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Article ; Online: Saliva as a useful tool for evaluating upper mucosal antibody response to influenza.

Tsunetsugu-Yokota, Yasuko / Ito, Sayaka / Adachi, Yu / Onodera, Taishi / Kageyama, Tsutomu / Takahashi, Yoshimasa

2022 Volume 17, Issue 2, Page(s) e0263419

Abstract: Mucosal immunity plays a crucial role in controlling upper respiratory infections, including influenza. We established a quantitative ELISA to measure the amount of influenza virus-specific salivery IgA (sIgA) and salivary IgG (sIgG) antibodies using a ... ...

Abstract	Mucosal immunity plays a crucial role in controlling upper respiratory infections, including influenza. We established a quantitative ELISA to measure the amount of influenza virus-specific salivery IgA (sIgA) and salivary IgG (sIgG) antibodies using a standard antibody broadly reactive to the influenza A virus. We then analyzed saliva and serum samples from seven individuals infected with the A(H1N1)pdm09 influenza virus during the 2019-2020 flu seasons. We detected an early (6-10 days post-infection) increase of sIgA in five of the seven samples and a later (3-5 weeks) increase of sIgG in six of the seven saliva samples. Although the conventional parenteral influenza vaccine did not induce IgA production in saliva, vaccinated individuals with a history of influenza infection had higher basal levels of sIgA than those without a history. Interestingly, we observed sIgA and sIgG in an asymptomatic individual who had close contact with two influenza cases. Both early mucosal sIgA secretion and late systemically induced sIgG in the mucosal surface may protect against virus infection. Despite the small sample size, our results indicate that the saliva test system can be useful for analyzing upper mucosal immunity in influenza.
MeSH term(s)	Adult ; Aged ; Antibodies, Viral/analysis ; Antibodies, Viral/metabolism ; Antibody Formation ; Cohort Studies ; Female ; History, 21st Century ; Humans ; Immunity, Mucosal/physiology ; Immunoglobulin A/analysis ; Immunoglobulin A/metabolism ; Immunoglobulin A, Secretory/analysis ; Immunoglobulin A, Secretory/metabolism ; Immunoglobulin G/analysis ; Immunoglobulin G/metabolism ; Influenza A Virus, H1N1 Subtype/immunology ; Influenza Vaccines/therapeutic use ; Influenza, Human/diagnosis ; Influenza, Human/immunology ; Influenza, Human/prevention & control ; Japan ; Longitudinal Studies ; Male ; Predictive Value of Tests ; Prognosis ; Saliva/chemistry ; Saliva/immunology ; Saliva/metabolism ; Young Adult
Chemical Substances	Antibodies, Viral ; Immunoglobulin A ; Immunoglobulin A, Secretory ; Immunoglobulin G ; Influenza Vaccines
Language	English
Publishing date	2022-02-07
Publishing country	United States
Document type	Historical Article ; Journal Article
ZDB-ID	2267670-3
ISSN	1932-6203 ; 1932-6203
ISSN (online)	1932-6203
ISSN	1932-6203
DOI	10.1371/journal.pone.0263419
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: High-throughput isolation of SARS-CoV-2 nucleocapsid antibodies for improved antigen detection.

Fujisawa, Mizuki / Adachi, Yu / Onodera, Taishi / Shiwa-Sudo, Nozomi / Iwata-Yoshikawa, Naoko / Nagata, Noriyo / Suzuki, Tadaki / Takeoka, Shinji / Takahashi, Yoshimasa

Biochemical and biophysical research communications

2023 Volume 673, Page(s) 114–120

Abstract: SARS-CoV-2 nucleocapsid protein (NP) is the main target for COVID-19-diagnostic PCR and antigen rapid diagnostic tests (Ag-RDTs). Ag-RDTs are more convenient than PCR tests for point-of-care testing or self-testing to identify the SARS-CoV-2 antigen. The ...

Abstract	SARS-CoV-2 nucleocapsid protein (NP) is the main target for COVID-19-diagnostic PCR and antigen rapid diagnostic tests (Ag-RDTs). Ag-RDTs are more convenient than PCR tests for point-of-care testing or self-testing to identify the SARS-CoV-2 antigen. The sensitivity and specificity of this method depends mainly on the affinity and specificity of NP-binding antibodies; therefore, antigen-antibody binding is key elements for the Ag-RDTs. Here, we applied the high-throughput antibody isolation platform that has been utilized to isolate therapeutic antibodies against rare epitopes. Two NP antibodies were identified to recognize non-overlapping epitopes with high affinity. One antibody specifically binds to SARS-CoV-2 NP, and the other rapidly and tightly binds to SARS-CoV-2 NP with cross-reactivity to SARS-CoV NP. Furthermore, these antibodies were compatible with a sandwich enzyme-linked immunosorbent assay that exhibited enhanced sensitivity for NP detection compared to the previously isolated NP antibodies. Thus, the NP antibody pair is applicable to more sensitive and specific Ag-RDTs, highlighting the utility of a high-throughput antibody isolation platform for diagnostics development.
MeSH term(s)	Humans ; SARS-CoV-2 ; COVID-19/diagnosis ; Nucleocapsid ; Antibodies, Viral ; Epitopes ; Sensitivity and Specificity
Chemical Substances	Antibodies, Viral ; Epitopes
Language	English
Publishing date	2023-06-19
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	205723-2
ISSN	1090-2104 ; 0006-291X ; 0006-291X
ISSN (online)	1090-2104 ; 0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2023.06.067
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Article ; Online: Overcoming antibody-resistant SARS-CoV-2 variants with bispecific antibodies constructed using non-neutralizing antibodies.

Inoue, Tetsuya / Yamamoto, Yuichiro / Sato, Kaoru / Okemoto-Nakamura, Yuko / Shimizu, Yoshimi / Ogawa, Motohiko / Onodera, Taishi / Takahashi, Yoshimasa / Wakita, Takaji / Kaneko, Mika K / Fukasawa, Masayoshi / Kato, Yukinari / Noguchi, Kohji

iScience

2024 Volume 27, Issue 4, Page(s) 109363

Abstract: A current challenge is the emergence of SARS-CoV-2 variants, such as BQ.1.1 and XBB.1.5, that can evade immune defenses, thereby limiting antibody drug effectiveness. Emergency-use antibody drugs, including the widely effective bebtelovimab, are losing ... ...

Abstract	A current challenge is the emergence of SARS-CoV-2 variants, such as BQ.1.1 and XBB.1.5, that can evade immune defenses, thereby limiting antibody drug effectiveness. Emergency-use antibody drugs, including the widely effective bebtelovimab, are losing their benefits. One potential approach to address this issue are bispecific antibodies which combine the targeting abilities of two antibodies with distinct epitopes. We engineered neutralizing bispecific antibodies in the IgG-scFv format from two initially non-neutralizing antibodies, CvMab-6 (which binds to the receptor-binding domain [RBD]) and CvMab-62 (targeting a spike protein S2 subunit epitope adjacent to the known anti-S2 antibody epitope). Furthermore, we created a bispecific antibody by incorporating the scFv of bebtelovimab with our anti-S2 antibody, demonstrating significant restoration of effectiveness against bebtelovimab-resistant BQ.1.1 variants. This study highlights the potential of neutralizing bispecific antibodies, which combine existing less effective anti-RBD antibodies with anti-S2 antibodies, to revive the effectiveness of antibody therapeutics compromised by immune-evading variants.
Language	English
Publishing date	2024-02-29
Publishing country	United States
Document type	Journal Article
ISSN	2589-0042
ISSN (online)	2589-0042
DOI	10.1016/j.isci.2024.109363
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Article: Neutralizing mAbs against SFTS Virus Gn Protein Show Strong Therapeutic Effects in an SFTS Animal Model

Shimojima, Masayuki / Sugimoto, Satoko / Umekita, Kunihiko / Onodera, Taishi / Sano, Kaori / Tani, Hideki / Takamatsu, Yuki / Yoshikawa, Tomoki / Kurosu, Takeshi / Suzuki, Tadaki / Takahashi, Yoshimasa / Ebihara, Hideki / Saijo, Masayuki

Viruses. 2022 July 28, v. 14, no. 8

2022

Abstract: Severe fever with thrombocytopenia syndrome (SFTS) is an infectious disease with a high case fatality rate caused by the SFTS virus, and currently there are no approved specific treatments. Neutralizing monoclonal antibodies (mAbs) against the virus ... ...

Abstract	Severe fever with thrombocytopenia syndrome (SFTS) is an infectious disease with a high case fatality rate caused by the SFTS virus, and currently there are no approved specific treatments. Neutralizing monoclonal antibodies (mAbs) against the virus could be a therapeutic agent in SFTS treatment, but their development has not sufficiently been carried out. In the present study, mouse and human mAbs exposed to the viral envelope proteins Gn and Gc (16 clones each) were characterized in vitro and in vivo by using recombinant proteins, cell culture with viruses, and an SFTS animal model with IFNAR⁻/⁻ mice. Neutralization activities against the recombinant vesicular stomatitis virus bearing SFTS virus Gn/Gc as envelope proteins were observed with three anti-Gn and six anti-Gc mAbs. Therapeutic activities were observed among anti-Gn, but not anti-Gc mAbs with neutralizing activities. These results propose an effective strategy to obtain promising therapeutic mAb candidates for SFTS treatment, and a necessity to reveal precise roles of the SFTS virus Gn/Gc proteins.
Keywords	Huaiyangshan banyangvirus ; Vesiculovirus ; animal models ; cell culture ; humans ; mice ; mortality ; neutralization ; severe fever with thrombocytopenia syndrome ; therapeutics ; viruses
Language	English
Dates of publication	2022-0728
Publishing place	Multidisciplinary Digital Publishing Institute
Document type	Article
ZDB-ID	2516098-9
ISSN	1999-4915
ISSN	1999-4915
DOI	10.3390/v14081665
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Heterologous SARS-CoV-2 spike protein booster elicits durable and broad antibody responses against the receptor-binding domain.

Takano, Tomohiro / Sato, Takashi / Kotaki, Ryutaro / Moriyama, Saya / Fukushi, Shuetsu / Shinoda, Masahiro / Kabasawa, Kiyomi / Shimada, Nagashige / Kousaka, Mio / Adachi, Yu / Onodera, Taishi / Terahara, Kazutaka / Isogawa, Masanori / Matsumura, Takayuki / Shinkai, Masaharu / Takahashi, Yoshimasa

Nature communications

2023 Volume 14, Issue 1, Page(s) 1451

Abstract: The immunogenicity of mRNA vaccines has not been well studied when compared to different vaccine modalities in the context of additional boosters. Here we show that longitudinal analysis reveals more sustained SARS-CoV-2 spike receptor-binding domain ( ... ...

Abstract	The immunogenicity of mRNA vaccines has not been well studied when compared to different vaccine modalities in the context of additional boosters. Here we show that longitudinal analysis reveals more sustained SARS-CoV-2 spike receptor-binding domain (RBD)-binding IgG titers with the breadth to antigenically distinct variants by the S-268019-b spike protein booster compared to the BNT162b2 mRNA homologous booster. The durability and breadth of RBD-angiotensin-converting enzyme 2 (ACE2) binding inhibitory antibodies are pronounced in the group without systemic adverse events (AEs) after the S-268019-b booster, leading to the elevated neutralizing activities against Omicron BA.1 and BA.5 variants in the stratified group. In contrast, BNT162b2 homologous booster elicited antibodies to spike N-terminal domain in proportion to the AE scores. High-dimensional immune profiling identifies early CD16
MeSH term(s)	Humans ; Antibodies, Neutralizing ; Antibodies, Viral ; Antibody Formation ; BNT162 Vaccine ; COVID-19 ; Immunoglobulin G ; SARS-CoV-2 ; Spike Glycoprotein, Coronavirus/genetics ; COVID-19 Vaccines/immunology
Chemical Substances	Antibodies, Neutralizing ; Antibodies, Viral ; BNT162 Vaccine ; Immunoglobulin G ; S-268019-b COVID-19 vaccine ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2 ; COVID-19 Vaccines
Language	English
Publishing date	2023-03-15
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/s41467-023-37128-1
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Article ; Online: Adaptive B Cell Responses to Influenza Virus Infection in the Lung.

Takahashi, Yoshimasa / Onodera, Taishi / Adachi, Yu / Ato, Manabu

Viral immunology

2017 Volume 30, Issue 6, Page(s) 431–437

Abstract: Adaptive B cell response is a key arm of protective immunity against influenza viruses. Owing to the acutely infectious and cytopathic nature of these viruses, efficient containment of viral spread relies on the prompt provision of protective antibodies ... ...

Abstract	Adaptive B cell response is a key arm of protective immunity against influenza viruses. Owing to the acutely infectious and cytopathic nature of these viruses, efficient containment of viral spread relies on the prompt provision of protective antibodies to the site of virus infection, the respiratory tract (RT). To accelerate the protective antibody response, B cell responses can be ectopically induced, maintained, and reactivated in the lungs after primary and secondary infection, thereby providing an anatomical advantage in supplying neutralizing antibodies against reinfecting viruses with faster kinetics. However, the prompt supply of protective antibodies may be insufficient to protect against reinfection because influenza viruses can easily change their antigenic profiles to escape antibody surveillance. B cell responses have multiple strategies for adjusting antibody repertoires according to viral fitness, one of which is the formation of local germinal centers capable of selecting B cell repertoires for antigenically subdominant, but conserved, epitopes. In this review, we discuss several unique aspects of B cell responses that take place at local sites to combat acutely infectious and rapidly mutating influenza viruses.
Language	English
Publishing date	2017-07
Publishing country	United States
Document type	Journal Article
ZDB-ID	639075-4
ISSN	1557-8976 ; 0882-8245
ISSN (online)	1557-8976
ISSN	0882-8245
DOI	10.1089/vim.2017.0025
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Zs.A 2227: Show issues

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Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

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Article ; Online: SARS-CoV-2-specific CD4

Terahara, Kazutaka / Sato, Takashi / Adachi, Yu / Tonouchi, Keisuke / Onodera, Taishi / Moriyama, Saya / Sun, Lin / Takano, Tomohiro / Nishiyama, Ayae / Kawana-Tachikawa, Ai / Matano, Tetsuro / Matsumura, Takayuki / Shinkai, Masaharu / Isogawa, Masanori / Takahashi, Yoshimasa

iScience

2022 Volume 25, Issue 9, Page(s) 104959

Abstract: Determinants of memory T cell longevity following severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection remain unknown. In addition, phenotypes associated with memory T cell longevity, antibody titers, and disease severity are ... ...

Abstract	Determinants of memory T cell longevity following severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection remain unknown. In addition, phenotypes associated with memory T cell longevity, antibody titers, and disease severity are incompletely understood. Here, we longitudinally analyzed SARS-CoV-2-specific T cell and antibody responses of a unique cohort with similar numbers of mild, moderate, and severe coronavirus disease 2019 cases. The half-lives of CD4
Language	English
Publishing date	2022-08-17
Publishing country	United States
Document type	Journal Article
ISSN	2589-0042
ISSN (online)	2589-0042
DOI	10.1016/j.isci.2022.104959
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Neutralizing mAbs against SFTS Virus Gn Protein Show Strong Therapeutic Effects in an SFTS Animal Model.

Viruses

2022 Volume 14, Issue 8

Abstract	Severe fever with thrombocytopenia syndrome (SFTS) is an infectious disease with a high case fatality rate caused by the SFTS virus, and currently there are no approved specific treatments. Neutralizing monoclonal antibodies (mAbs) against the virus could be a therapeutic agent in SFTS treatment, but their development has not sufficiently been carried out. In the present study, mouse and human mAbs exposed to the viral envelope proteins Gn and Gc (16 clones each) were characterized in vitro and in vivo by using recombinant proteins, cell culture with viruses, and an SFTS animal model with IFNAR
MeSH term(s)	Animals ; Antibodies, Monoclonal/therapeutic use ; Antibodies, Neutralizing/therapeutic use ; Antibodies, Viral/therapeutic use ; Disease Models, Animal ; Humans ; Mice ; Phlebovirus ; Severe Fever with Thrombocytopenia Syndrome ; Viral Envelope Proteins/metabolism
Chemical Substances	Antibodies, Monoclonal ; Antibodies, Neutralizing ; Antibodies, Viral ; Viral Envelope Proteins
Language	English
Publishing date	2022-07-28
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2516098-9
ISSN	1999-4915 ; 1999-4915
ISSN (online)	1999-4915
ISSN	1999-4915
DOI	10.3390/v14081665
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: The function of SARS-CoV-2 spike protein is impaired by disulfide-bond disruption with mutation at cysteine-488 and by thiol-reactive N-acetyl-cysteine and glutathione

Murae, Mana / Shimizu, Yoshimi / Yamamoto, Yuichiro / Kobayashi, Asuka / Houri, Masumi / Inoue, Tetsuya / Irie, Takuya / Gemba, Ryutaro / Kondo, Yosuke / Nakano, Yoshio / Miyazaki, Satoru / Yamada, Daisuke / Saitoh, Akiyoshi / Ishii, Isao / Onodera, Taishi / Takahashi, Yoshimasa / Wakita, Takaji / Fukasawa, Masayoshi / Noguchi, Kohji

Biochemical and biophysical research communications. 2022 Mar. 15, v. 597

2022

Abstract: Viral spike proteins play important roles in the viral entry process, facilitating attachment to cellular receptors and fusion of the viral envelope with the cell membrane. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike protein binds ... ...

Abstract	Viral spike proteins play important roles in the viral entry process, facilitating attachment to cellular receptors and fusion of the viral envelope with the cell membrane. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike protein binds to the cellular receptor angiotensin converting enzyme-2 (ACE2) via its receptor-binding domain (RBD). The cysteine residue at position 488, consisting of a disulfide bridge with cysteine 480 is located in an important structural loop at ACE2-binding surface of RBD, and is highly conserved among SARS-related coronaviruses. We showed that the substitution of Cys-488 with alanine impaired pseudotyped SARS-CoV-2 infection, syncytium formation, and cell-cell fusion triggered by SARS-CoV-2 spike expression. Consistently, in vitro binding of RBD and ACE2, spike-mediated cell-cell fusion, and pseudotyped viral infection of VeroE6/TMPRSS2 cells were inhibited by the thiol-reactive compounds N-acetylcysteine (NAC) and a reduced form of glutathione (GSH). Furthermore, we demonstrated that the activity of variant spikes from the SARS-CoV-2 alpha and delta strains were also suppressed by NAC and GSH. Taken together, these data indicate that Cys-488 in spike RBD is required for SARS-CoV-2 spike functions and infectivity, and could be a target of anti-SARS-CoV-2 therapeutics.
Keywords	Severe acute respiratory syndrome coronavirus 2 ; acetylcysteine ; alanine ; cell membranes ; cysteine ; disulfide bonds ; giant cells ; glutathione ; mutation ; pathogenicity ; research ; therapeutics
Language	English
Dates of publication	2022-0315
Size	p. 30-36.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	205723-2
ISSN	0006-291X ; 0006-291X
ISSN (online)	0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2022.01.106
Database	NAL-Catalogue (AGRICOLA)

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Z 71/706: Show issues
Z 3.8: Show issues

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Article ; Online: Overcoming antibody-resistant SARS-CoV-2 variants with bispecific antibodies constructed using non-neutralizing antibodies

Inoue, Tetsuya / Yamamoto, Yuichiro / Sato, Kaoru / Nakamura, Yuko / Shimizu, Yoshimi / Ogawa, Motohiko / Onodera, Taishi / Takahashi, Yoshimasa / Wakita, Takaji / Kaneko, Mika K / Fukasawa, Masayoshi / Kato, Yukinari / Noguchi, Kohji

bioRxiv

Abstract	A current challenge is the emergence of SARS-CoV-2 variants, such as BQ.1.1 and XBB.1.5, that can evade immune defenses, thereby limiting antibody drug effectiveness. Emergency-use antibody drugs, including the widely effective bebtelovimab, are losing their benefits. One potential approach to address this issue are bispecific antibodies which combine the targeting abilities of two antibodies with distinct epitopes. We engineered neutralizing bispecific antibodies in the IgG-scFv format from two initially non-neutralizing antibodies, CvMab-6 (which binds to the receptor-binding domain [RBD]) and CvMab-62 (targeting a spike protein S2 subunit epitope adjacent to the known anti-S2 antibody epitope). Furthermore, we created a bispecific antibody by incorporating the scFv of bebtelovimab with our anti-S2 antibody, demonstrating significant restoration of effectiveness against bebtelovimab-resistant BQ.1.1 variants. This study highlights the potential of neutralizing bispecific antibodies, which combine existing less effective anti-RBD antibodies with anti-S2 antibodies, to revive the effectiveness of antibody therapeutics compromised by immune-evading variants.
Keywords	covid19
Language	English
Publishing date	2023-10-27
Publisher	Cold Spring Harbor Laboratory
Document type	Article ; Online
DOI	10.1101/2023.10.26.564289
Database	COVID19

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