LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 7 of total 7

Search options

  1. Article ; Online: Rational design of a highly immunogenic prefusion-stabilized F glycoprotein antigen for a respiratory syncytial virus vaccine.

    Che, Ye / Gribenko, Alexey V / Song, Xi / Handke, Luke D / Efferen, Kari S / Tompkins, Kristin / Kodali, Srinivas / Nunez, Lorna / Prasad, A Krishna / Phelan, Lynn M / Ammirati, Mark / Yu, Xiaodi / Lees, Joshua A / Chen, Wei / Martinez, Lyndsey / Roopchand, Vidia / Han, Seungil / Qiu, Xiayang / DeVincenzo, John P /
    Jansen, Kathrin U / Dormitzer, Philip R / Swanson, Kena A

    Science translational medicine

    2023  Volume 15, Issue 693, Page(s) eade6422

    Abstract: Respiratory syncytial virus (RSV) is the leading, global cause of serious respiratory disease in infants and is an important cause of respiratory illness in older adults. No RSV vaccine is currently available. The RSV fusion (F) glycoprotein is a key ... ...

    Abstract Respiratory syncytial virus (RSV) is the leading, global cause of serious respiratory disease in infants and is an important cause of respiratory illness in older adults. No RSV vaccine is currently available. The RSV fusion (F) glycoprotein is a key antigen for vaccine development, and its prefusion conformation is the target of the most potent neutralizing antibodies. Here, we describe a computational and experimental strategy for designing immunogens that enhance the conformational stability and immunogenicity of RSV prefusion F. We obtained an optimized vaccine antigen after screening nearly 400 engineered F constructs. Through in vitro and in vivo characterization studies, we identified F constructs that are more stable in the prefusion conformation and elicit ~10-fold higher serum-neutralizing titers in cotton rats than DS-Cav1. The stabilizing mutations of the lead construct (847) were introduced onto F glycoprotein backbones of strains representing the dominant circulating genotypes of the two major RSV subgroups, A and B. Immunization of cotton rats with a bivalent vaccine formulation of these antigens conferred complete protection against RSV challenge, with no evidence of disease enhancement. The resulting bivalent RSV prefusion F investigational vaccine has recently been shown to be efficacious against RSV disease in two pivotal phase 3 efficacy trials, one for passive protection of infants by immunization of pregnant women and the second for active protection of older adults by direct immunization.
    MeSH term(s) Pregnancy ; Female ; Humans ; Animals ; Respiratory Syncytial Virus Vaccines ; Antibodies, Viral ; Antibodies, Neutralizing ; Respiratory Syncytial Virus Infections/prevention & control ; Respiratory Syncytial Virus, Human/genetics ; Glycoproteins ; Sigmodontinae ; Viral Fusion Proteins/genetics
    Chemical Substances Respiratory Syncytial Virus Vaccines ; Antibodies, Viral ; Antibodies, Neutralizing ; Glycoproteins ; Viral Fusion Proteins
    Language English
    Publishing date 2023-04-26
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2518854-9
    ISSN 1946-6242 ; 1946-6234
    ISSN (online) 1946-6242
    ISSN 1946-6234
    DOI 10.1126/scitranslmed.ade6422
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 6941: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  2. Article: Factor XIIIa mediated attachment of S. aureus fibronectin-binding protein A (FnbA) to fibrin: identification of Gln103 as a major cross-linking site.

    Severina, Elena / Nunez, Lorna / Baker, Steven / Matsuka, Yury V

    Biochemistry

    2006  Volume 45, Issue 6, Page(s) 1870–1880

    Abstract: In the present study we investigated the role of factor XIIIa reactive Gln and Lys sites of staphylococcal FnbA receptor in cross-linking reaction with alpha chains of fibrin. For this purpose we produced two recombinant FnbA mutants in which either a ... ...

    Abstract In the present study we investigated the role of factor XIIIa reactive Gln and Lys sites of staphylococcal FnbA receptor in cross-linking reaction with alpha chains of fibrin. For this purpose we produced two recombinant FnbA mutants in which either a single Gln103 site (1Q FnbA) or all identified reactive Gln103, 105, 783, 830 and Lys157, 503, 620, 762 sites (4Q4K FnbA) were substituted with Ala residues. The results of FXIIIa-catalyzed incorporation of dansylcadaverine and dansylated peptide patterned on the NH2-terminal segment of fibronectin revealed that the reactivity of Gln substrate sites was drastically reduced in 1Q FnbA and 4Q4K FnbA mutants, while the reactivity of Lys substrate sites was only moderately decreased in 4Q4K FnbA. When it was tested in the FXIIIa-mediated fibrin cross-linking reaction, the 1Q FnbA mutant exhibited about 70-85% reduction in reactivity compared to that of the wild-type FnbA. These results demonstrate that FnbA participates in cross-linking to alpha chains of fibrin predominantly via its Gln103 reactive site. Several minor sites, including residues replaced in 4Q4K FnbA mutant, contributed to an additional 15-30% of the total fibrin cross-linking reactivity of FnbA. Comparison of amino acid sequences that follow the major reactive Gln site in FnbA and several known substrate proteins revealed that FXIIIa displays a preference for the glutamine residue in an xQAxBxPx sequence, where Q represents reactive glutamine, x is any amino acid residue, A is a polar residue, B is either valine or leucine, and P is proline.
    MeSH term(s) Adhesins, Bacterial/metabolism ; Base Sequence ; Binding Sites ; Catalysis ; Cross-Linking Reagents/chemistry ; Electrophoresis, Polyacrylamide Gel ; Factor XIIIa/metabolism ; Fibrin/metabolism ; Glutamine/chemistry ; Glutamine/metabolism ; Leucine/chemistry ; Leucine/metabolism ; Lysine/chemistry ; Lysine/metabolism ; Proline/chemistry ; Proline/metabolism ; Staphylococcus aureus/chemistry ; Time Factors ; Urea/pharmacology
    Chemical Substances Adhesins, Bacterial ; Cross-Linking Reagents ; fibronectin-binding proteins, bacterial ; Glutamine (0RH81L854J) ; Urea (8W8T17847W) ; Fibrin (9001-31-4) ; Proline (9DLQ4CIU6V) ; Factor XIIIa (EC 2.3.2.13) ; Leucine (GMW67QNF9C) ; Lysine (K3Z4F929H6)
    Language English
    Publishing date 2006-02-14
    Publishing country United States
    Document type Comparative Study ; Journal Article
    ZDB-ID 1108-3
    ISSN 1520-4995 ; 0006-2960
    ISSN (online) 1520-4995
    ISSN 0006-2960
    DOI 10.1021/bi0521240
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 217: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  3. Article ; Online: Staphylococcus aureus manganese transport protein C is a highly conserved cell surface protein that elicits protective immunity against S. aureus and Staphylococcus epidermidis.

    Anderson, Annaliesa S / Scully, Ingrid L / Timofeyeva, Yekaterina / Murphy, Ellen / McNeil, Lisa K / Mininni, Terri / Nuñez, Lorna / Carriere, Marjolaine / Singer, Christine / Dilts, Deborah A / Jansen, Kathrin U

    The Journal of infectious diseases

    2012  Volume 205, Issue 11, Page(s) 1688–1696

    Abstract: Staphylococcus aureus and other staphylococci cause severe human disease, and there are currently no vaccines available. We evaluated whether manganese transport protein C (MntC), which is conserved across the staphylococcal species group, could confer ... ...

    Abstract Staphylococcus aureus and other staphylococci cause severe human disease, and there are currently no vaccines available. We evaluated whether manganese transport protein C (MntC), which is conserved across the staphylococcal species group, could confer protection against S. aureus and Staphylococcus epidermidis. In vivo analysis of S. aureus MntC expression revealed that expression occurs very early during the infectious cycle. Active immunization with MntC was effective at reducing the bacterial load associated with S. aureus and S. epidermidis infection in an acute murine bacteremia model. Anti-MntC monoclonal antibodies have been identified that can bind S. aureus and S. epidermidis cells and are protective in an infant rat passive protection model and induce neutrophil respiratory burst activity. This is the first description of a protein that has the potential to provide protection across the staphylococcal species group.
    MeSH term(s) Animals ; Antibodies, Bacterial/blood ; Antibodies, Bacterial/immunology ; Bacteremia/immunology ; Bacteremia/prevention & control ; Bacteremia/therapy ; Bacterial Load ; Bacterial Proteins/genetics ; Bacterial Proteins/immunology ; Carrier Proteins/genetics ; Carrier Proteins/immunology ; Disease Models, Animal ; Female ; Immunization, Passive ; Membrane Proteins/genetics ; Membrane Proteins/immunology ; Mice ; Rabbits ; Rats ; Rats, Sprague-Dawley ; Staphylococcal Infections/immunology ; Staphylococcal Infections/prevention & control ; Staphylococcal Infections/therapy ; Staphylococcal Vaccines/administration & dosage ; Staphylococcal Vaccines/genetics ; Staphylococcal Vaccines/immunology ; Staphylococcus aureus/immunology ; Staphylococcus epidermidis/immunology ; Treatment Outcome
    Chemical Substances Antibodies, Bacterial ; Bacterial Proteins ; Carrier Proteins ; Membrane Proteins ; Staphylococcal Vaccines
    Language English
    Publishing date 2012-04-02
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 3019-3
    ISSN 1537-6613 ; 0022-1899
    ISSN (online) 1537-6613
    ISSN 0022-1899
    DOI 10.1093/infdis/jis272
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Uh II Zs.50: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)
    Zs.MO 445: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  4. Article ; Online: Challenges for the evaluation of Staphylococcus aureus protein based vaccines: monitoring antigenic diversity.

    Murphy, Ellen / Lin, Shuo L / Nunez, Lorna / Andrew, Lubomira / Fink, Pamela S / Dilts, Deborah A / Hoiseth, Susan K / Jansen, Kathrin U / Anderson, Annaliesa S

    Human vaccines

    2011  Volume 7 Suppl, Page(s) 51–59

    Abstract: Clumping factors A (ClfA) and B (ClfB) are Staphylococcus aureus virulence proteins that are displayed on the cell surface of the organism and have potential as vaccine antigens for the prevention of S. aureus disease. Here we evaluate the phylogeny of S. ...

    Abstract Clumping factors A (ClfA) and B (ClfB) are Staphylococcus aureus virulence proteins that are displayed on the cell surface of the organism and have potential as vaccine antigens for the prevention of S. aureus disease. Here we evaluate the phylogeny of S. aureus in the context of antigenic variation of these two surface proteins. ClfA and ClfB gene sequences, along with epidemiological markers (MLST, spa and capsule genotype) were obtained for 224 S. aureus isolates including both historical strains and a collection representative of current MRSA isolates from the United States. Variation within ClfA and ClfB was consistent with the established population biology of S. aureus, namely, that S. aureus strains belong to a relatively small number of clonal lineages, with evolution proceeding mainly by mutation and with little to no recombination between clades. Thus most variation in ClfA and ClfB occurs between but not within lineages, and particular groups of ClfA and ClfB variants are closely linked. This has important implications for vaccine development and assessment as it suggests that a relatively small survey of strains will be representative of the total population variation, whereas for species that evolve mainly by recombination, such as Neisseria meningitidis, analysis of a much larger number of strains is needed to accomplish the same purpose. Our study also revealed evidence for the de-evolution of ClfB and therefore its reduced suitability as a target for vaccine development compared to ClfA.
    MeSH term(s) Antigenic Variation ; Antigens, Bacterial/genetics ; Antigens, Bacterial/immunology ; Cluster Analysis ; Coagulase/genetics ; Coagulase/immunology ; DNA, Bacterial/chemistry ; DNA, Bacterial/genetics ; Evolution, Molecular ; Genotype ; Humans ; Mutation ; Phylogeny ; Polymorphism, Genetic ; Recombination, Genetic ; Sequence Analysis, DNA ; Staphylococcus aureus/genetics ; Staphylococcus aureus/immunology ; United States
    Chemical Substances Antigens, Bacterial ; Coagulase ; DNA, Bacterial
    Language English
    Publishing date 2011-01-01
    Publishing country United States
    Document type Journal Article
    ISSN 1554-8619
    ISSN (online) 1554-8619
    DOI 10.4161/hv.7.0.14562
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  5. Article: Mapping sites responsible for interactions of agrin with neurons.

    Burgess, Robert W / Dickman, Dion K / Nunez, Lorna / Glass, David J / Sanes, Joshua R

    Journal of neurochemistry

    2002  Volume 83, Issue 2, Page(s) 271–284

    Abstract: The multidomain proteoglycan agrin is a critical organizer of postsynaptic differentiation at the skeletal neuromuscular junction. Agrin is also abundant in the brain, but its roles there are unknown. As a step toward understanding these roles, we mapped ...

    Abstract The multidomain proteoglycan agrin is a critical organizer of postsynaptic differentiation at the skeletal neuromuscular junction. Agrin is also abundant in the brain, but its roles there are unknown. As a step toward understanding these roles, we mapped sites responsible for interactions of neurons with agrin. First, we used a series of recombinant agrin fragments to show that at least four sites on agrin interact with chick ciliary neurons. Use of blocking antibodies and peptides indicated that neurons adhere to a site in the second of three G domains by means of alphaVbeta1 integrin, and to a site in the last of four epidermal growth factor (EGF) repeats via a distinct beta1 integrin. A third, integrin-independent adhesion site is near to but distinct from the site that induces postsynaptic differentiation in muscles. These domains are insufficient, however, to account for neurite outgrowth-inhibiting properties of full-length agrin, which are mediated by the N-terminal half of the molecule. We then used a second set of agrin mutants to demonstrate and map a transmembrane domain in the amino-terminus of the SN-isoform of agrin. The extracellular matrix-bound form of agrin, called LN, bears an amino-terminus required for secretion and binding to laminin. The SN form, which is selectively expressed by neurons, bears a variant amino terminus that converts agrin from a secreted, matrix-associated protein to a type-II transmembrane protein, providing a mechanism for presenting agrin in central, as opposed to neuromuscular, synaptic clefts. The SN-amino terminus can mediate externalization and membrane anchoring of heterologous proteins, but is insufficient to target them to the synapse. Together, these studies define sites that contribute to the subcellular localization of and signaling by neuronal agrin.
    MeSH term(s) Agrin/metabolism ; Amino Acid Sequence ; Animals ; Binding Sites/physiology ; COS Cells ; Cell Adhesion/physiology ; Cell Membrane/metabolism ; Cells, Cultured ; Chick Embryo ; Fibroblasts/cytology ; Fibroblasts/metabolism ; Integrins/metabolism ; Molecular Sequence Data ; Neurons/cytology ; Neurons/metabolism ; Peptide Fragments/metabolism ; Protein Binding/physiology ; Protein Structure, Tertiary/physiology ; Structure-Activity Relationship
    Chemical Substances Agrin ; Integrins ; Peptide Fragments
    Language English
    Publishing date 2002-08-23
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 80158-6
    ISSN 1471-4159 ; 0022-3042 ; 1474-1644
    ISSN (online) 1471-4159
    ISSN 0022-3042 ; 1474-1644
    DOI 10.1046/j.1471-4159.2002.01102.x
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Ui II Zs.170: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  6. Article: Heterogeneous in vivo expression of clumping factor A and capsular polysaccharide by Staphylococcus aureus: implications for vaccine design.

    Nanra, Jasdeep S / Timofeyeva, Yekaterina / Buitrago, Sandra M / Sellman, Bret R / Dilts, Deborah A / Fink, Pamela / Nunez, Lorna / Hagen, Michael / Matsuka, Yury V / Mininni, Terri / Zhu, Duzhang / Pavliak, Viliam / Green, Bruce A / Jansen, Kathrin U / Anderson, Annaliesa S

    Vaccine

    2009  Volume 27, Issue 25-26, Page(s) 3276–3280

    Abstract: There is a clear unmet medical need for a vaccine that would prevent infections from Staphylococcus aureus (S. aureus). To validate antigens as potential vaccine targets it has to be demonstrated that the antigens are expressed in vivo. Using murine ... ...

    Abstract There is a clear unmet medical need for a vaccine that would prevent infections from Staphylococcus aureus (S. aureus). To validate antigens as potential vaccine targets it has to be demonstrated that the antigens are expressed in vivo. Using murine bacteremia and wound infection models, we demonstrate that the expression of clumping factor A (ClfA) and capsular polysaccharide antigens are heterogeneous and dependent on the challenge strains examined and the in vivo microenvironment. We also demonstrate opsonophagocitic activity mediated by either antigen is not impeded by the presence of the other antigen. The data presented in this report support a multiantigen approach for the development of a prophylactic S. aureus vaccine to ensure broad coverage against this versatile pathogen.
    MeSH term(s) Animals ; Antigens, Bacterial/biosynthesis ; Bacteremia/immunology ; Bacterial Capsules/analysis ; Bacterial Capsules/biosynthesis ; Bacterial Capsules/immunology ; Coagulase/analysis ; Coagulase/biosynthesis ; Coagulase/immunology ; Drug Design ; Female ; HL-60 Cells ; Humans ; Mice ; Mice, Inbred C57BL ; Phagocytosis ; Staphylococcal Vaccines/immunology ; Staphylococcus aureus/immunology
    Chemical Substances Antigens, Bacterial ; ClfA protein, Staphylococcus aureus ; Coagulase ; Staphylococcal Vaccines
    Language English
    Publishing date 2009-05-26
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 605674-x
    ISSN 1873-2518 ; 0264-410X
    ISSN (online) 1873-2518
    ISSN 0264-410X
    DOI 10.1016/j.vaccine.2009.01.062
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 1930: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)
    Zs.MO 458: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  7. Article: Sequence diversity of the factor H binding protein vaccine candidate in epidemiologically relevant strains of serogroup B Neisseria meningitidis.

    Murphy, Ellen / Andrew, Lubomira / Lee, Kwok-Leung / Dilts, Deborah A / Nunez, Lorna / Fink, Pamela S / Ambrose, Karita / Borrow, Ray / Findlow, Jamie / Taha, Muhamed-Kheir / Deghmane, Ala-Eddine / Kriz, Paula / Musilek, Martin / Kalmusova, Jitka / Caugant, Dominique A / Alvestad, Torill / Mayer, Leonard W / Sacchi, Claudio T / Wang, Xin /
    Martin, Diana / von Gottberg, Anne / du Plessis, Mignon / Klugman, Keith P / Anderson, Annaliesa S / Jansen, Kathrin U / Zlotnick, Gary W / Hoiseth, Susan K

    The Journal of infectious diseases

    2009  Volume 200, Issue 3, Page(s) 379–389

    Abstract: Background: Recombinant forms of Neisseria meningitidis human factor H binding protein (fHBP) are undergoing clinical trials in candidate vaccines against invasive meningococcal serogroup B disease. We report an extensive survey and phylogenetic ... ...

    Abstract Background: Recombinant forms of Neisseria meningitidis human factor H binding protein (fHBP) are undergoing clinical trials in candidate vaccines against invasive meningococcal serogroup B disease. We report an extensive survey and phylogenetic analysis of the diversity of fhbp genes and predicted protein sequences in invasive clinical isolates obtained in the period 2000-2006.
    Methods: Nucleotide sequences of fhbp genes were obtained from 1837 invasive N. meningitidis serogroup B (MnB) strains from the United States, Europe, New Zealand, and South Africa. Multilocus sequence typing (MLST) analysis was performed on a subset of the strains.
    Results: Every strain contained the fhbp gene. All sequences fell into 1 of 2 subfamilies (A or B), with 60%-75% amino acid identity between subfamilies and at least 83% identity within each subfamily. One fHBP sequence may have arisen via inter-subfamily recombination. Subfamily B sequences were found in 70% of the isolates, and subfamily A sequences were found in 30%. Multiple fHBP variants were detected in each of the common MLST clonal complexes. All major MLST complexes include strains in both subfamily A and subfamily B.
    Conclusions: The diversity of strains observed underscores the importance of studying the distribution of the vaccine antigen itself rather than relying on common epidemiological surrogates such as MLST.
    MeSH term(s) Amino Acid Sequence ; Antigens, Bacterial/chemistry ; Antigens, Bacterial/genetics ; Antigens, Bacterial/metabolism ; Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Europe/epidemiology ; Gene Expression Regulation, Bacterial/physiology ; Genetic Variation ; Humans ; Meningitis, Meningococcal/epidemiology ; Meningitis, Meningococcal/microbiology ; Meningococcal Vaccines/chemistry ; Meningococcal Vaccines/genetics ; Meningococcal Vaccines/metabolism ; Molecular Sequence Data ; Neisseria meningitidis, Serogroup B/genetics ; Neisseria meningitidis, Serogroup B/immunology ; Neisseria meningitidis, Serogroup B/metabolism ; New Zealand/epidemiology ; South Africa/epidemiology ; United States/epidemiology
    Chemical Substances Antigens, Bacterial ; Bacterial Proteins ; Meningococcal Vaccines ; factor H-binding protein, Neisseria meningitidis
    Language English
    Publishing date 2009-08-01
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 3019-3
    ISSN 1537-6613 ; 0022-1899
    ISSN (online) 1537-6613
    ISSN 0022-1899
    DOI 10.1086/600141
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Uh II Zs.50: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)
    Zs.MO 445: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

To top