المؤلفون: Christian Haupt

المصدر: Hemato, Vol 2, Iss 32, Pp 505-514 (2021)

مصطلحات موضوعية: cryo electron microscopy, Chemistry, macromolecular substances, AL fibrils, medicine.disease, Amyloid fibril, Fibril, Fibril formation, AL amyloidosis, medicine, Molecular mechanism, Biophysics, Medicine, In patient

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0b07b08fe79f438087062dedb40df8e7Test
https://doi.org/10.3390/hemato2030032Test

المؤلفون: Bouke P. C. Hazenberg, Stefan Schoenland, Bernd Reif, Tejaswini Pradhan, Christian Haupt, M. Faendrich, J. Schoenfelder, Johan Bijzet, Ute Hegenbart, P. B. Pfeiffer

المساهمون: Translational Immunology Groningen (TRIGR)

المصدر: Amyloid, 28(4), 243-251. Taylor & Francis Ltd

مصطلحات موضوعية: PROTEINS, medicine.medical_treatment, proteolytic stability, macromolecular substances, Fibril, prion, Amyloid disease, Internal Medicine, medicine, Serum amyloid A, protein misfolding, immunoglobulin light chain, GLYCOSAMINOGLYCANS, chemistry.chemical_classification, Protease, biology, Chemistry, serum amyloid A, Amyloid fibril, TRANSTHYRETIN, In vitro, POLYMORPHISM, Amino acid, Transthyretin, Amyloid structure, biology.protein, Biophysics, Protein folding, Ex vivo

وصف الملف: application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e229dee1268b3cc10a97beb6344d5b95Test
https://doi.org/10.1080/13506129.2021.1960501Test

المؤلفون: Thomas Heerde, Matthies Rennegarbe, Alexander Biedermann, Dilan Savran, Peter B. Pfeiffer, Manuel Hitzenberger, Julian Baur, Ioana Puscalau-Girtu, Martin Zacharias, Nadine Schwierz, Christian Haupt, Matthias Schmidt, Marcus Fändrich

المصدر: Nature Communications
Nature Communications, Vol 13, Iss 1, Pp 1-8 (2022)

مصطلحات موضوعية: DDC 540 / Chemistry & allied sciences, Amyloid, Prions, Protein Conformation, Science, Genetic Vectors, General Physics and Astronomy, Gene Expression, Mice, Transgenic, macromolecular substances, Molecular Dynamics Simulation, General Biochemistry, Genetics and Molecular Biology, Article, Mice, DDC 570 / Life sciences, Cryoelectron microscopy, ddc:570, Escherichia coli, Animals, Humans, Protein Isoforms, ddc:530, Cloning, Molecular, Serum Amyloid A Protein, Multidisciplinary, Protein Stability, Cryoelectron Microscopy, food and beverages, General Chemistry, Amyloidosis, Molecular conformation, Recombinant Proteins, ddc:540, Proteolysis, Prion, Protein aggregation, Endopeptidase K

وصف الملف: application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29953e768386712fcd255c923e97f72fTest
http://europepmc.org/articles/PMC8748726Test

المؤلفون: Sara Karimi-Farsijani, Stefanie Huhn, Marcus Fändrich, Lynn Radamaker, Julian David Baur, Giada Andreotti, Paul Walther, Matthias Neumann, Sarah Schreiner, Volker Schmidt, Clarissa Read, Matthias Schmidt, Ute Hegenbart, Christian Haupt, Stefan Schönland, Raoul Motika, Sebastian Wiese, Natalie Berghaus

المصدر: Nature Communications
Nature Communications, Vol 12, Iss 1, Pp 1-11 (2021)

مصطلحات موضوعية: INVOLVEMENT, Protein Folding, Glycosylation, PREDICTION, Protein Conformation, General Physics and Astronomy, Protein aggregation, Aggregation (Chemistry), Immunoglobulin light-chain amyloidosis, chemistry.chemical_compound, DDC 570 / Life sciences, FIBRILS, Cryoelectron microscopy, Immunoglobulin Light-chain Amyloidosis, Multidisciplinary, Strukturbiologie, Immunglobuline, lipids (amino acids, peptides, and proteins), Structural biology, GERMLINE GENE, Amyloid, Science, Somatic hypermutation, Immunoglobulins, macromolecular substances, Fibril, Immunoglobulin light chain, DEPOSITS, General Biochemistry, Genetics and Molecular Biology, Article, ddc:570, AL amyloidosis, medicine, ddc:610, LAMBDA-III, Immunoglobulin light chains, General Chemistry, Amyloidose, medicine.disease, carbohydrates (lipids), chemistry, Mutation, Biophysics, VISUALIZATION, Cryoelectron tomography, DDC 610 / Medicine & health

وصف الملف: application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ebd3e500479b0af12a5673f1585a4e06Test
https://pubmed.ncbi.nlm.nih.gov/34741031Test

المؤلفون: Stefan Schönland, Matthias Schmidt, Akanksha Bansal, Ute Hegenbart, Marcus Fändrich, Christian Haupt, Julian David Baur, Lynn Radamaker, Stefanie Huhn

المصدر: Nature Communications
Nature Communications, Vol 12, Iss 1, Pp 1-10 (2021)

مصطلحات موضوعية: Amyloid, Cryo-electron microscopy, Protein Conformation, Science, Sequence (biology), macromolecular substances, Immunoglobulin light chain, Fibril, Article, Protein Aggregates, Variable domain, AL amyloidosis, medicine, Humans, Immunoglobulin Light-chain Amyloidosis, Amino Acid Sequence, Chemistry, Cryoelectron Microscopy, Middle Aged, Amyloid fibril, medicine.disease, Mutation, Biophysics, Fatal disease, Female, Immunoglobulin Light Chains, Protein aggregation, Structural biology

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3e1bec955e12e28b5adc33371c1b5abTest
https://pubmed.ncbi.nlm.nih.gov/33558536Test

المؤلفون: Marie-Theres Vielberg, Karl-Heinz Gührs, Andreas Schmidt, Rolf Koehler, Stefan Schönland, Marcus Fändrich, Angelika Schierhorn, Matthias Schmidt, William Close, Hauke Lilie, Falk Liberta, Christian Haupt, Ute Hegenbart, Karthikeyan Annamalai, Michael Groll

المصدر: Angewandte Chemie. 129:7618-7622

مصطلحات موضوعية: 0301 basic medicine, Protein Folding, Amyloid, macromolecular substances, Fibril, 010402 general chemistry, 01 natural sciences, Catalysis, Mass Spectrometry, Protein Structure, Secondary, Amyloid beta-Protein Precursor, Mice, 03 medical and health sciences, 0302 clinical medicine, AA amyloidosis, Microscopy, Electron, Transmission, X-Ray Diffraction, In vivo, medicine, Amyloid precursor protein, Animals, Humans, Amino Acid Sequence, biology, Chemistry, Amyloidosis, Myocardium, General Chemistry, General Medicine, medicine.disease, 0104 chemical sciences, 030104 developmental biology, Biochemistry, Adipose Tissue, biology.protein, Biophysics, Protein folding, Electrophoresis, Polyacrylamide Gel, Peptides, Protein Processing, Post-Translational, 030217 neurology & neurosurgery, Fibril morphology, Spleen

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98f03a22a9169be54f89d632b09dfd9eTest
https://doi.org/10.1002/ange.201701761Test

المؤلفون: Uwe Horn, Julia Linder, Marius Kollmer, Volker Schmidt, Falk Liberta, Tatiana Syrovets, Marcus Fändrich, Thomas Simmet, Katrin Meinhardt, Per Westermark, Gunilla T. Westermark, Matthias Schmidt, Paul Walther, Liesa Heinrich, Christian Haupt, Melanie Wulff, Lisa Handl, Cornelia Loos

المصدر: Proceedings of the National Academy of Sciences. 113:5604-5609

مصطلحات موضوعية: 0301 basic medicine, Amyloid, Electron Microscope Tomography, Lipid Bilayers, Nanotechnology, macromolecular substances, Fibril, Mice, 03 medical and health sciences, medicine, Animals, Serum amyloid A, Lipid bilayer, Cells, Cultured, Serum Amyloid A Protein, Multidisciplinary, Chemistry, Amyloidosis, Biological Sciences, medicine.disease, Lipids, 030104 developmental biology, Electron tomography, Biophysics, Female

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ee701dcd05797d4e35f4d131634f06d1Test
https://doi.org/10.1073/pnas.1523496113Test

المؤلفون: Christoph Parthier, Isabel Morgado, Senthil Kumar, Milton T. Stubbs, Christian Haupt, Marcus Fändrich, Magdalena Bereza, Peter Hortschansky, Uwe Horn

المصدر: Journal of Molecular Biology. 405:341-348

مصطلحات موضوعية: Amyloid, Amyloid beta-Peptides, Protein Conformation, Chemistry, Molecular Sequence Data, Static Electricity, P3 peptide, macromolecular substances, Plasma protein binding, Complementarity determining region, Crystallography, X-Ray, Fibril, Complementarity Determining Regions, Antibodies, Protein structure, Biochemistry, Structural Biology, Static electricity, Humans, Amino Acid Sequence, Molecular Biology, Peptide sequence, Protein Binding

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33066047be27fdddfba7aab4de8729d0Test
https://doi.org/10.1016/j.jmb.2010.10.059Test

المؤلفون: Gerald P. Gellermann, Karl-Jürgen Halbhuber, Christoph Röcken, Peter Hortschansky, Uwe Horn, Carsten Sachse, Marcus Fändrich, Jürgen Götz, Michael Brodhun, Christian Haupt, Jessica Meinhardt, Ralf P. Friedrich, Gernot Habicht, Karin Wieligmann

المصدر: Proceedings of the National Academy of Sciences of the United States of America, 104(49): 19232-19237

مصطلحات موضوعية: Amyloid, macromolecular substances, Biology, Fibril, Epitope, Antibodies, Epitopes, Protein structure, Peptide Library, medicine, Animals, Humans, Peptide library, Multidisciplinary, Amyloid beta-Peptides, Neurodegeneration, P3 peptide, Biological Sciences, medicine.disease, protein folding, prion, neurodegeneration, Peptide Fragments, Recombinant Proteins, Protein Structure, Tertiary, Biochemistry, Biophysics, Protein folding, Camelids, New World

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4858a1d5b75a6a97586973118b69c7bfTest
https://europepmc.org/articles/PMC2148273Test/