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Book ; Thesis: Design and development of Pichia pastoris based dengue specific virus-like particles concerted with insights into stress responses during expression using a proteomic approach

Nemani, Satish Kumar

2015

Abstract: Dengue, envelope domain III, virus-like particles, hepatitis B surface antigen, Pichia pastoris, transmission electron microscopy, two-dimensional gel electrophoresis, unfolded protein response, endoplasmic reticulum associated degradation. - Hüllprotein ...

Author's details	von Nemani Satish Kumar
Abstract	Dengue, envelope domain III, virus-like particles, hepatitis B surface antigen, Pichia pastoris, transmission electron microscopy, two-dimensional gel electrophoresis, unfolded protein response, endoplasmic reticulum associated degradation. - Hüllprotein Domäne III, virusartige Partikel, Hepatitis B Oberflächenantigen, Transmissionselektronenmikroskopie, zweidimensionale Gelektrophorese, ungefaltete Proteinantwort, endoplasmatisches Retikulum assoziierte Degradierung
Language	English
Size	XX, 101 Bl., Ill., graph. Darst.
Document type	Book ; Thesis
Thesis / German Habilitation thesis	Univ., Diss.--Hannover, 2015
Database	Library catalogue of the German National Library of Science and Technology (TIB), Hannover

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Book ; Online ; Thesis: Design and development of Pichia pastoris based dengue specific virus-like particles concerted with insights into stress responses during expression using a proteomic approach

Nemani, Satish Kumar [Verfasser]

2015

Author's details	Nemani Satish Kumar
Keywords	Technische Chemie ; Technical Chemistry
Subject code	sg660
Language	English
Publisher	Technische Informationsbibliothek und Universitätsbibliothek Hannover (TIB)
Publishing place	Hannover
Document type	Book ; Online ; Thesis
Database	Digital theses on the web

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Article ; Online: PMCA-replicated PrP

Cali, Ignazio / Lavrich, Jody / Moda, Fabio / Kofskey, Diane / Nemani, Satish Kumar / Appleby, Brian / Tagliavini, Fabrizio / Soto, Claudio / Gambetti, Pierluigi / Notari, Silvio

Scientific reports

2019 Volume 9, Issue 1, Page(s) 5191

Abstract: The presence of abnormal, disease-related prion protein ( ... ...

Abstract	The presence of abnormal, disease-related prion protein (PrP
MeSH term(s)	Animals ; Brain/metabolism ; Brain/pathology ; Creutzfeldt-Jakob Syndrome/transmission ; Creutzfeldt-Jakob Syndrome/urine ; Humans ; Mice, Transgenic ; Prion Proteins/urine ; Prions/pathogenicity ; Protein Folding ; Protein Stability
Chemical Substances	Prion Proteins ; Prions
Language	English
Publishing date	2019-03-26
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-019-41694-0
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: PMCA-replicated PrPD in urine of vCJD patients maintains infectivity and strain characteristics of brain PrPD

Ignazio Cali / Jody Lavrich / Fabio Moda / Diane Kofskey / Satish Kumar Nemani / Brian Appleby / Fabrizio Tagliavini / Claudio Soto / Pierluigi Gambetti / Silvio Notari

Scientific Reports, Vol 9, Iss 1, Pp 1-

Transmission study

2019 Volume 7

Abstract: Abstract The presence of abnormal, disease-related prion protein (PrPD) has recently been demonstrated by protein misfolding cyclic amplification (PMCA) in urine of patients affected with variant Creutzfeldt-Jakob disease (vCJD), a prion disease ... ...

Abstract	Abstract The presence of abnormal, disease-related prion protein (PrPD) has recently been demonstrated by protein misfolding cyclic amplification (PMCA) in urine of patients affected with variant Creutzfeldt-Jakob disease (vCJD), a prion disease typically acquired from consumption of prion contaminated bovine meat. The complexity and multistage process of urine excretion along with the obligatory use of PMCA raise the issue of whether strain characteristics of the PrPD present in vCJD brains, such as infectivity and phenotype determination, are maintained in urine excreted PrPD and following amplification by PMCA. We inoculated transgenic mice expressing normal human PrP with amplified urine and brain homogenate achieving the same 100% attack rate, similar incubation periods (in both cases extremely long) and histopathological features as for type and severity of the lesions. Furthermore, PrPD characteristics analyzed by immunoblot and conformational stability immunoassay were indistinguishable. Inoculation of raw vCJD urine caused no disease, confirming the extremely low concentration of PrPD in vCJD urine. These findings show that strain characteristics of vCJD brain PrPD, including infectivity, are preserved in PrPD present in urine and are faithfully amplified by means of PMCA; moreover, they suggest that the PrPD urine test might allow for the diagnosis and identification of disease subtype also in sporadic CJD.
Keywords	Medicine ; R ; Science ; Q
Subject code	610
Language	English
Publishing date	2019-03-01T00:00:00Z
Publisher	Nature Publishing Group
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Co-occurrence of chronic traumatic encephalopathy and prion disease.

Nemani, Satish Kumar / Notari, Silvio / Cali, Ignazio / Alvarez, Victor E / Kofskey, Diane / Cohen, Mark / Stern, Robert A / Appleby, Brian / Abrams, Joseph / Schonberger, Lawrence / McKee, Ann / Gambetti, Pierluigi

Acta neuropathologica communications

2018 Volume 6, Issue 1, Page(s) 140

Abstract: Chronic traumatic encephalopathy (CTE) is a neurodegenerative disease associated with repetitive traumatic brain injury (TBI). CTE is generally found in athletes participating in contact sports and military personnel exposed to explosive blasts but can ... ...

Abstract	Chronic traumatic encephalopathy (CTE) is a neurodegenerative disease associated with repetitive traumatic brain injury (TBI). CTE is generally found in athletes participating in contact sports and military personnel exposed to explosive blasts but can also affect civilians. Clinically and pathologically, CTE overlaps with post-traumatic stress disorder (PTSD), a term mostly used in a clinical context. The histopathology of CTE is defined by the deposition of hyperphosphorylated tau protein in neurons and astrocytes preferentially with perivascular distribution and at the depths of the cortical sulci. In addition to hyperphosphorylated tau, other pathologic proteins are deposited in CTE, including amyloid β (Aβ), transactive response (TAR) DNA-binding protein 43 kDa (TDP-43) and α-synuclein. However, the coexistence of prion disease in CTE has not been observed. We report three cases of histopathologically validated CTE with co-existing sporadic prion disease. Two were identified in a cohort of 55 pathologically verified cases of CTE submitted to the CTE Center of Boston University. One was identified among brain tissues submitted to the National Prion Disease Pathology Surveillance Center of Case Western Reserve University. The histopathological phenotype and properties of the abnormal, disease-related prion protein (PrP
MeSH term(s)	Aged ; Aged, 80 and over ; Brain/metabolism ; Brain/pathology ; Chronic Traumatic Encephalopathy/complications ; Chronic Traumatic Encephalopathy/diagnostic imaging ; Humans ; Male ; Neurofibrillary Tangles/metabolism ; Neurofibrillary Tangles/pathology ; Prion Diseases/complications ; Prion Diseases/diagnostic imaging ; Prion Proteins/metabolism ; tau Proteins/metabolism
Chemical Substances	Prion Proteins ; tau Proteins
Language	English
Publishing date	2018-12-18
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2715589-4
ISSN	2051-5960 ; 2051-5960
ISSN (online)	2051-5960
ISSN	2051-5960
DOI	10.1186/s40478-018-0643-9
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Article ; Online: Optimization of conditions for secretion of dengue virus type 2 envelope domain III using Pichia pastoris.

Batra, Gaurav / Gurramkonda, Chandrasekhar / Nemani, Satish Kumar / Jain, Swatantra Kumar / Swaminathan, Sathyamangalam / Khanna, Navin

Journal of bioscience and bioengineering

2010 Volume 110, Issue 4, Page(s) 408–414

Abstract: We have developed a recombinant clone of the methylotrophic yeast Pichia pastoris capable of secreting dengue virus type 2 envelope domain III (sEDIII-2). We explored various induction parameters including media composition, temperature, pH, and methanol ...

Abstract	We have developed a recombinant clone of the methylotrophic yeast Pichia pastoris capable of secreting dengue virus type 2 envelope domain III (sEDIII-2). We explored various induction parameters including media composition, temperature, pH, and methanol concentration, to optimize conditions for sEDIII-2 expression in shake flask culture. Induction at 20°C in the presence of 2% (v/v) methanol in a medium buffered to pH 5.8 resulted in highest secretion of sEDIII-2. This yield could be further enhanced up to 70% by repeated induction of the same initial biomass. Using a fed-batch cultivation strategy, we observed that shake-flask yields can be scaled up ∼8-fold in a bioreactor. We obtained ∼94% purity with >70% recovery after purification. This study, which demonstrates for the first time the feasibility of secreting envelope domain III using the P. pastoris host, will be relevant to sub-unit approaches to dengue vaccine development.
MeSH term(s)	Biomass ; Bioreactors ; Chromatography, Liquid ; Culture Media ; Dengue Virus/genetics ; Electrophoresis, Polyacrylamide Gel ; Hydrogen-Ion Concentration ; Pichia/genetics ; Recombination, Genetic ; Temperature ; Viral Proteins/genetics
Chemical Substances	Culture Media ; Viral Proteins
Keywords	covid19
Language	English
Publishing date	2010-10
Publishing country	Japan
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1465387-4
ISSN	1347-4421 ; 1389-1723
ISSN (online)	1347-4421
ISSN	1389-1723
DOI	10.1016/j.jbiosc.2010.05.001
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Escherichia coli-expressed near full length HIV-1 envelope glycoprotein is a highly sensitive and specific diagnostic antigen.

Talha, Sheikh M / Nemani, Satish Kumar / Salminen, Teppo / Kumar, Sushil / Swaminathan, Sathyamangalam / Soukka, Tero / Pettersson, Kim / Khanna, Navin

BMC infectious diseases

2012 Volume 12, Page(s) 325

Abstract: Background: The Human Immunodeficiency Virus type 1 (HIV-1) envelope glycoprotein gp160, useful in detecting anti-HIV-1 antibodies, is difficult to express in heterologous hosts. The major hurdles are its signal sequence, strong hydrophobic regions and ... ...

Abstract	Background: The Human Immunodeficiency Virus type 1 (HIV-1) envelope glycoprotein gp160, useful in detecting anti-HIV-1 antibodies, is difficult to express in heterologous hosts. The major hurdles are its signal sequence, strong hydrophobic regions and heavy glycosylation. While it has not been possible to express full length recombinant (r)-gp160 in E. coli, it can be expressed in insect and mammalian cells, but at relatively higher cost. In this work, we report E. coli-based over-expression of r-gp160 variant and evaluate its performance in diagnostic immunoassays for the detection of anti-HIV-1 antibodies. Methods: A deletion variant of r-gp160 lacking hydrophobic regions of the parent full length molecule was expressed in E. coli and purified to near homogeneity using single-step Ni(II)-affinity chromatography. Biotinylated and europium(III) chelate-labeled versions of this antigen were used to set up one- and two-step time-resolved fluorometric double antigen sandwich assays. The performance of these assays was evaluated against a collection of well-characterized human sera (n=131), that included an in-house panel and four commercially procured panels. Results: In-frame deletion of three hydrophobic regions, spanning amino acid residues 1-43, 519-538 and 676-706, of full length HIV-1 gp160 resulted in its expression in E. coli. Both the one- and two-step assays manifested high sensitivity unambiguously identifying 75/77 and 77/77 HIV-1 positive sera, respectively. Both assays also identified all 52 HIV-seronegative sera correctly. Between the two assays, the mean signal-to-cutoff value of the two-step assay was an order of magnitude greater than that of the one-step assay. Both assays were highly specific manifesting no cross-reactivity towards antibodies specific to other viruses like hepatitis B, C, and human T cell leukemia viruses. Conclusions: This study has demonstrated the expression of r-gp160 variant in E. coli, by deletion of hydrophobic regions, and its purification in reasonable yields. This underscores the potential for cost saving in antigen production. Evaluation of this antigen in a double antigen sandwich two-step assay showed it to be a highly sensitive and specific HIV-1 diagnostic reagent. The amenability of this assay to the one-step format suggests its potential utility in developing a rapid point-of-care HIV-1 diagnostic test.
MeSH term(s)	Antigens, Viral/genetics ; Antigens, Viral/isolation & purification ; Chromatography, Affinity ; Clinical Laboratory Techniques/methods ; Escherichia coli/genetics ; Gene Expression ; HIV Antibodies/blood ; HIV Envelope Protein gp160/genetics ; HIV Envelope Protein gp160/isolation & purification ; HIV Infections/diagnosis ; Humans ; Immunoassay/methods ; Recombinant Proteins/genetics ; Recombinant Proteins/isolation & purification ; Sensitivity and Specificity ; Sequence Deletion
Chemical Substances	Antigens, Viral ; HIV Antibodies ; HIV Envelope Protein gp160 ; Recombinant Proteins ; gp160 protein, Human immunodeficiency virus 1
Language	English
Publishing date	2012-11-27
Publishing country	England
Document type	Comparative Study ; Evaluation Study ; Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1471-2334
ISSN (online)	1471-2334
DOI	10.1186/1471-2334-12-325
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Article: Optimization of conditions for secretion of dengue virus type 2 envelope domain III using Pichia pastoris

Batra, Gaurav / Gurramkonda, Chandrasekhar / Nemani, Satish Kumar / Jain, Swatantra Kumar / Swaminathan, Sathyamangalam / Khanna, Navin

Journal of bioscience and bioengineering. 2010 Oct., v. 110, no. 4

2010

Abstract	We have developed a recombinant clone of the methylotrophic yeast Pichia pastoris capable of secreting dengue virus type 2 envelope domain III (sEDIII-2). We explored various induction parameters including media composition, temperature, pH, and methanol concentration, to optimize conditions for sEDIII-2 expression in shake flask culture. Induction at 20°C in the presence of 2% (v/v) methanol in a medium buffered to pH 5.8 resulted in highest secretion of sEDIII-2. This yield could be further enhanced up to 70% by repeated induction of the same initial biomass. Using a fed-batch cultivation strategy, we observed that shake-flask yields can be scaled up ∼8-fold in a bioreactor. We obtained ∼94% purity with >70% recovery after purification. This study, which demonstrates for the first time the feasibility of secreting envelope domain III using the P. pastoris host, will be relevant to sub-unit approaches to dengue vaccine development.
Keywords	covid19
Language	English
Dates of publication	2010-10
Size	p. 408-414.
Publishing place	Osaka, Japan: Society for Bioscience and Bioengineering, Japan; Amsterdam, the Netherlands: Distributed outside Japan by Elsevier Science
Document type	Article
ZDB-ID	1465387-4
ISSN	1347-4421 ; 1389-1723
ISSN (online)	1347-4421
ISSN	1389-1723
DOI	10.1016/j.jbiosc.2010.05.001
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Expression, purification and characterization of in vivo biotinylated dengue virus envelope domain III based tetravalent antigen.

Batra, Gaurav / Talha, Sheikh Mohd / Nemani, Satish Kumar / Dhar, Nisha / Swaminathan, Sathyamangalam / Khanna, Navin

Protein expression and purification

2010 Volume 74, Issue 1, Page(s) 99–105

Abstract: Dengue is a rapidly spreading mosquito-borne viral disease prevalent in over a hundred countries around the world. A definitive identification of dengue infection depends on reliable dengue diagnostic tests. This study describes the design, expression ... ...

Abstract	Dengue is a rapidly spreading mosquito-borne viral disease prevalent in over a hundred countries around the world. A definitive identification of dengue infection depends on reliable dengue diagnostic tests. This study describes the design, expression and purification of an in vivo biotinylated chimeric dengue antigen to exploit the high affinity of biotin-streptavidin interaction to detect anti-dengue antibodies. This chimeric antigen incorporates the envelope domain III (EDIII) of the four dengue virus serotypes. A biotin acceptor peptide was fused with the chimeric dengue antigen for in vivo biotinylation in Escherichia coli through simultaneous co-expression of the biotin ligase, BirA. Despite the localization of the chimeric dengue antigen to the insoluble fraction of induced E. coli cells, it was found to be biotinylated in vivo. It was purified to near homogeneity using affinity chromatography with final yields of 20mg protein of approximately 95% purity, from 1L of induced E. coli shake flask culture, and the efficiency of biotinylation was estimated to be approximately 85%. Mouse antibodies specific to recombinant EDIII of each of the four dengue serotypes, captured on microtiter wells sensitized with anti-mouse immunoglobulin antibodies, were recognized specifically and with high efficiency by the biotinylated antigen in conjunction with streptavidin-enzyme conjugate. An evaluation of the biotinylated antigen against a panel of pre-characterized dengue-positive and dengue-negative human sera (n=164), in an antibody capture ELISA format, showed that it manifested 100% specificity, but also suggested that additional epitopes may need to be included in its design to enhance sensitivity.
MeSH term(s)	Animals ; Antibodies/immunology ; Antigens, Viral/genetics ; Antigens, Viral/immunology ; Antigens, Viral/isolation & purification ; Biotinylation ; Dengue/diagnosis ; Dengue Virus/genetics ; Dengue Virus/immunology ; Dengue Virus/isolation & purification ; Enzyme-Linked Immunosorbent Assay/methods ; Escherichia coli/genetics ; Gene Expression ; Humans ; Mice ; Viral Envelope Proteins/genetics ; Viral Envelope Proteins/immunology ; Viral Envelope Proteins/isolation & purification
Chemical Substances	Antibodies ; Antigens, Viral ; Viral Envelope Proteins
Language	English
Publishing date	2010-11
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1055455-5
ISSN	1096-0279 ; 1046-5928
ISSN (online)	1096-0279
ISSN	1046-5928
DOI	10.1016/j.pep.2010.04.017
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Zs.A 3084: Show issues

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Article ; Online: Purification of hepatitis B surface antigen virus-like particles from recombinant Pichia pastoris and in vivo analysis of their immunogenic properties.

Gurramkonda, Chandrasekhar / Zahid, Maria / Nemani, Satish Kumar / Adnan, Ahmad / Gudi, Satheesh Kumar / Khanna, Navin / Ebensen, Thomas / Lünsdorf, Heinrich / Guzmán, Carlos A / Rinas, Ursula

Journal of chromatography. B, Analytical technologies in the biomedical and life sciences

2013 Volume 940, Page(s) 104–111

Abstract: Following earlier studies on high-level intracellular production of hepatitis B surface antigen (HBsAg) using recombinant Pichia pastoris, we present here in detail an enhanced method for the purification of recombinant HBsAg virus-like particles (VLPs). ...

Abstract	Following earlier studies on high-level intracellular production of hepatitis B surface antigen (HBsAg) using recombinant Pichia pastoris, we present here in detail an enhanced method for the purification of recombinant HBsAg virus-like particles (VLPs). We have screened various detergents for their ability to promote the solubilization of recombinant intracellular HBsAg. In addition, we have analyzed the effect of cell disruption and extraction regarding their impact on the release of HBsAg. Our results show that introduction of the mild nonionic detergent Tween 20 in the initial process of cell lysis at ∼600bars by high pressure homogenization leads to the best results. The subsequent purification steps involved polyethylene glycol precipitation of host cell contaminants, hydrophobic adsorption of HBsAg to colloidal silica followed by ion-exchange chromatography and either isopycnic density ultracentrifugation or size exclusion chromatography for the recovery of the VLPs. After final KSCN treatment and dialysis, a total yield of ∼3% with a purity of >99% was reached. The pure protein was characterized by electron microscopy, showing the presence of uniform VLPs which are the pre-requisite for immunogenicity. The intramuscular co-administration of HBsAg VLPs, with either alum or a PEGylated-derivative of the toll-like receptor 2/6 agonist MALP-2, to mice resulted in the elicitation of significantly higher HBsAg-specific IgG titers as well as a stronger cellular immune response compared to mice vaccinated with a gold standard vaccine (Engerix™). These results show that P. pastoris derived HBsAg VLPs exhibit a high potential as a superior biosimilar vaccine against hepatitis B.
MeSH term(s)	Animals ; Chromatography, Gel ; Chromatography, Ion Exchange ; Female ; Hepatitis B Surface Antigens/chemistry ; Hepatitis B Surface Antigens/immunology ; Hepatitis B Surface Antigens/isolation & purification ; Hepatitis B Surface Antigens/metabolism ; Mice, Inbred BALB C ; Pichia/metabolism ; Recombinant Proteins/chemistry ; Recombinant Proteins/immunology ; Recombinant Proteins/isolation & purification ; Recombinant Proteins/metabolism ; Silicon Dioxide ; Statistics, Nonparametric ; Thiocyanates ; Ultracentrifugation ; Virion/chemistry ; Virion/immunology ; Virion/isolation & purification ; Virion/metabolism
Chemical Substances	Hepatitis B Surface Antigens ; Recombinant Proteins ; Thiocyanates ; Silicon Dioxide (7631-86-9) ; potassium thiocyanate (TM7213864A)
Language	English
Publishing date	2013-12-01
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1180823-8
ISSN	1873-376X ; 0378-4347 ; 1570-0232 ; 1387-2273
ISSN (online)	1873-376X
ISSN	0378-4347 ; 1570-0232 ; 1387-2273
DOI	10.1016/j.jchromb.2013.09.030
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