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[PMID]:29382836
[Au] Autor:Füzik T; Formanová P; Ruzek D; Yoshii K; Niedrig M; Plevka P
[Ad] Endereço:Structural Virology, Central European Institute of Technology, Masaryk University, Kamenice 753/5, 62500, Brno, Czech Republic.
[Ti] Título:Structure of tick-borne encephalitis virus and its neutralization by a monoclonal antibody.
[So] Source:Nat Commun;9(1):436, 2018 01 30.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Tick-borne encephalitis virus (TBEV) causes 13,000 cases of human meningitis and encephalitis annually. However, the structure of the TBEV virion and its interactions with antibodies are unknown. Here, we present cryo-EM structures of the native TBEV virion and its complex with Fab fragments of neutralizing antibody 19/1786. Flavivirus genome delivery depends on membrane fusion that is triggered at low pH. The virion structure indicates that the repulsive interactions of histidine side chains, which become protonated at low pH, may contribute to the disruption of heterotetramers of the TBEV envelope and membrane proteins and induce detachment of the envelope protein ectodomains from the virus membrane. The Fab fragments bind to 120 out of the 180 envelope glycoproteins of the TBEV virion. Unlike most of the previously studied flavivirus-neutralizing antibodies, the Fab fragments do not lock the E-proteins in the native-like arrangement, but interfere with the process of virus-induced membrane fusion.
[Mh] Termos MeSH primário: Anticorpos Neutralizantes/química
Anticorpos Antivirais/química
Vírus da Encefalite Transmitidos por Carrapatos/ultraestrutura
Fragmentos Fab das Imunoglobulinas/química
Proteínas Virais/química
Vírion/ultraestrutura
[Mh] Termos MeSH secundário: Anticorpos Neutralizantes/biossíntese
Anticorpos Antivirais/biossíntese
Linhagem Celular Tumoral
Microscopia Crioeletrônica
Vírus da Encefalite Transmitidos por Carrapatos/genética
Vírus da Encefalite Transmitidos por Carrapatos/metabolismo
Expressão Gênica
Seres Humanos
Concentração de Íons de Hidrogênio
Fragmentos Fab das Imunoglobulinas/biossíntese
Fusão de Membrana/genética
Neurônios/patologia
Neurônios/virologia
Domínios Proteicos
Multimerização Proteica
Proteínas Virais/genética
Proteínas Virais/metabolismo
Vírion/genética
Vírion/metabolismo
Internalização do Vírus
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antibodies, Neutralizing); 0 (Antibodies, Viral); 0 (Immunoglobulin Fab Fragments); 0 (Viral Proteins)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180307
[Lr] Data última revisão:
180307
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180201
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-018-02882-0


  2 / 11523 MEDLINE  
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[PMID]:29199990
[Au] Autor:Bzymek KP; Ma Y; Avery KN; Horne DA; Williams JC
[Ad] Endereço:Department of Molecular Medicine, Beckman Research Institute of City of Hope, 1710 Flower Street, Duarte, CA 91101, USA.
[Ti] Título:Meditope-Fab interaction: threading the hole.
[So] Source:Acta Crystallogr F Struct Biol Commun;73(Pt 12):688-694, 2017 Dec 01.
[Is] ISSN:2053-230X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Meditope, a cyclic 12-residue peptide, binds to a unique binding side between the light and heavy chains of the cetuximab Fab. In an effort to improve the affinity of the interaction, it was sought to extend the side chain of Arg8 in the meditope, a residue that is accessible from the other side of the meditope binding site, in order to increase the number of interactions. These modifications included an n-butyl and n-octyl extension as well as hydroxyl, amine and carboxyl substitutions. The atomic structures of the complexes and the binding kinetics for each modified meditope indicated that each extension threaded through the Fab `hole' and that the carboxyethylarginine substitution makes a favorable interaction with the Fab, increasing the half-life of the complex by threefold compared with the unmodified meditope. Taken together, these studies provide a basis for the design of additional modifications to enhance the overall affinity of this unique interaction.
[Mh] Termos MeSH primário: Cetuximab/metabolismo
Peptídeos Cíclicos/química
Peptídeos Cíclicos/metabolismo
[Mh] Termos MeSH secundário: Arginina/química
Sítios de Ligação
Cetuximab/química
Cristalografia por Raios X
Meia-Vida
Ligações de Hidrogênio
Fragmentos Fab das Imunoglobulinas/química
Fragmentos Fab das Imunoglobulinas/metabolismo
Modelos Moleculares
Conformação Proteica
Eletricidade Estática
Relação Estrutura-Atividade
Ressonância de Plasmônio de Superfície
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Immunoglobulin Fab Fragments); 0 (Peptides, Cyclic); 94ZLA3W45F (Arginine); PQX0D8J21J (Cetuximab)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171205
[St] Status:MEDLINE
[do] DOI:10.1107/S2053230X17016272


  3 / 11523 MEDLINE  
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[PMID]:28470954
[Au] Autor:Mendes JF; Amorim J; Calvão-Santos G
[Ad] Endereço:Department of Ophthalmology, Hospital de Braga, Braga, Portugal.
[Ti] Título:Systemic intravenous abciximab: a novel treatment for acute central retinal artery occlusion?
[So] Source:Acta Ophthalmol;96(1):e101-e102, 2018 02.
[Is] ISSN:1755-3768
[Cp] País de publicação:England
[La] Idioma:eng
[Mh] Termos MeSH primário: Anticorpos Monoclonais/uso terapêutico
Fragmentos Fab das Imunoglobulinas/uso terapêutico
Inibidores da Agregação de Plaquetas/uso terapêutico
Oclusão da Artéria Retiniana/tratamento farmacológico
[Mh] Termos MeSH secundário: Doença Aguda
Idoso de 80 Anos ou mais
Seres Humanos
Infusões Intravenosas
Masculino
Oclusão da Artéria Retiniana/diagnóstico
Oclusão da Artéria Retiniana/fisiopatologia
Acuidade Visual/efeitos dos fármacos
[Pt] Tipo de publicação:CASE REPORTS; LETTER
[Nm] Nome de substância:
0 (Antibodies, Monoclonal); 0 (Immunoglobulin Fab Fragments); 0 (Platelet Aggregation Inhibitors); X85G7936GV (abciximab)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180216
[Lr] Data última revisão:
180216
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1111/aos.13446


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[PMID]:27773473
[Au] Autor:Levinson KJ; Baranova DE; Mantis NJ
[Ad] Endereço:Division of Infectious Diseases, Wadsworth Center, New York State Department of Health, Albany, NY 12208, United States; Department of Biomedical Sciences, University at Albany, Albany, NY 12208, United States.
[Ti] Título:A monoclonal antibody that targets the conserved core/lipid A region of lipopolysaccharide affects motility and reduces intestinal colonization of both classical and El Tor Vibrio cholerae biotypes.
[So] Source:Vaccine;34(48):5833-5836, 2016 11 21.
[Is] ISSN:1873-2518
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Vibrio cholerae is the causative agent of cholera, an acute diarrheal disease that remains endemic in many parts of the world. The mechanisms underlying immunity to cholera remain poorly defined, though it is increasingly clear that protection is associated with antibodies against lipopolysaccharide (LPS). Here we report that ZAC-3, a monoclonal antibody against the core/lipid A region of V. cholerae LPS is a potent inhibitor of V. cholerae flagellum-based motility in viscous and liquid environments. ZAC-3 arrested motility of the classical Ogawa strain O395, as well as the El Tor Inaba strain C6706. In addition, we demonstrate, in the neonatal mouse model, that ZAC-3 IgG and Fab fragments significantly reduced the ability of both V. cholerae strains O395 and C6706 to colonize the intestinal epithelium, revealing the potential of antibodies against the core/lipid A to contribute to immunity across biotypes, possibly through a mechanism involving motility arrest.
[Mh] Termos MeSH primário: Anticorpos Monoclonais/imunologia
Cólera/microbiologia
Cólera/prevenção & controle
Lipídeo A/imunologia
Vibrio cholerae/imunologia
[Mh] Termos MeSH secundário: Animais
Animais Recém-Nascidos
Anticorpos Antibacterianos/imunologia
Anticorpos Monoclonais/administração & dosagem
Antígenos de Bactérias/imunologia
Técnicas de Tipagem Bacteriana
Modelos Animais de Doenças
Flagelos/efeitos dos fármacos
Flagelos/fisiologia
Fragmentos Fab das Imunoglobulinas/administração & dosagem
Fragmentos Fab das Imunoglobulinas/imunologia
Imunoglobulina G/administração & dosagem
Imunoglobulina G/imunologia
Mucosa Intestinal/imunologia
Mucosa Intestinal/microbiologia
Lipídeo A/química
Camundongos
Movimento
Vibrio cholerae/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Antibodies, Bacterial); 0 (Antibodies, Monoclonal); 0 (Antigens, Bacterial); 0 (Immunoglobulin Fab Fragments); 0 (Immunoglobulin G); 0 (Lipid A)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180206
[Lr] Data última revisão:
180206
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161025
[St] Status:MEDLINE


  5 / 11523 MEDLINE  
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[PMID]:29240734
[Au] Autor:Vazquez-Lombardi R; Nevoltris D; Luthra A; Schofield P; Zimmermann C; Christ D
[Ad] Endereço:Garvan Institute of Medical Research, Sydney, Australia.
[Ti] Título:Transient expression of human antibodies in mammalian cells.
[So] Source:Nat Protoc;13(1):99-117, 2018 Jan.
[Is] ISSN:1750-2799
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Recombinant expression of antibody molecules in mammalian cells offers important advantages over traditionally utilized bacterial expression, including glycosylation required for antibody functionality and markedly reduced levels of endotoxin contamination. Advances in transient mammalian expression systems enable high yields (>100 mg/liter) that now allow for effective recombinant antibody production at a reasonable cost. Here, we provide step-by-step protocols for the design and recombinant expression of full-length IgG antibodies and antibody-derived constructs (including Fab, Fc-fusions and bispecifics) in mammalian cells. Antibody constructs are designed by combining antibody variable domains, generated by phage display or derived from human/humanized monoclonals, with constant regions. The constructs are then expressed from mammalian vectors, secreted into culture media, purified by affinity chromatography and characterized by biolayer interferometry. This article provides detailed protocols, sequences and strategies that allow the expression and purification of endotoxin-free antibody reagents suitable for testing in animal models within a 3-week time frame.
[Mh] Termos MeSH primário: Anticorpos/genética
Engenharia de Proteínas/métodos
Proteínas Recombinantes/genética
Proteínas Recombinantes/isolamento & purificação
[Mh] Termos MeSH secundário: Animais
Anticorpos/metabolismo
Células Cultivadas
Cromatografia de Afinidade
Eletroforese em Gel de Poliacrilamida/métodos
Vetores Genéticos
Seres Humanos
Fragmentos Fab das Imunoglobulinas/genética
Fragmentos Fab das Imunoglobulinas/isolamento & purificação
Fragmentos Fab das Imunoglobulinas/metabolismo
Imunoglobulina G/genética
Imunoglobulina G/metabolismo
Interferometria/métodos
Mamíferos
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies); 0 (Immunoglobulin Fab Fragments); 0 (Immunoglobulin G); 0 (Recombinant Proteins)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171225
[Lr] Data última revisão:
171225
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171215
[St] Status:MEDLINE
[do] DOI:10.1038/nprot.2017.126


  6 / 11523 MEDLINE  
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[PMID]:28471362
[Au] Autor:Teplyakov A; Obmolova G; Malia TJ; Gilliland GL
[Ad] Endereço:Janssen Research and Development LLC, 1400 McKean Road, Spring House, PA 19477, USA.
[Ti] Título:Crystal structure of CD27 in complex with a neutralizing noncompeting antibody.
[So] Source:Acta Crystallogr F Struct Biol Commun;73(Pt 5):294-299, 2017 May 01.
[Is] ISSN:2053-230X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:CD27 is a T-cell and B-cell co-stimulatory glycoprotein of the tumor necrosis factor (TNF) receptor superfamily that is dependent on the availability of the TNF-like ligand CD70. Therapeutic approaches to treating autoimmune diseases and cancers with antagonistic and agonistic anti-CD27 monoclonal antibodies (mAbs), respectively, have recently been developed. Mouse anti-human CD27 mAb 2177 shows potency in neutralizing CD70-induced signaling; however, it does not block the binding of soluble CD70. To provide insight into the mechanism of action of the mAb, the crystal structure of the CD27 extracellular domain in complex with the Fab fragment of mAb 2177 was determined at 1.8 Šresolution. CD27 exhibits the assembly of cysteine-rich domains characteristic of the TNF receptor superfamily. The structure reveals a unique binding site of mAb 2177 at the edge of the receptor molecule, which allows the mAb to sterically block the cell-bound form of CD70 from reaching CD27 while leaving the ligand epitope clear. This mode of action suggests a potential dual use of mAb 2177 either as an antagonist or as an agonist.
[Mh] Termos MeSH primário: Anticorpos Monoclonais/química
Anticorpos Neutralizantes/química
Complexo Antígeno-Anticorpo/química
Ligante CD27/química
Fragmentos Fab das Imunoglobulinas/química
Membro 7 da Superfamília de Receptores de Fatores de Necrose Tumoral/química
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Animais
Anticorpos Monoclonais/genética
Anticorpos Neutralizantes/genética
Complexo Antígeno-Anticorpo/genética
Baculoviridae/genética
Baculoviridae/metabolismo
Sítios de Ligação
Ligante CD27/genética
Ligante CD27/imunologia
Clonagem Molecular
Cristalografia por Raios X
Expressão Gênica
Vetores Genéticos/química
Vetores Genéticos/metabolismo
Células HEK293
Seres Humanos
Fragmentos Fab das Imunoglobulinas/genética
Ligantes
Camundongos
Modelos Moleculares
Ligação Proteica
Conformação Proteica em Folha beta
Domínios e Motivos de Interação entre Proteínas
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/genética
Proteínas Recombinantes de Fusão/imunologia
Alinhamento de Sequência
Células Sf9
Spodoptera
Membro 7 da Superfamília de Receptores de Fatores de Necrose Tumoral/genética
Membro 7 da Superfamília de Receptores de Fatores de Necrose Tumoral/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Monoclonal); 0 (Antibodies, Neutralizing); 0 (Antigen-Antibody Complex); 0 (CD27 Ligand); 0 (CD70 protein, human); 0 (Immunoglobulin Fab Fragments); 0 (Ligands); 0 (Recombinant Fusion Proteins); 0 (Tumor Necrosis Factor Receptor Superfamily, Member 7)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171204
[Lr] Data última revisão:
171204
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1107/S2053230X17005957


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[PMID]:28984776
[Au] Autor:Sun B; Liu Z; Yin H; Wang T; Chen T; Yang S; Jiang Z
[Ad] Endereço:aDepartment of Cardiology, The Third Hospital of Hebei Medical University bDepartment of Epidemiology and Health Statistics, Center for Disease Control and Prevention of Hebei Province, Shijiazhuang, P.R. China.
[Ti] Título:Intralesional versus intracoronary administration of glycoprotein IIb/IIIa inhibitors during percutaneous coronary intervention in patients with acute coronary syndromes: A meta-analysis of randomized controlled trials.
[So] Source:Medicine (Baltimore);96(40):e8223, 2017 Oct.
[Is] ISSN:1536-5964
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Glycoprotein IIb/IIIa inhibitors (GPIs) have been regarded as an adjuvant regimen to deal with no-reflow. However, whether intralesional (IL) administration of GPIs improves myocardial reperfusion without increasing bleeding in patients with acute coronary syndrome (ACS) compared with intracoronary (IC) administration has not been well addressed. Our meta-analysis aimed to evaluate the efficacy and safety of IL versus IC administration of GPIs for patients with ACS during percutaneous coronary intervention. METHODS: We systematically searched Medline, Embase, the Cochrane Central Register of Controlled Trials, and Cambridge Scientific Abstracts from January 2007 to May 2017. Thrombolysis in Myocardial Infarction (TIMI) 3 flow, corrected TIMI frame count (CTFC), and complete ST-segment resolution (>70%) were selected as the primary outcomes. Major adverse cardiac events (MACEs) were the secondary outcome, and major bleeding complications were the safety outcome. Data analysis was conducted using the Review Manager 5.3 software. RESULTS: Six randomized controlled trials were included in our meta-analysis. Compared with IC, IL obtained better results in terms of TIMI grade 3 flow [odds ratio (OR) 2.29; 95% confidence intervals (CIs) 1.31-4.01; P = .004], CTFC [weighted mean difference (WMD) -4.63; 95% CI -8.82 to -0.43; P = .03], and complete ST-segment resolution (OR 1.55; 95% CI 1.12-2.14; P = .008). There was a trend toward decreased MACE in the IL administration groups, which was not of statistical significance (OR 0.63; 95% CI 0.30-1.31; P = .22). No significant difference was found between the two groups in terms of in-hospital major bleeding events (OR 2.52; 95% CI .66 to 9.62; P = .18). CONCLUSION: IL administration yielded favorable outcomes in terms of myocardial tissue reperfusion as evidenced by the improved TIMI flow grade, CTFC, complete ST-segment resolution, and decreased MACE without increasing in-hospital major bleeding events. The IL administration of GPIs can be recommended as the preferred regimen to guard against no-reflow.
[Mh] Termos MeSH primário: Síndrome Coronariana Aguda/tratamento farmacológico
Injeções Intra-Arteriais/métodos
Injeções Intralesionais/métodos
Intervenção Coronária Percutânea/métodos
Inibidores da Agregação de Plaquetas/administração & dosagem
[Mh] Termos MeSH secundário: Síndrome Coronariana Aguda/cirurgia
Anticorpos Monoclonais/administração & dosagem
Vasos Coronários
Sistema de Condução Cardíaco/efeitos dos fármacos
Seres Humanos
Fragmentos Fab das Imunoglobulinas/administração & dosagem
Reperfusão Miocárdica/métodos
Complexo Glicoproteico GPIIb-IIIa de Plaquetas/antagonistas & inibidores
Ensaios Clínicos Controlados Aleatórios como Assunto
Tirosina/administração & dosagem
Tirosina/análogos & derivados
[Pt] Tipo de publicação:JOURNAL ARTICLE; META-ANALYSIS; REVIEW
[Nm] Nome de substância:
0 (Antibodies, Monoclonal); 0 (Immunoglobulin Fab Fragments); 0 (Platelet Aggregation Inhibitors); 0 (Platelet Glycoprotein GPIIb-IIIa Complex); 42HK56048U (Tyrosine); GGX234SI5H (tirofiban); X85G7936GV (abciximab)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171012
[Lr] Data última revisão:
171012
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:171007
[St] Status:MEDLINE
[do] DOI:10.1097/MD.0000000000008223


  8 / 11523 MEDLINE  
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[PMID]:28919420
[Au] Autor:Syvänen S; Edén D; Sehlin D
[Ad] Endereço:Department of Public Health and Caring Sciences/Geriatrics, Uppsala University, Rudbeck Laboratory, SE-751 85 Uppsala, Sweden. Electronic address: stina.syvanen@pubcare.uu.se.
[Ti] Título:Cationization increases brain distribution of an amyloid-beta protofibril selective F(ab') fragment.
[So] Source:Biochem Biophys Res Commun;493(1):120-125, 2017 Nov 04.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Antibodies and fragments thereof are, because of high selectivity for their targets, considered as potential therapeutics and biomarkers for several neurological disorders. However, due to their large molecular size, antibodies/fragments do not easily penetrate into the brain. The aim of the present study was to improve the brain distribution via adsorptive-mediated transcytosis of an amyloid-beta (Aß) protofibril selective F(ab') fragment (F(ab') -h158). F(ab') -h158 was cationized to different extents and the specific and unspecific binding was studied in vitro. Next, cationized F(ab') -h158 was labelled with iodine-125 and its brain distribution and pharmacokinetics was studied in mice. Cationization did not alter the in vitro affinity to Aß protofibrils, but increased the unspecific binding somewhat. Ex vivo experiments revealed a doubling of brain concentrations compared with unmodified F(ab') -h158 and in vivo imaging with single photon emission computed tomography (SPECT) showed that the cationized F(ab') -h158, but not the unmodified F(ab') -h158 could be visualized in the brain. To conclude, cationization is a means to increase brain concentrations of therapeutic antibodies or fragments and may facilitate the use of antibodies/fragments as imaging biomarkers in the brain.
[Mh] Termos MeSH primário: Peptídeos beta-Amiloides/química
Peptídeos beta-Amiloides/metabolismo
Encéfalo/metabolismo
Carbodi-Imidas/química
Fragmentos Fab das Imunoglobulinas/química
Fragmentos Fab das Imunoglobulinas/metabolismo
[Mh] Termos MeSH secundário: Animais
Cátions/administração & dosagem
Reagentes para Ligações Cruzadas/química
Camundongos
Camundongos Transgênicos
Distribuição Tecidual/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (1-ethyl-3-(3-(diethylamino)propyl)carbodiimide); 0 (Amyloid beta-Peptides); 0 (Carbodiimides); 0 (Cations); 0 (Cross-Linking Reagents); 0 (Immunoglobulin Fab Fragments)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171023
[Lr] Data última revisão:
171023
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170919
[St] Status:MEDLINE


  9 / 11523 MEDLINE  
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[PMID]:28818634
[Au] Autor:Peng H; Nerreter T; Chang J; Qi J; Li X; Karunadharma P; Martinez GJ; Fallahi M; Soden J; Freeth J; Beerli RR; Grawunder U; Hudecek M; Rader C
[Ad] Endereço:Department of Immunology and Microbiology, The Scripps Research Institute, Jupiter, FL 33458, USA.
[Ti] Título:Mining Naïve Rabbit Antibody Repertoires by Phage Display for Monoclonal Antibodies of Therapeutic Utility.
[So] Source:J Mol Biol;429(19):2954-2973, 2017 Sep 15.
[Is] ISSN:1089-8638
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Owing to their high affinities and specificities, rabbit monoclonal antibodies (mAbs) have demonstrated value and potential primarily as basic research and diagnostic reagents, but, in some cases, also as therapeutics. To accelerate access to rabbit mAbs bypassing immunization, we generated a large naïve rabbit antibody repertoire represented by a phage display library encompassing >10 billion independent antibodies in chimeric rabbit/human Fab format and validated it by next-generation sequencing. Panels of rabbit mAbs selected from this library against two emerging cancer targets, ROR1 and ROR2, revealed high diversity, affinity, and specificity. Moreover, ROR1- and ROR2-targeting rabbit mAbs demonstrated therapeutic utility as components of chimeric antigen receptor-engineered T cells, further corroborating the value of the naïve rabbit antibody library as a rich and virtually unlimited source of rabbit mAbs.
[Mh] Termos MeSH primário: Anticorpos Monoclonais/isolamento & purificação
Fatores Imunológicos/isolamento & purificação
[Mh] Termos MeSH secundário: Animais
Anticorpos Monoclonais/uso terapêutico
Antígenos de Neoplasias/imunologia
Linhagem Celular Tumoral
Proliferação Celular
Citocinas/secreção
Testes Imunológicos de Citotoxicidade
Seres Humanos
Fragmentos Fab das Imunoglobulinas/genética
Fatores Imunológicos/uso terapêutico
Imunoterapia/métodos
Biblioteca de Peptídeos
Coelhos
Receptores Órfãos Semelhantes a Receptor Tirosina Quinase/imunologia
Proteínas Recombinantes/isolamento & purificação
Proteínas Recombinantes/uso terapêutico
Linfócitos T/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Monoclonal); 0 (Antigens, Neoplasm); 0 (Cytokines); 0 (Immunoglobulin Fab Fragments); 0 (Immunologic Factors); 0 (Peptide Library); 0 (Recombinant Proteins); EC 2.7.10.1 (ROR1 protein, human); EC 2.7.10.1 (ROR2 protein, human); EC 2.7.10.1 (Receptor Tyrosine Kinase-like Orphan Receptors)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171002
[Lr] Data última revisão:
171002
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170819
[St] Status:MEDLINE


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[PMID]:28784690
[Au] Autor:Stoyle CL; Stephens PE; Humphreys DP; Heywood S; Cain K; Bulleid NJ
[Ad] Endereço:Institute of Molecular, Cell and Systems Biology, CMVLS, University of Glasgow, Davidson Building, Glasgow G12 8QQ, U.K.
[Ti] Título:IgG light chain-independent secretion of heavy chain dimers: consequence for therapeutic antibody production and design.
[So] Source:Biochem J;474(18):3179-3188, 2017 Sep 07.
[Is] ISSN:1470-8728
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Rodent monoclonal antibodies with specificity towards important biological targets are developed for therapeutic use by a process of humanisation. This process involves the creation of molecules, which retain the specificity of the rodent antibody but contain predominantly human coding sequence. Here, we show that some humanised heavy chains (HCs) can fold, form dimers and be secreted even in the absence of a light chain (LC). Quality control of recombinant antibody assembly is thought to rely upon folding of the HC C 1 domain. This domain acts as a switch for secretion, only folding upon interaction with the LC C domain. We show that the secreted heavy-chain dimers contain folded C 1 domains and contribute to the heterogeneity of antibody species secreted during the expression of therapeutic antibodies. This subversion of the normal quality control process is dependent on the HC variable domain, is prevalent with engineered antibodies and can occur when only the Fab fragments are expressed. This discovery will have an impact on the efficient production of both humanised antibodies and the design of novel antibody formats.
[Mh] Termos MeSH primário: Anticorpos Monoclonais/biossíntese
Imunoglobulina G/metabolismo
Cadeias Pesadas de Imunoglobulinas/metabolismo
Cadeias Leves de Imunoglobulina/metabolismo
Proteínas Recombinantes/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Formação de Anticorpos
Especificidade de Anticorpos
Células CHO
Cricetulus
Seres Humanos
Fragmentos Fab das Imunoglobulinas/química
Fragmentos Fab das Imunoglobulinas/metabolismo
Imunoglobulina G/química
Cadeias Pesadas de Imunoglobulinas/química
Cadeias Leves de Imunoglobulina/química
Dobramento de Proteína
Proteínas Recombinantes/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Monoclonal); 0 (Immunoglobulin Fab Fragments); 0 (Immunoglobulin G); 0 (Immunoglobulin Heavy Chains); 0 (Immunoglobulin Light Chains); 0 (Recombinant Proteins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170809
[St] Status:MEDLINE
[do] DOI:10.1042/BCJ20170342



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