and septum cleavage by AtlA, the major N-acetylglucosaminidase of Enterococcus faecalis.

Roig-Zamboni, Véronique / Barelier, Sarah / Dixon, Robert / Galley, Nicola F / Ghanem, Amani / Nguyen, Quoc Phong / Cahuzac, Héloize / Salamaga, Bartłomiej / Davis, Peter J / Bourne, Yves / Mesnage, Stéphane / Vincent, Florence

The Journal of biological chemistry

2022 Volume 298, Issue 5, Page(s) 101915

Abstract: The cleavage of septal peptidoglycan at the end of cell division facilitates the separation of the two daughter cells. The hydrolases involved in this process (called autolysins) are potentially lethal enzymes that can cause cell death; their activity, ... ...

Abstract	The cleavage of septal peptidoglycan at the end of cell division facilitates the separation of the two daughter cells. The hydrolases involved in this process (called autolysins) are potentially lethal enzymes that can cause cell death; their activity, therefore, must be tightly controlled during cell growth. In Enterococcus faecalis, the N-acetylglucosaminidase AtlA plays a predominant role in cell separation. atlA mutants form long cell chains and are significantly less virulent in the zebrafish model of infection. The attenuated virulence of atlA mutants is underpinned by a limited dissemination of bacterial chains in the host organism and a more efficient uptake by phagocytes that clear the infection. AtlA has structural homologs in other important pathogens, such as Listeria monocytogenes and Salmonella typhimurium, and therefore represents an attractive model to design new inhibitors of bacterial pathogenesis. Here, we provide a 1.45 Å crystal structure of the E. faecalis AtlA catalytic domain that reveals a closed conformation of a conserved β-hairpin and a complex network of hydrogen bonds that bring two catalytic residues to the ideal distance for an inverting mechanism. Based on the model of the AtlA-substrate complex, we identify key residues critical for substrate recognition and septum cleavage during bacterial growth. We propose that this work will provide useful information for the rational design of specific inhibitors targeting this enterococcal virulence factor and its orthologs in other pathogens.
MeSH term(s)	Acetylglucosaminidase/chemistry ; Animals ; Bacterial Proteins/metabolism ; Enterococcus faecalis/enzymology ; Enterococcus faecalis/metabolism ; Peptidoglycan/metabolism ; Zebrafish/metabolism
Chemical Substances	Bacterial Proteins ; Peptidoglycan ; Acetylglucosaminidase (EC 3.2.1.52)
Language	English
Publishing date	2022-04-07
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	10.1016/j.jbc.2022.101915
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Article ; Online: Prospects for novel inhibitors of peptidoglycan transglycosylases.

Galley, Nicola F / O'Reilly, Amy M / Roper, David I

Bioorganic chemistry

2014 Volume 55, Page(s) 16–26

Abstract: The lack of novel antimicrobial drugs under development coupled with the increasing occurrence of resistance to existing antibiotics by community and hospital acquired infections is of grave concern. The targeting of biosynthesis of the peptidoglycan ... ...

Abstract	The lack of novel antimicrobial drugs under development coupled with the increasing occurrence of resistance to existing antibiotics by community and hospital acquired infections is of grave concern. The targeting of biosynthesis of the peptidoglycan component of the bacterial cell wall has proven to be clinically valuable but relatively little therapeutic development has been directed towards the transglycosylase step of this process. Advances towards the isolation of new antimicrobials that target transglycosylase activity will rely on the development of the enzymological tools required to identify and characterise novel inhibitors of these enzymes. Therefore, in this article, we review the assay methods developed for transglycosylases and review recent novel chemical inhibitors discovered in relation to both the lipidic substrates and natural product inhibitors of the transglycosylase step.
MeSH term(s)	Animals ; Enzyme Inhibitors/pharmacology ; Humans ; Peptidoglycan/biosynthesis ; Peptidoglycan/chemistry ; Peptidoglycan Glycosyltransferase/antagonists & inhibitors
Chemical Substances	Enzyme Inhibitors ; Peptidoglycan ; Peptidoglycan Glycosyltransferase (EC 2.4.1.129)
Language	English
Publishing date	2014-05-21
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	120080-x
ISSN	1090-2120 ; 0045-2068
ISSN (online)	1090-2120
ISSN	0045-2068
DOI	10.1016/j.bioorg.2014.05.007
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Article ; Online: Substrate and Stereochemical Control of Peptidoglycan Cross-Linking by Transpeptidation by

Catherwood, Anita C / Lloyd, Adrian J / Tod, Julie A / Chauhan, Smita / Slade, Susan E / Walkowiak, Grzegorz P / Galley, Nicola F / Punekar, Avinash S / Smart, Katie / Rea, Dean / Evans, Neil D / Chappell, Michael J / Roper, David I / Dowson, Christopher G

Journal of the American Chemical Society

2020 Volume 142, Issue 11, Page(s) 5034–5048

Abstract: Penicillin binding proteins (PBPs) catalyzing transpeptidation reactions that stabilize the peptidoglycan component of the bacterial cell wall are the targets of β-lactams, the most clinically successful antibiotics to date. However, PBP-transpeptidation ...

Abstract	Penicillin binding proteins (PBPs) catalyzing transpeptidation reactions that stabilize the peptidoglycan component of the bacterial cell wall are the targets of β-lactams, the most clinically successful antibiotics to date. However, PBP-transpeptidation enzymology has evaded detailed analysis, because of the historical unavailability of kinetically competent assays with physiologically relevant substrates and the previously unappreciated contribution of protein cofactors to PBP activity. By re-engineering peptidoglycan synthesis, we have constructed a continuous spectrophotometric assay for transpeptidation of native or near native peptidoglycan precursors and fragments by
MeSH term(s)	Bacterial Outer Membrane Proteins/chemistry ; Biocatalysis ; Enzyme Assays/methods ; Escherichia coli/enzymology ; Escherichia coli Proteins/chemistry ; Kinetics ; Penicillin-Binding Proteins/chemistry ; Peptidoglycan/chemistry ; Peptidoglycan Glycosyltransferase/chemistry ; Polyisoprenyl Phosphate Monosaccharides/chemistry ; Polyisoprenyl Phosphate Oligosaccharides/chemistry ; Serine-Type D-Ala-D-Ala Carboxypeptidase/chemistry ; Stereoisomerism ; Substrate Specificity
Chemical Substances	Bacterial Outer Membrane Proteins ; Escherichia coli Proteins ; LpoB protein, E coli ; Penicillin-Binding Proteins ; Peptidoglycan ; Polyisoprenyl Phosphate Monosaccharides ; Polyisoprenyl Phosphate Oligosaccharides ; Peptidoglycan Glycosyltransferase (EC 2.4.1.129) ; penicillin-binding protein 1B, E coli (EC 2.4.1.129) ; Serine-Type D-Ala-D-Ala Carboxypeptidase (EC 3.4.16.4)
Language	English
Publishing date	2020-03-02
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	3155-0
ISSN	1520-5126 ; 0002-7863
ISSN (online)	1520-5126
ISSN	0002-7863
DOI	10.1021/jacs.9b08822
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Article: Substrate and Stereochemical Control of Peptidoglycan Cross-Linking by Transpeptidation by Escherichia coli PBP1B

Journal of the American Chemical Society. 2020 Feb. 12, v. 142, no. 11

2020

Abstract	Penicillin binding proteins (PBPs) catalyzing transpeptidation reactions that stabilize the peptidoglycan component of the bacterial cell wall are the targets of β-lactams, the most clinically successful antibiotics to date. However, PBP-transpeptidation enzymology has evaded detailed analysis, because of the historical unavailability of kinetically competent assays with physiologically relevant substrates and the previously unappreciated contribution of protein cofactors to PBP activity. By re-engineering peptidoglycan synthesis, we have constructed a continuous spectrophotometric assay for transpeptidation of native or near native peptidoglycan precursors and fragments by Escherichia coli PBP1B, allowing us to (a) identify recognition elements of transpeptidase substrates, (b) reveal a novel mechanism of stereochemical editing within peptidoglycan transpeptidation, (c) assess the impact of peptidoglycan substrates on β-lactam targeting of transpeptidation, and (d) demonstrate that both substrates have to be bound before transpeptidation occurs. The results allow characterization of high molecular weight PBPs as enzymes and not merely the targets of β-lactam acylation.
Keywords	Escherichia coli ; acylation ; bacteria ; binding proteins ; cell walls ; crosslinking ; enzyme substrates ; enzymes ; molecular weight ; penicillins ; peptidoglycans ; stereochemistry
Language	English
Dates of publication	2020-0212
Size	p. 5034-5048.
Publishing place	American Chemical Society
Document type	Article
ZDB-ID	3155-0
ISSN	1520-5126 ; 0002-7863
ISSN (online)	1520-5126
ISSN	0002-7863
DOI	10.1021/jacs.9b08822
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Article ; Online: In vitro characterization of the antivirulence target of Gram-positive pathogens, peptidoglycan O-acetyltransferase A (OatA).

Sychantha, David / Jones, Carys S / Little, Dustin J / Moynihan, Patrick J / Robinson, Howard / Galley, Nicola F / Roper, David I / Dowson, Christopher G / Howell, P Lynne / Clarke, Anthony J

PLoS pathogens

2017 Volume 13, Issue 10, Page(s) e1006667

Abstract: The O-acetylation of the essential cell wall polymer peptidoglycan occurs in most Gram-positive bacterial pathogens, including species of Staphylococcus, Streptococcus and Enterococcus. This modification to peptidoglycan protects these pathogens from the ...

Abstract	The O-acetylation of the essential cell wall polymer peptidoglycan occurs in most Gram-positive bacterial pathogens, including species of Staphylococcus, Streptococcus and Enterococcus. This modification to peptidoglycan protects these pathogens from the lytic action of the lysozymes of innate immunity systems and, as such, is recognized as a virulence factor. The key enzyme involved, peptidoglycan O-acetyltransferase A (OatA) represents a particular challenge to biochemical study since it is a membrane associated protein whose substrate is the insoluble peptidoglycan cell wall polymer. OatA is predicted to be bimodular, being comprised of an N-terminal integral membrane domain linked to a C-terminal extracytoplasmic domain. We present herein the first biochemical and kinetic characterization of the C-terminal catalytic domain of OatA from two important human pathogens, Staphylococcus aureus and Streptococcus pneumoniae. Using both pseudosubstrates and novel biosynthetically-prepared peptidoglycan polymers, we characterized distinct substrate specificities for the two enzymes. In addition, the high resolution crystal structure of the C-terminal domain reveals an SGNH/GDSL-like hydrolase fold with a catalytic triad of amino acids but with a non-canonical oxyanion hole structure. Site-specific replacements confirmed the identity of the catalytic and oxyanion hole residues. A model is presented for the O-acetylation of peptidoglycan whereby the translocation of acetyl groups from a cytoplasmic source across the cytoplasmic membrane is catalyzed by the N-terminal domain of OatA for their transfer to peptidoglycan by its C-terminal domain. This study on the structure-function relationship of OatA provides a molecular and mechanistic understanding of this bacterial resistance mechanism opening the prospect for novel chemotherapeutic exploration to enhance innate immunity protection against Gram-positive pathogens.
MeSH term(s)	Acetyltransferases/metabolism ; Bacterial Proteins/metabolism ; Cell Wall/metabolism ; Drug Resistance ; Gram-Positive Bacteria/metabolism ; Humans ; Peptidoglycan/metabolism ; Peptidoglycan/pharmacology ; Staphylococcus aureus/drug effects ; Staphylococcus aureus/pathogenicity ; Substrate Specificity/immunology ; Virulence ; Virulence Factors/metabolism
Chemical Substances	Bacterial Proteins ; Peptidoglycan ; Virulence Factors ; Acetyltransferases (EC 2.3.1.-)
Language	English
Publishing date	2017-10-27
Publishing country	United States
Document type	Journal Article
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7374
ISSN (online)	1553-7374
ISSN	1553-7374
DOI	10.1371/journal.ppat.1006667
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Article ; Online: Surfactant-free purification of membrane protein complexes from bacteria: application to the staphylococcal penicillin-binding protein complex PBP2/PBP2a.

Paulin, Sarah / Jamshad, Mohammed / Dafforn, Timothy R / Garcia-Lara, Jorge / Foster, Simon J / Galley, Nicola F / Roper, David I / Rosado, Helena / Taylor, Peter W

Nanotechnology

2014 Volume 25, Issue 28, Page(s) 285101

Abstract: Surfactant-mediated removal of proteins from biomembranes invariably results in partial or complete loss of function and disassembly of multi-protein complexes. We determined the capacity of styrene-co-maleic acid (SMA) co-polymer to remove components of ...

Abstract	Surfactant-mediated removal of proteins from biomembranes invariably results in partial or complete loss of function and disassembly of multi-protein complexes. We determined the capacity of styrene-co-maleic acid (SMA) co-polymer to remove components of the cell division machinery from the membrane of drug-resistant staphylococcal cells. SMA-lipid nanoparticles solubilized FtsZ-PBP2-PBP2a complexes from intact cells, demonstrating the close physical proximity of these proteins within the lipid bilayer. Exposure of bacteria to (-)-epicatechin gallate, a polyphenolic agent that abolishes β-lactam resistance in staphylococci, disrupted the association between PBP2 and PBP2a. Thus, SMA purification provides a means to remove native integral membrane protein assemblages with minimal physical disruption and shows promise as a tool for the interrogation of molecular aspects of bacterial membrane protein structure and function.
MeSH term(s)	Bacterial Proteins/chemistry ; Catechin/analogs & derivatives ; Catechin/chemistry ; Cell Division/physiology ; Lipid Bilayers/chemistry ; Maleates/chemistry ; Membrane Proteins/chemistry ; Penicillin-Binding Proteins/chemistry ; Peptide Synthases/chemistry ; Polystyrenes/chemistry ; Staphylococcus aureus/chemistry ; Surface-Active Agents/chemistry
Chemical Substances	Bacterial Proteins ; Lipid Bilayers ; Maleates ; Membrane Proteins ; Penicillin-Binding Proteins ; Polystyrenes ; Surface-Active Agents ; penicillin-binding protein 2a, Streptococcus ; styrene-maleic acid polymer (25300-64-5) ; Catechin (8R1V1STN48) ; epicatechin gallate (92587OVD8Z) ; Peptide Synthases (EC 6.3.2.-)
Language	English
Publishing date	2014-06-27
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1362365-5
ISSN	1361-6528 ; 0957-4484
ISSN (online)	1361-6528
ISSN	0957-4484
DOI	10.1088/0957-4484/25/28/285101
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Article ; Online: Carbohydrate scaffolds as glycosyltransferase inhibitors with in vivo antibacterial activity.

Zuegg, Johannes / Muldoon, Craig / Adamson, George / McKeveney, Declan / Le Thanh, Giang / Premraj, Rajaratnam / Becker, Bernd / Cheng, Mu / Elliott, Alysha G / Huang, Johnny X / Butler, Mark S / Bajaj, Megha / Seifert, Joachim / Singh, Latika / Galley, Nicola F / Roper, David I / Lloyd, Adrian J / Dowson, Christopher G / Cheng, Ting-Jen /

Cheng, Wei-Chieh / Demon, Dieter / Meyer, Evelyne / Meutermans, Wim / Cooper, Matthew A

Nature communications

2015 Volume 6, Page(s) 7719

Abstract: The rapid rise of multi-drug-resistant bacteria is a global healthcare crisis, and new antibiotics are urgently required, especially those with modes of action that have low-resistance potential. One promising lead is the liposaccharide antibiotic ... ...

Abstract	The rapid rise of multi-drug-resistant bacteria is a global healthcare crisis, and new antibiotics are urgently required, especially those with modes of action that have low-resistance potential. One promising lead is the liposaccharide antibiotic moenomycin that inhibits bacterial glycosyltransferases, which are essential for peptidoglycan polymerization, while displaying a low rate of resistance. Unfortunately, the lipophilicity of moenomycin leads to unfavourable pharmacokinetic properties that render it unsuitable for systemic administration. In this study, we show that using moenomycin and other glycosyltransferase inhibitors as templates, we were able to synthesize compound libraries based on novel pyranose scaffold chemistry, with moenomycin-like activity, but with improved drug-like properties. The novel compounds exhibit in vitro inhibition comparable to moenomycin, with low toxicity and good efficacy in several in vivo models of infection. This approach based on non-planar carbohydrate scaffolds provides a new opportunity to develop new antibiotics with low propensity for resistance induction.
MeSH term(s)	Animals ; Anti-Bacterial Agents/chemical synthesis ; Anti-Bacterial Agents/therapeutic use ; Female ; Glycosyltransferases/antagonists & inhibitors ; Humans ; Mastitis/drug therapy ; Mice ; Microbial Sensitivity Tests ; Molecular Docking Simulation ; Oligosaccharides/chemistry ; Staphylococcus aureus
Chemical Substances	Anti-Bacterial Agents ; Oligosaccharides ; Glycosyltransferases (EC 2.4.-) ; moenomycin (PP922A42V2)
Language	English
Publishing date	2015-07-21
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/ncomms8719
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