نتائج البحث - "Env, envelope"

1

Ceramide synthase 2 deletion decreases the infectivity of HIV-1

المؤلفون: Thomas O. Metz, Iris D. Zelnik, Lisa M. Bramer, Eric Barklis, R. Max Petty, Kent J. Bloodsworth, Jennifer E. Kyle, Ayna Alfadhli, Anthony H. Futerman, Robin Lid Barklis, Fikadu G. Tafesse, Hans C. Leier

المصدر: The Journal of Biological Chemistry

مصطلحات موضوعية: 0301 basic medicine, viruses, β-gal, β-galactosidase, HIV Infections, Biochemistry, chemistry.chemical_compound, NIH, National Institutes of Health, PIP2, phosphatidyl-4,5-bisphosphate, BME, β-mercaptoethanol, Sphingosine N-Acyltransferase, Ceramide synthase, CA, capsid, Infectivity, biology, Chemistry, Ceramide synthase 2, virus diseases, PS, phosphatidylserine, Cell biology, Vesicular stomatitis virus, PM, plasma membrane, PrGag, precursor Gag, SL, sphingolipid, Sphingomyelin, Research Article, Ceramide, CT, cytoplasmic tail, VSV, vesicular stomatitis virus, HexCer, hexosylceramide, Ceramides, 03 medical and health sciences, G, glycoprotein, fusion protein, Humans, ceramide, Molecular Biology, 030102 biochemistry & molecular biology, Tumor Suppressor Proteins, Membrane Proteins, HIV, Cell Biology, Virus Internalization, HEK293T, human embryonic kidney 293T, biology.organism_classification, Fusion protein, Sphingolipid, ceramide synthase, 030104 developmental biology, HEK293 Cells, CerS, ceramide synthase, Env, envelope, HIV-1, sphingolipid, Gene Deletion

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d95d3b26a57ef253f47dc2293f746c62Test
https://pubmed.ncbi.nlm.nih.gov/33515546Test

2

X-ray structures of the post-fusion 6-helix bundle of the human syncytins and their functional implications

المؤلفون: Julian Buchrieser, Marie-Christine Vaney, Marija Backovic, Eduard Baquero, Bruno Baron, Katinka Ruigrok, Patrick England, Jan Hellert, Félix A. Rey, Olivier Schwartz

المساهمون: Virologie Structurale - Structural Virology, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Université Paris Descartes - Paris 5 (UPD5), Virus et Immunité - Virus and immunity, Vaccine Research Institute (VRI), Université Paris-Est Créteil Val-de-Marne - Paris 12 (UPEC UP12), This work was funded by the European Research council (ERC ‘CelCelFus’ grant #340371) awarded to F.A.R, and recurrent funding from the Institut Pasteur (IP) and CNRS, We thank Ahmed Haouz and staff at the IP core facility for protein crystallization, and staff at the Proxima-2 beamline at the SOLEIL synchrotron for assistance with data collection and processing. We also thank Ignacio Fernandez for helpful discussions and critical reading of the manuscript, Delphine Brun for technical assistance, and Etienne Simon-Loriere for discussions and help with phylogenetic analyses., Centre National de la Recherche Scientifique (CNRS)-Institut Pasteur [Paris], Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Virus et Immunité - Virus and immunity (CNRS-UMR3569), Vaccine Research Institute [Créteil, France] (VRI), Virologie Structurale, Virus et Immunité

المصدر: Journal of Molecular Biology
Journal of Molecular Biology, Elsevier, 2019, pp.S0022-2836(19)30616-3. ⟨10.1016/j.jmb.2019.10.020⟩
Journal of Molecular Biology, 2019, pp.S0022-2836(19)30616-3. ⟨10.1016/j.jmb.2019.10.020⟩

مصطلحات موضوعية: TM, transmembrane subunit, WT, wild type, Models, Molecular, Protein Conformation, HR, heptad repeat, Pregnancy Proteins, Crystallography, X-Ray, 0302 clinical medicine, Viral Envelope Proteins, MPER, membrane-proximal external region, Aa, amino acid, PDB, protein data bank, TMA, transmembrane anchor, GFP, green fluorescent protein, chemistry.chemical_classification, Helix bundle, 0303 health sciences, Syncytin, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], Transmembrane protein, 3. Good health, Cell biology, HIV, human immunodeficiency virus, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], Env, envelope protein, TME, ectodomain of the transmembrane subunit, Syn1, human syncytin-1, [SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology, HTLV, human T-lymphotropic virus, EBOV, Ebola virus, Structural biology, Fusion protein, SU, surface subunit, BLV, bovine leukemia virus, MPMV, Mason–Pfizer monkey virus, MARV, Marburg virus, Protein subunit, Membrane fusion, SEM, standard error of the mean value, Article, Syn2, human syncytin-2, TEV, tobacco etch virus, ER, endoplasmic reticulum, 03 medical and health sciences, Humans, HERV, human endogenous retrovirus, Protein Interaction Domains and Motifs, Amino Acid Sequence, Molecular Biology, 030304 developmental biology, X-ray crystallography, Lipid bilayer fusion, Gene Products, env, Membrane protein, chemistry, SP, signal peptide, SEC, size exclusion chromatography, Gammaretrovirus, Glycoprotein, 030217 neurology & neurosurgery, 6HB, six-helix bundle

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::813f60ae76087870391779aea60f82cdTest
https://hal.archives-ouvertes.fr/hal-02375766Test

3

Invaplex functions as an intranasal adjuvant for subunit and DNA vaccines co-delivered in the nasal cavity of nonhuman primates

المؤلفون: Robert W. Kaminski, James Blanchard, Robert L. Wilson, Pamela A. Kozlowski, Anna Aldovini, Edwin V. Oaks, Morgan Singletary, Jeremy V. Camp

المصدر: Vaccine: X, Vol 8, Iss, Pp 100105-(2021)
Vaccine: X

مصطلحات موضوعية: Mucosal adjuvant, viruses, medicine.medical_treatment, T cell, Respiratory tract, medicine.disease_cause, NS, nasal secretions, DNA vaccination, Reproductive, medicine, CVS, cervicovaginal secretions, IM, intramuscular, NHP, nonhuman primates, Cytotoxic T cell, Shigella vaccine, Th, T helper, General Veterinary, General Immunology and Microbiology, biology, business.industry, Ad, adenovirus, Public Health, Environmental and Occupational Health, virus diseases, RC581-607, Simian immunodeficiency virus, Virology, RS, rectal secretions, S-IgA, secretory IgA, Infectious Diseases, medicine.anatomical_structure, Regular paper, Env, envelope, biology.protein, HIV/AIDS, Molecular Medicine, Nasal administration, Immunologic diseases. Allergy, Antibody, IN, intranasal, business, Adjuvant, IgA, ICS, intracellular cytokine staining

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9d3c8f3f7bd566a1ceba1065278e47d2Test
https://doi.org/10.1016/j.jvacx.2021.100105Test

4

Brief introduction of current technologies in isolation of broadly neutralizing HIV-1 antibodies

المؤلفون: Qian Qian, Jerica Lenberg, Wan Liu, Zehua Sun, Yilin Wang, Lixin Yan, Dandan Zhu, Shiqiang Lu, Jiansong Tang, Kao Wu

المصدر: Virus Research

مصطلحات موضوعية: 0301 basic medicine, Monoclonal antibody, Cancer Research, Technology, Isolation (health care), medicine.drug_class, Human immunodeficiency virus (HIV), HIV Infections, HIV Antibodies, medicine.disease_cause, Neutralization, Article, 03 medical and health sciences, Acquired immunodeficiency syndrome (AIDS), bnmAbs, broadly neutralizing monoclonal antibodies, Neutralization Tests, Virology, Pandemic, medicine, Animals, Humans, Single-cell sorting, bNAbs, broadly neutralizing antibodies, biology, Phage/yeast display, medicine.disease, Antibodies, Neutralizing, 030104 developmental biology, Infectious Diseases, Immunization, Immunology, Env, envelope, biology.protein, HIV-1, Immunologic Techniques, hbNAbs, human broadly neutralizing antibodies, Antibody

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::410b42d7284970347f8548121cc3ef07Test
http://europepmc.org/articles/PMC7114535Test

5

Protein and glycan mimicry in HIV vaccine design

المؤلفون: Max Crispin, Gemma E. Seabright, Katherine Doores, Dennis R. Burton

المصدر: Journal of Molecular Biology
Seabright, G E, Doores, K J, Burton, D R & Crispin, M 2019, ' Protein and glycan mimicry in HIV vaccine design ', Journal of Molecular Biology, vol. 431, no. 12, https://doi.org/10.1016/j.jmb.2019.04.016Test, pp. 2223-2247 . https://doi.org/10.1016/j.jmb.2019.04.016Test

مصطلحات موضوعية: Models, Molecular, GnT I, N-acetylglucosaminyltransferase I, viruses, HIV Infections, Epitope, HIV-1, human immunodeficiency virus type 1, chemistry.chemical_compound, Epitopes, 0302 clinical medicine, TM, transmembrane region, MPER, membrane proximal external region, Structural Biology, BCR, B cell receptor, Env, envelope spike, antibodies, UFO, uncleaved prefusion-optimized, CD4bs, CD4 binding site, LOS, lipooligosaccharides, HIV vaccine, TF, transmitted/founder, HR1/2, heptad repeat 1 or 2, AIDS Vaccines, 0303 health sciences, GlcN, glucosamine, biology, human immunodeficiency virus, Immunogenicity, env Gene Products, Human Immunodeficiency Virus, Glc, glucose, GlcNAc, N-acetylglucosamine, 3. Good health, CDR, complementarity-determining regions, NFL, native flexibly linked, Antibody, Glycan, CT, cytoplasmic tail, PBMC, peripheral blood mononuclear cell, Glycosylation, nAb(s), neutralizing antibody(ies), cGMP, current good manufacturing practices, Fuc, fucose, glycosylation, AIDS, acquired immune deficiency syndrome, SC, single-chain, Computational biology, CXCR4, C-X-C chemokine receptor type 4, CHO, Chinese hamster ovary, KDO, 2-keto-3-deoxy-D-manno-octulosonic acid, Virus, Article, bnAb(s), broadly neutralizing antibody(ies), ER, endoplasmic reticulum, 03 medical and health sciences, HEK, human embryonic kidney, Polysaccharides, Humans, structure, Molecular Biology, 030304 developmental biology, EM, electron microscopy, HCDR3, third heavy-chain complementarity-determining regions, Molecular Mimicry, Man, mannose, CCR5, C-C chemokine receptor type 5, gl-bnAb(s), germline-bnAb(s), Viral membrane, Antibodies, Neutralizing, PNGS, potential N-glycosylation sites, IMP, intrinsic mannose patch, Gal, galactose, chemistry, SP, signal peptide, biology.protein, HIV-1, PNS, peripheral nervous system, vaccinology, TAMP, trimer-associated mannose patch, α-man I and II, α-mannosidase I and II, 030217 neurology & neurosurgery, Neu5Ac, N-acetylneuraminic acid (sialic acid)