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Article ; Online: Spike D614G - A Candidate Vaccine Antigen Against Covid-19.

Koenig, Paul-Albert / Schmidt, Florian I

2021 Volume 384, Issue 24, Page(s) 2349–2351

MeSH term(s)	COVID-19 ; Humans ; SARS-CoV-2 ; Spike Glycoprotein, Coronavirus ; Vaccines
Chemical Substances	Spike Glycoprotein, Coronavirus ; Vaccines ; spike protein, SARS-CoV-2
Language	English
Publishing date	2021-06-11
Publishing country	United States
Document type	Journal Article ; Comment
ZDB-ID	207154-x
ISSN	1533-4406 ; 0028-4793
ISSN (online)	1533-4406
ISSN	0028-4793
DOI	10.1056/NEJMcibr2106054
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Article: Protein quality control in the endoplasmic reticulum.

Koenig, Paul-Albert / Ploegh, Hidde L

F1000prime reports

2014 Volume 6, Page(s) 49

Abstract: THE TOPOLOGICAL BARRIERS DEFINED BY BIOLOGICAL MEMBRANES ARE NOT IMPERMEABLE: from small solutes to intact proteins, specialized transport and translocation mechanisms adjust to the cell's needs. Here, we review the removal of unwanted proteins from the ... ...

Abstract	THE TOPOLOGICAL BARRIERS DEFINED BY BIOLOGICAL MEMBRANES ARE NOT IMPERMEABLE: from small solutes to intact proteins, specialized transport and translocation mechanisms adjust to the cell's needs. Here, we review the removal of unwanted proteins from the endoplasmic reticulum (ER) and emphasize the need to extend observations from tissue culture models and simple eukaryotes to studies in whole animals. The variation in protein production and composition that characterizes different cell types and tissues requires tailor-made solutions to exert proper control over both protein synthesis and breakdown. The ER is an organelle essential to achieve and maintain such homeostasis.
Language	English
Publishing date	2014-07-08
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	2709303-7
ISSN	2051-7599
ISSN	2051-7599
DOI	10.12703/P6-49
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Article ; Online: Structural and mechanistic analysis of a tripartite ATP-independent periplasmic TRAP transporter

Martin F. Peter / Jan A. Ruland / Peer Depping / Niels Schneberger / Emmanuele Severi / Jonas Moecking / Karl Gatterdam / Sarah Tindall / Alexandre Durand / Veronika Heinz / Jan Peter Siebrasse / Paul-Albert Koenig / Matthias Geyer / Christine Ziegler / Ulrich Kubitscheck / Gavin H. Thomas / Gregor Hagelueken

Nature Communications, Vol 13, Iss 1, Pp 1-

2022 Volume 15

Abstract: Tripartite ATP-independent periplasmic (TRAP) transporters are widespread in bacteria and archaea. Here, the authors used cryo-EM and a range of biophysical techniques to study the structure of function of the sialic acid TRAP transporter HiSiaQM. ...

Abstract	Tripartite ATP-independent periplasmic (TRAP) transporters are widespread in bacteria and archaea. Here, the authors used cryo-EM and a range of biophysical techniques to study the structure of function of the sialic acid TRAP transporter HiSiaQM.
Keywords	Science ; Q
Language	English
Publishing date	2022-08-01T00:00:00Z
Publisher	Nature Portfolio
Document type	Article ; Online
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Article ; Online: Posttranscriptional Regulation of Glycoprotein Quality Control in the Endoplasmic Reticulum Is Controlled by the E2 Ub-Conjugating Enzyme UBC6e.

Hagiwara, Masatoshi / Ling, Jingjing / Koenig, Paul-Albert / Ploegh, Hidde L

Molecular cell

2016 Volume 63, Issue 5, Page(s) 753–767

Abstract: ER-associated degradation (ERAD) is essential for protein quality control in the ER, not only when the ER is stressed, but also at steady state. We report a new layer of homeostatic control, in which ERAD activity itself is regulated ... ...

Abstract	ER-associated degradation (ERAD) is essential for protein quality control in the ER, not only when the ER is stressed, but also at steady state. We report a new layer of homeostatic control, in which ERAD activity itself is regulated posttranscriptionally and independently of the unfolded protein response by adjusting the endogenous levels of EDEM1, OS-9, and SEL1L (ERAD enhancers). Functional UBC6e requires its precise location in the ER to form a supramolecular complex with Derlin2. This complex targets ERAD enhancers for degradation, a function that depends on UBC6e's enzymatic activity. Ablation of UBC6e causes upregulation of active ERAD enhancers and so increases clearance not only of terminally misfolded substrates, but also of wild-type glycoproteins that fold comparatively slowly in vitro and in vivo. The levels of proteins that comprise the ERAD machinery are thus carefully tuned and adjusted to prevailing needs.
MeSH term(s)	Animals ; Endoplasmic Reticulum/metabolism ; Endoplasmic Reticulum-Associated Degradation ; Fibroblasts/cytology ; Fibroblasts/metabolism ; Genetic Vectors/chemistry ; Genetic Vectors/metabolism ; Glycosylation ; HEK293 Cells ; Humans ; Lectins/genetics ; Lectins/metabolism ; Lentivirus/genetics ; Lentivirus/metabolism ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Mice ; Neoplasm Proteins/genetics ; Neoplasm Proteins/metabolism ; Protein Processing, Post-Translational ; Proteins/genetics ; Proteins/metabolism ; Proteolysis ; Ubiquitin-Conjugating Enzymes/deficiency ; Ubiquitin-Conjugating Enzymes/genetics ; Unfolded Protein Response
Chemical Substances	DERL2 protein, human ; EDEM1 protein, human ; Lectins ; Membrane Proteins ; Neoplasm Proteins ; OS9 protein, human ; Proteins ; SEL1L protein, human ; UBE2J1 protein, human (EC 2.3.2.23) ; Ubiquitin-Conjugating Enzymes (EC 2.3.2.23)
Language	English
Publishing date	2016-09-01
Publishing country	United States
Document type	Journal Article
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2016.07.014
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Article ; Online: Structural and mechanistic analysis of a tripartite ATP-independent periplasmic TRAP transporter.

Peter, Martin F / Ruland, Jan A / Depping, Peer / Schneberger, Niels / Severi, Emmanuele / Moecking, Jonas / Gatterdam, Karl / Tindall, Sarah / Durand, Alexandre / Heinz, Veronika / Siebrasse, Jan Peter / Koenig, Paul-Albert / Geyer, Matthias / Ziegler, Christine / Kubitscheck, Ulrich / Thomas, Gavin H / Hagelueken, Gregor

Nature communications

2022 Volume 13, Issue 1, Page(s) 4471

Abstract: Tripartite ATP-independent periplasmic (TRAP) transporters are found widely in bacteria and archaea and consist of three structural domains, a soluble substrate-binding protein (P-domain), and two transmembrane domains (Q- and M-domains). HiSiaPQM and ... ...

Abstract	Tripartite ATP-independent periplasmic (TRAP) transporters are found widely in bacteria and archaea and consist of three structural domains, a soluble substrate-binding protein (P-domain), and two transmembrane domains (Q- and M-domains). HiSiaPQM and its homologs are TRAP transporters for sialic acid and are essential for host colonization by pathogenic bacteria. Here, we reconstitute HiSiaQM into lipid nanodiscs and use cryo-EM to reveal the structure of a TRAP transporter. It is composed of 16 transmembrane helices that are unexpectedly structurally related to multimeric elevator-type transporters. The idiosyncratic Q-domain of TRAP transporters enables the formation of a monomeric elevator architecture. A model of the tripartite PQM complex is experimentally validated and reveals the coupling of the substrate-binding protein to the transporter domains. We use single-molecule total internal reflection fluorescence (TIRF) microscopy in solid-supported lipid bilayers and surface plasmon resonance to study the formation of the tripartite complex and to investigate the impact of interface mutants. Furthermore, we characterize high-affinity single variable domains on heavy chain (VHH) antibodies that bind to the periplasmic side of HiSiaQM and inhibit sialic acid uptake, providing insight into how TRAP transporter function might be inhibited in vivo.
MeSH term(s)	Adenosine Triphosphate/metabolism ; Archaea/metabolism ; Bacteria/metabolism ; Bacterial Proteins/metabolism ; Carrier Proteins/metabolism ; Membrane Transport Proteins/metabolism ; N-Acetylneuraminic Acid/metabolism
Chemical Substances	Bacterial Proteins ; Carrier Proteins ; Membrane Transport Proteins ; Adenosine Triphosphate (8L70Q75FXE) ; N-Acetylneuraminic Acid (GZP2782OP0)
Language	English
Publishing date	2022-08-04
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/s41467-022-31907-y
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Article: Posttranscriptional Regulation of Glycoprotein Quality Control in the Endoplasmic Reticulum Is Controlled by the E2 Ub-Conjugating Enzyme UBC6e

Hagiwara, Masatoshi / Hidde L. Ploegh / Jingjing Ling / Paul-Albert Koenig

Molecular cell. 2016 Sept. 01, v. 63, no. 5

2016

Abstract	ER-associated degradation (ERAD) is essential for protein quality control in the ER, not only when the ER is stressed, but also at steady state. We report a new layer of homeostatic control, in which ERAD activity itself is regulated posttranscriptionally and independently of the unfolded protein response by adjusting the endogenous levels of EDEM1, OS-9, and SEL1L (ERAD enhancers). Functional UBC6e requires its precise location in the ER to form a supramolecular complex with Derlin2. This complex targets ERAD enhancers for degradation, a function that depends on UBC6e’s enzymatic activity. Ablation of UBC6e causes upregulation of active ERAD enhancers and so increases clearance not only of terminally misfolded substrates, but also of wild-type glycoproteins that fold comparatively slowly in vitro and in vivo. The levels of proteins that comprise the ERAD machinery are thus carefully tuned and adjusted to prevailing needs.
Keywords	endoplasmic reticulum ; enzyme activity ; glycoproteins ; quality control ; unfolded protein response
Language	English
Dates of publication	2016-0901
Size	p. 753-767.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2016.07.014
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Article ; Online: The fungal peptide toxin Candidalysin activates the NLRP3 inflammasome and causes cytolysis in mononuclear phagocytes

Lydia Kasper / Annika König / Paul-Albert Koenig / Mark S. Gresnigt / Johannes Westman / Rebecca A. Drummond / Michail S. Lionakis / Olaf Groß / Jürgen Ruland / Julian R. Naglik / Bernhard Hube

Nature Communications, Vol 9, Iss 1, Pp 1-

2018 Volume 20

Abstract: Phagocytic cells of the innate immune system play critical roles in defence against invading pathogens including the opportunistic pathogen Candida albicans. Here the authors show that C. albicans derived Candidalysin in addition to being a cell-damaging ...

Abstract	Phagocytic cells of the innate immune system play critical roles in defence against invading pathogens including the opportunistic pathogen Candida albicans. Here the authors show that C. albicans derived Candidalysin in addition to being a cell-damaging toxin to mononuclear phagocytes is a trigger of NLRP3 inflammasome activation in these cells.
Keywords	Science ; Q
Language	English
Publishing date	2018-10-01T00:00:00Z
Publisher	Nature Portfolio
Document type	Article ; Online
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Article ; Online: The fungal peptide toxin Candidalysin activates the NLRP3 inflammasome and causes cytolysis in mononuclear phagocytes.

Kasper, Lydia / König, Annika / Koenig, Paul-Albert / Gresnigt, Mark S / Westman, Johannes / Drummond, Rebecca A / Lionakis, Michail S / Groß, Olaf / Ruland, Jürgen / Naglik, Julian R / Hube, Bernhard

Nature communications

2018 Volume 9, Issue 1, Page(s) 4260

Abstract: Clearance of invading microbes requires phagocytes of the innate immune system. However, successful pathogens have evolved sophisticated strategies to evade immune killing. The opportunistic human fungal pathogen Candida albicans is efficiently ... ...

Abstract	Clearance of invading microbes requires phagocytes of the innate immune system. However, successful pathogens have evolved sophisticated strategies to evade immune killing. The opportunistic human fungal pathogen Candida albicans is efficiently phagocytosed by macrophages, but causes inflammasome activation, host cytolysis, and escapes after hypha formation. Previous studies suggest that macrophage lysis by C. albicans results from early inflammasome-dependent cell death (pyroptosis), late damage due to glucose depletion and membrane piercing by growing hyphae. Here we show that Candidalysin, a cytolytic peptide toxin encoded by the hypha-associated gene ECE1, is both a central trigger for NLRP3 inflammasome-dependent caspase-1 activation via potassium efflux and a key driver of inflammasome-independent cytolysis of macrophages and dendritic cells upon infection with C. albicans. This suggests that Candidalysin-induced cell damage is a third mechanism of C. albicans-mediated mononuclear phagocyte cell death in addition to damage caused by pyroptosis and the growth of glucose-consuming hyphae.
MeSH term(s)	Actins/metabolism ; Animals ; Bone Marrow Cells/drug effects ; Bone Marrow Cells/metabolism ; Caspase 1/metabolism ; Cell Death/drug effects ; Dendritic Cells/drug effects ; Dendritic Cells/metabolism ; Female ; Fungal Proteins/toxicity ; Humans ; Inflammasomes/metabolism ; Inflammation/pathology ; Interleukin-1beta/metabolism ; Leukocytes, Mononuclear/cytology ; Leukocytes, Mononuclear/drug effects ; Leukocytes, Mononuclear/metabolism ; Macrophages/drug effects ; Macrophages/metabolism ; Mice, Inbred C57BL ; Mycotoxins/toxicity ; NLR Family, Pyrin Domain-Containing 3 Protein/metabolism ; Necrosis ; Phagocytes/cytology ; Phagocytes/drug effects ; Phagocytes/metabolism ; Phagosomes/drug effects ; Phagosomes/metabolism ; Potassium/pharmacology
Chemical Substances	Actins ; ECE1 protein, Candida albicans ; Fungal Proteins ; Inflammasomes ; Interleukin-1beta ; Mycotoxins ; NLR Family, Pyrin Domain-Containing 3 Protein ; Caspase 1 (EC 3.4.22.36) ; Potassium (RWP5GA015D)
Language	English
Publishing date	2018-10-15
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/s41467-018-06607-1
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Article ; Online: Amino acid copolymers that alleviate experimental autoimmune encephalomyelitis in vivo interact with heparan sulfates and glycoprotein 96 in APCs.

Koenig, Paul-Albert / Spooner, Eric / Kawamoto, Norio / Strominger, Jack L / Ploegh, Hidde L

Journal of immunology (Baltimore, Md. : 1950)

2013 Volume 191, Issue 1, Page(s) 208–216

Abstract: Multiple sclerosis (MS) is an autoimmune disease that affects the CNS. One approved treatment for relapsing forms of MS is YEAK, a random copolymer of the amino acids tyrosine, glutamic acid, alanine, and lysine. YFAK, a second-generation copolymer ... ...

Abstract	Multiple sclerosis (MS) is an autoimmune disease that affects the CNS. One approved treatment for relapsing forms of MS is YEAK, a random copolymer of the amino acids tyrosine, glutamic acid, alanine, and lysine. YFAK, a second-generation copolymer composed of tyrosine, phenylalanine, alanine, and lysine, is more successful in treating experimental autoimmune encephalomyelitis, a mouse model of MS. Although originally designed and optimized based on the autoantigen myelin basic protein (MBP) and the MBP-derived peptide MBP85-99 presented to the MS-associated class II MHC molecule HLA-DR2, YEAK and YFAK also stimulate cytokine and chemokine production in APCs that lack class II MHC products. How YEAK and YFAK copolymers interact with APCs remains enigmatic. We used biotinylated YFAK to affinity-purify YFAK-interacting proteins from RAW264.7 cells and tested APCs from mice deficient in several of the newly identified interactors for their capacity to secrete CCL22 in response to YEAK and YFAK. We propose that initial contact of YFAK with cells is mediated mainly by electrostatic interactions, and find that interaction of YFAK with host proteins is strongly dependent on ionic strength. Cells deficient in enzymes involved in sulfation of proteins and proteoglycans showed strongly reduced binding of biotinylated YFAK. Lastly, cells stimulated with YFAK in the presence of heparin, structurally similar to heparan sulfates, failed to produce CCL22. We conclude that charge-dependent interactions of copolymers that alleviate MS/experimental autoimmune encephalomyelitis are critical for their effects exerted on APCs and may well be the main initial mediators of these therapeutically active copolymers.
MeSH term(s)	Amino Acids/chemistry ; Amino Acids/metabolism ; Amino Acids/pharmacology ; Animals ; Antigen-Presenting Cells/chemistry ; Antigen-Presenting Cells/immunology ; Antigen-Presenting Cells/metabolism ; Biopolymers/chemistry ; Biopolymers/metabolism ; Biopolymers/pharmacology ; Biotinylation ; Cell Line ; Encephalomyelitis, Autoimmune, Experimental/immunology ; Encephalomyelitis, Autoimmune, Experimental/metabolism ; Encephalomyelitis, Autoimmune, Experimental/prevention & control ; Endoplasmic Reticulum/genetics ; Endoplasmic Reticulum/immunology ; Endoplasmic Reticulum/metabolism ; Heparitin Sulfate/metabolism ; Membrane Glycoproteins/deficiency ; Membrane Glycoproteins/metabolism ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Oligopeptides/chemistry ; Oligopeptides/metabolism ; Oligopeptides/pharmacology ; Primary Cell Culture ; Protein Interaction Mapping/methods ; Random Allocation
Chemical Substances	Amino Acids ; Biopolymers ; Membrane Glycoproteins ; Oligopeptides ; endoplasmin ; Heparitin Sulfate (9050-30-0)
Language	English
Publishing date	2013-06-05
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	3056-9
ISSN	1550-6606 ; 0022-1767 ; 1048-3233 ; 1047-7381
ISSN (online)	1550-6606
ISSN	0022-1767 ; 1048-3233 ; 1047-7381
DOI	10.4049/jimmunol.1300345
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Article ; Online: A catalytically inactive mutant of the deubiquitylase YOD-1 enhances antigen cross-presentation.

Sehrawat, Sharvan / Koenig, Paul-Albert / Kirak, Oktay / Schlieker, Christian / Fankhauser, Manuel / Ploegh, Hidde L

Blood

2012 Volume 121, Issue 7, Page(s) 1145–1156

Abstract: Antigen presenting cells (APCs) that express a catalytically inactive version of the deubiquitylase YOD1 (YOD1-C160S) present exogenous antigens more efficiently to CD8(+) T cells, both in vitro and in vivo. Compared with controls, immunization of YOD1- ... ...

Abstract	Antigen presenting cells (APCs) that express a catalytically inactive version of the deubiquitylase YOD1 (YOD1-C160S) present exogenous antigens more efficiently to CD8(+) T cells, both in vitro and in vivo. Compared with controls, immunization of YOD1-C160S mice led to greater expansion of specific CD8(+) T cells and showed improved control of infection with a recombinant -herpes virus, MHV-68, engineered to express SIINFEKL peptide, the ligand for the ovalbumin-specific TCR transgenic OT-I cells. Enhanced expansion of specific CD8(+) T cells was likewise observed on infection of YOD1-C160S mice with a recombinant influenza A virus expressing SIINFEKL. YOD1-C160S APCs retained antigen longer than did control APCs. Enhanced crosspresentation by YOD1-C160S APCs was transporter associated with antigen processing (TAP1)-independent but sensitive to inclusion of inhibitors of acidification and of the proteasome. The activity of deubiquitylating enzymes may thus help control antigenspecific CD8(+) T-cell responses during immunization.
MeSH term(s)	ATP Binding Cassette Transporter, Subfamily B, Member 2 ; ATP-Binding Cassette Transporters/deficiency ; ATP-Binding Cassette Transporters/genetics ; ATP-Binding Cassette Transporters/immunology ; Adoptive Transfer ; Animals ; Antigen-Presenting Cells/enzymology ; Antigen-Presenting Cells/immunology ; Brefeldin A/pharmacology ; CD8-Positive T-Lymphocytes/immunology ; Cross-Priming/drug effects ; Cross-Priming/genetics ; Female ; Hydrogen-Ion Concentration ; Immunization ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Mice, Transgenic ; Mutation, Missense ; Ovalbumin/immunology ; Peptide Fragments/immunology ; Rhadinovirus/immunology ; Rhadinovirus/pathogenicity ; Ubiquitin Thiolesterase/genetics ; Ubiquitin Thiolesterase/immunology ; Ubiquitin Thiolesterase/metabolism
Chemical Substances	ATP Binding Cassette Transporter, Subfamily B, Member 2 ; ATP-Binding Cassette Transporters ; OVA-8 ; Peptide Fragments ; Tap1 protein, mouse ; Brefeldin A (20350-15-6) ; Ovalbumin (9006-59-1) ; Ubiquitin Thiolesterase (EC 3.4.19.12)
Language	English
Publishing date	2012-12-13
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	80069-7
ISSN	1528-0020 ; 0006-4971
ISSN (online)	1528-0020
ISSN	0006-4971
DOI	10.1182/blood-2012-08-447409
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