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1. Full Text Reducing Macro‐ and Microheterogeneity of N‐Glycans Enables the Crystal Structure of the Lectin and EGF‐Like Domains of Human L‐Selectin To Be Solved at 1.9 Å Resolution
by Wedepohl, Stefanie and Dernedde, Jens and Vahedi‐Faridi, Ardeschir and Tauber, Rudolf and Saenger, Wolfram and Bulut, Haydar
Chembiochem : a European journal of chemical biology, ISSN 1439-4227, 07/2017, Volume 18, Issue 13, pp. 1338 - 1345
glycosylation | L-selectin | glycoproteins | crystal growth | mutagenesis | Calcium - metabolism | Humans | Crystallography, X-Ray | L-Selectin - genetics | Lectins, C-Type - genetics | Calcium - chemistry | Lectins, C-Type - chemistry | L-Selectin - metabolism | Lectins, C-Type - metabolism | Epidermal Growth Factor - chemistry | Cloning, Molecular | HEK293 Cells | Polysaccharides - chemistry | Protein Domains | Protein Interaction Domains and Motifs | Binding Sites | Recombinant Proteins - metabolism | Gene Expression | Protein Structure, Secondary | Epidermal Growth Factor - genetics | Models, Molecular | Recombinant Proteins - chemistry | Epidermal Growth Factor - metabolism | Glycosylation | Recombinant Proteins - genetics | Polysaccharides - metabolism | L-Selectin - chemistry | Protein Binding | Mutation | Index Medicus
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2. Full Text Aquaporin-7: A Dynamic Aquaglyceroporin With Greater Water and Glycerol Permeability Than Its Bacterial Homolog GlpF
by Moss, Fraser J and Mahinthichaichan, Paween and Lodowski, David T and Kowatz, Thomas and Tajkhorshid, Emad and Engel, Andreas and Boron, Walter F and Vahedi-Faridi, Ardeschir
Frontiers in physiology, ISSN 1664-042X, 06/2020, Volume 11, pp. 728 - 728
Life Sciences & Biomedicine | Physiology | Science & Technology | Glycerin | Molecular dynamics | Glycerol | Permeability | Aquaporins | atomic structure | Xenopus oocytes | osmotic water permeability | AQP7 | glycerol facilitator | molecular dynamics simulation
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3. Full Text Conformational changes within the HLA‐A1:MAGE‐A1 complex induced by binding of a recombinant antibody fragment with TCR‐like specificity
by Kumar, Pravin and Vahedi‐Faridi, Ardeschir and Saenger, Wolfram and Ziegler, Andreas and Uchanska‐Ziegler, Barbara
Protein science, ISSN 0961-8368, 01/2009, Volume 18, Issue 1, pp. 37 - 49
ligand‐induced conformational changes | HLA‐A1 | T cell receptor | peptide‐restricted antibody | X‐ray crystallography | X-ray crystallography | Ligand-induced conformational changes | HLA-A1 | Peptide-restricted antibody | Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Melanoma-Specific Antigens | Humans | HLA-A1 Antigen - chemistry | Crystallography, X-Ray | Neoplasm Proteins - chemistry | Receptors, Antigen, T-Cell | Recombinant Fusion Proteins - chemistry | Neoplasm Proteins - metabolism | Antigens, Neoplasm - chemistry | Recombinant Fusion Proteins - metabolism | Antigens, Neoplasm - metabolism | Ligands | Protein Conformation | HLA-A1 Antigen - metabolism | Protein Binding - physiology | Index Medicus | ligand-induced conformational changes | peptide-restricted antibody
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4. Full Text Structural Basis for T Cell Alloreactivity among Three HLA-B14 and HLA-B27 Antigens
by Pravin Kumar and Ardeschir Vahedi-Faridi and Wolfram Saenger and Elena Merino and José A. López de Castro and Barbara Uchanska-Ziegler and Andreas Ziegler
The Journal of biological chemistry, ISSN 0021-9258, 10/2009, Volume 284, Issue 43, pp. 29784 - 29797
Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | HLA-B Antigens - chemistry | Peptides - chemistry | Humans | Peptides - immunology | HLA-B Antigens - immunology | Crystallography, X-Ray | T-Lymphocytes, Cytotoxic | Cross Reactions - immunology | Cathepsin A - chemistry | Viral Matrix Proteins - chemistry | Protein Structure, Quaternary | HLA-B27 Antigen - immunology | Viral Matrix Proteins - immunology | Cathepsin A - immunology | HLA-B27 Antigen - chemistry | Antigen presentation | LMP2 protein | Cross-reactivity | Amino acids | Cytotoxicity | Histocompatibility antigen HLA | Lymphocytes T | Carboxypeptidase C | Histocompatibility | Crystal structure | Index Medicus | Protein Structure and Folding
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5. Full Text Molecular basis for SH3 domain regulation of F-BAR—mediated membrane deformation
by Yijian Rao and Qingjun Ma and Ardeschir Vahedi-Faridi and Anna Sundborger and Arndt Pechstein and Dmytro Puchkov and Lin Luo and Oleg Shupliakov and Wolfram Saenger and Volker Haucke and Gottfried Schatz
Proceedings of the National Academy of Sciences - PNAS, ISSN 0027-8424, 5/2010, Volume 107, Issue 18, pp. 8213 - 8218
Proteins | Endocytosis | Neurons | Crystals | Bending | Cell membranes | Dimers | Physiological regulation | Liposomes | P branes | Membrane bending | Dynamin | Syndapin | Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Protein Structure, Tertiary | Amino Acid Sequence | Carrier Proteins - ultrastructure | Cercopithecus aethiops | Molecular Sequence Data | Crystallography, X-Ray | Cell Membrane - ultrastructure | Microscopy, Electron | src Homology Domains | Cell Membrane - chemistry | Animals | Carrier Proteins - chemistry | COS Cells | Cellular control mechanisms | Research | Properties | Structure | Observations | Guanosine triphosphatase | Methods | Membranes | Cells | Binding sites | Cell adhesion & migration | Index Medicus | membrane bending | Biological Sciences | endocytosis | syndapin | dynamin | Medicin och hälsovetenskap
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6. Full Text Regulation of Synaptic Vesicle Recycling by Complex Formation between Intersectin 1 and the Clathrin Adaptor Complex AP2
by Arndt Pechstein and Jelena Bacetic and Ardeschir Vahedi-Faridi and Kira Gromova and Anna Sundborger and Nikolay Tomlin and Georg Krainer and Olga Vorontsova and Johannes G. Schäfer and Simen G. Owe and Michael A. Cousin and Wolfram Saenger and Oleg Shupliakov and Volker Haucke and Pietro de Camilli
Proceedings of the National Academy of Sciences - PNAS, ISSN 0027-8424, 3/2010, Volume 107, Issue 9, pp. 4206 - 4211
Axons | Endocytosis | Neurons | Antibodies | Cell membranes | Recycling | Physiological regulation | Appendages | Scaffolds | Synapses | Scaffolding proteins | Appendage | Synapse | Synaptojanin | Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Amino Acid Sequence | Synaptic Vesicles - metabolism | Models, Molecular | Molecular Sequence Data | Adaptor Proteins, Vesicular Transport - metabolism | Adaptor Protein Complex 2 - chemistry | src Homology Domains | Lampreys | Nerve Tissue Proteins - metabolism | Sequence Homology, Amino Acid | Adaptor Protein Complex 2 - metabolism | Animals | Adaptor Proteins, Vesicular Transport - chemistry | Phosphoric Monoester Hydrolases - metabolism | Binding Sites | Synaptic vesicles | Clathrin | Chemical properties | Research | Proteins | Membranes | Peptides | Cellular biology | Index Medicus | Biological Sciences | endocytosis | synapse | scaffolding proteins | synaptojanin | appendage | Medicin och hälsovetenskap
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7. Full Text 3D imaging and quantitative analysis of small solubilized membrane proteins and their complexes by transmission electron microscopy
by Vahedi-Faridi, Ardeschir and Jastrzebska, Beata and Palczewski, Krzysztof and Engel, Andreas
Journal of electron microscopy, ISSN 0022-0744, 02/2013, Volume 62, Issue 1, pp. 95 - 107
Negative staining | Membrane protein complex | Rhodopsin-transducin complex | Scanning transmission electron microscopy | 3D-electron microscopy | Detergent belt | Microscopy | Technology | Science & Technology | Gene Expression Regulation, Fungal | Rhodopsin - ultrastructure | Protein Structure, Secondary | Microscopy, Electron, Transmission - methods | Aquaporins - chemistry | Imaging, Three-Dimensional - methods | Negative Staining - methods | Transducin - chemistry | Transducin - ultrastructure | Aquaporins - ultrastructure | Membrane Proteins - chemistry | Membrane Proteins - ultrastructure | Pichia - genetics | Detergents - analysis | Cryoelectron Microscopy - methods | Evaluation Studies as Topic | Rhodopsin - chemistry | Scanning electron microscopy | Membranes | Glycoproteins | Transmission electron microscopy | Three dimensional imaging | Index Medicus | Reviews | detergent belt | scanning transmission electron microscopy | rhodopsin-transducin complex | negative staining | membrane protein complex
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8. Full Text The High-Resolution Structure of Activated Opsin Reveals a Conserved Solvent Network in the Transmembrane Region Essential for Activation
by Blankenship, Elise and Vahedi-Faridi, Ardeschir and Lodowski, David T and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Structure (London), ISSN 0969-2126, 12/2015, Volume 23, Issue 12, pp. 2358 - 2364
Biochemistry & Molecular Biology | Biophysics | Life Sciences & Biomedicine | Science & Technology | Cell Biology | Amino Acid Sequence | GTP-Binding Proteins - chemistry | Hydrogen Bonding | Water - chemistry | Molecular Sequence Data | Protein Binding | Rhodopsin - metabolism | Binding Sites | GTP-Binding Proteins - metabolism | Rhodopsin - chemistry | Rhodopsin | Hydrogen | Analysis | Chromophores | G proteins | Hydrogen bonding | Protein binding | Medical colleges | Bonds | Index Medicus
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9. Full Text Improvement of crystal quality by time controlled annealing
by Stojanoff, V and Vahedi-Faridi, A and Yeh, J. I
Acta crystallographica. Section A, Foundations of crystallography, ISSN 0108-7673, 08/2005, Volume 61, Issue a1, pp. c9 - c9
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10. Full Text Generation of Flp-in
by Soler, DC and Young, AE and Vahedi-Faridi and McCormick, TS
BioTechniques, ISSN 0736-6205, 07/2018, Volume 65, Issue 1, pp. 41 - 46
Lec 3.2.8.1 | Flp-in | CHO | DG44 | protein expression
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11. Full Text Generation of Flp-intm-ready DG44 and Lec 3.2.8.1 CHO cell lines for quick and easy constitutive protein expression
by Soler, DC and Young, AE and Vahedi-Faridi, A and McCormick, TS
BioTechniques, ISSN 0736-6205, 07/2018, Volume 65, Issue 1, pp. 41 - 46
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12. Full Text Generation of Flp-in tm -ready DG44 and Lec 3.2.8.1 CHO cell lines for quick and easy constitutive protein expression
by Soler, D.C and Young, A.E and Vahedi-Faridi, A and McCormick, T.S
BioTechniques, ISSN 0736-6205, 07/2018, Volume 65, Issue 1, pp. 41 - 46
Flp-in | Lec 3.2.8.1 | Protein expression | CHO | DG44
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13. Full Text Reducing Macro- and Microheterogeneity of N-Glycans Enables the Crystal Structure of the Lectin and EGF-Like Domains of Human L-Selectin To Be Solved at 1.9ￃ Resolution
by Stefanie Wedepohl and Jens Dernedde and Ardeschir Vahedi-Faridi and Rudolf Tauber and Wolfram Saenger and Haydar Bulut
Chembiochem : a European journal of chemical biology, ISSN 1439-4227, 07/2017, Volume 18, Issue 13, p. 1338
Calcium | Crystals | Mannose | Glycosylation | Leukocytes | N-glycans | Glycan | Polysaccharides | Epidermal growth factor | Diffraction | Calcium-binding protein | Selectins | Lectins | L-selectin | Mutation | Binding sites | P-selectin | Crystal structure | Structural analysis | Conformation | Microheterogeneity
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14. Full Text The effects of flash‐annealing on glycerol kinase crystals
by Vahedi‐Faridi, Ardeschir and Stojanoff, Vivian and Yeh, Joanne I and Brookhaven National Laboratory (BNL) National Synchrotron Light Source (NSLS)
Acta crystallographica. Section D, Biological crystallography., ISSN 1399-0047, 07/2005, Volume 61, Issue 7, pp. 982 - 989
flash‐annealing | cryocooling mosaicity | in situ annealing | crystal quality | glycerol kinase | Biochemistry & Molecular Biology | Physical Sciences | Life Sciences & Biomedicine | Biochemical Research Methods | Biophysics | Crystallography | Science & Technology | Protein Structure, Tertiary | Enterococcus - enzymology | Crystallization - instrumentation | Crystallization - methods | Freezing | Glycerol Kinase - chemistry | Index Medicus | CRYSTALS | POLYMERS | PHOSPHOTRANSFERASES | national synchrotron light source | GLYCEROL |