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1. Full Text Structure of the insulin receptor ectodomain reveals a folded-over conformation
by McKern, Neil M and Lawrence, Michael C and Streltsov, Victor A and Lou, Mei-Zhen and Adams, Timothy E and Lovrecz, George O and Elleman, Thomas C and Richards, Kim M and Bentley, John D and Pilling, Patricia A and Hoyne, Peter A and Cartledge, Kellie A and Pham, Tam M and Lewis, Jennifer L and Sankovich, Sonia E and Stoichevska, Violet and Da Silva, Elizabeth and Robinson, Christine P and Frenkel, Maurice J and Sparrow, Lindsay G and Fernley, Ross T and Epa, V. Chandana and Ward, Colin W
Nature, ISSN 0028-0836, 09/2006, Volume 443, Issue 7108, pp. 218 - 221
The insulin receptor is a phylogenetically ancient tyrosine kinase receptor found in organisms as primitive as cnidarians and insects. In higher organisms it... 
GROWTH-FACTOR RECEPTOR | ACTIVATION | ALPHA-SUBUNIT | SPECIFICITY | MULTIDISCIPLINARY SCIENCES | BINDING DOMAIN | 1ST 3 DOMAINS | MONOCLONAL-ANTIBODIES | REGION | Protein Structure, Tertiary | Receptor, Insulin - ultrastructure | Receptor, Insulin - chemistry | Protein Structure, Quaternary | Models, Molecular | Crystallography, X-Ray | Receptor, Insulin - metabolism | Immunoglobulin Fab Fragments - immunology | Microscopy, Electron | Receptor, Insulin - immunology | Dimerization | Protein Folding | Molecular structure | Peptides | Protein folding | Glucose | Kinases | Insulin | Binding sites | Crystal structure
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2. Full Text Crystal Structure of a Truncated Epidermal Growth Factor Receptor Extracellular Domain Bound to Transforming Growth Factor α
by Garrett, Thomas P.J and McKern, Neil M and Lou, Meizhen and Elleman, Thomas C and Adams, Timothy E and Lovrecz, George O and Zhu, Hong-Jian and Walker, Francesca and Frenkel, Morry J and Hoyne, Peter A and Jorissen, Robert N and Nice, Edouard C and Burgess, Antony W and Ward, Colin W
Cell, ISSN 0092-8674, 2002, Volume 110, Issue 6, pp. 763 - 773
We report the crystal structure, at 2.5 Å resolution, of a truncated human EGFR ectodomain bound to TGFα. TGFα interacts with both L1 and L2 domains of EGFR,... 
HEREGULIN-ALPHA | FACTOR EGF RECEPTOR | ATOMIC-STRUCTURE | COMPLEX | RECOGNITION | BIOCHEMISTRY & MOLECULAR BIOLOGY | NUCLEAR-MAGNETIC-RESONANCE | SIGNALING NETWORK | ECTODOMAIN | BINDING DOMAIN | LIGAND | CELL BIOLOGY | Humans | Molecular Sequence Data | Crystallography, X-Ray | Disulfides - chemistry | Conserved Sequence | Molecular Structure | Transforming Growth Factor alpha - metabolism | Binding Sites | Dimerization | Protein Structure, Tertiary | Amino Acid Sequence | Cell Line | ErbB Receptors - metabolism | Protein Structure, Secondary | Transforming Growth Factor alpha - chemistry | Crystallization | Models, Molecular | Transforming Growth Factor alpha - genetics | Sequence Alignment | Animals | ErbB Receptors - chemistry | Ligands | Mice | Mutation | 3T3 Cells | Amino Acid Substitution | Cell research | Gene mutations | Analysis | Ligands (Biochemistry) | Cancer cells | Physiological aspects | Genetic aspects
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3. Full Text The First Three Domains of the Insulin Receptor Differ Structurally from the Insulin-like Growth Factor 1 Receptor in the Regions Governing Ligand Specificity
by Meizhen Lou and Thomas P. J. Garrett and Neil M. McKern and Peter A. Hoyne and V. Chandana Epa and John D. Bentley and George O. Lovrecz and Leah J. Cosgrove and Maurice J. Frenkel and Colin W. Ward
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 8/2006, Volume 103, Issue 33, pp. 12429 - 12434
The insulin receptor (IR) and the type-1 insulin-like growth factor receptor (IGF1R) are homologous multidomain proteins that bind insulin and IGF with... 
Molecules | Receptors | Molecular structure | Disulfides | Crystals | Atoms | Ligands | Electrical potential | Insulin | Crystal structure | Insulin-binding site | Ectodomain | Protein Structure, Tertiary | Amino Acid Sequence | Receptor, IGF Type 1 - metabolism | Cricetinae | Insulin-Like Growth Factor I - chemistry | Protein Structure, Secondary | Humans | Models, Molecular | Molecular Sequence Data | Crystallography, X-Ray | Insulin-Like Growth Factor I - genetics | Receptor, IGF Type 1 - chemistry | Receptor, IGF Type 1 - genetics | Sequence Alignment | Animals | Receptor, Insulin - chemistry | Receptor, Insulin - genetics | Protein Binding | Receptor, Insulin - metabolism | Mutation | Insulin-Like Growth Factor I - metabolism | CHO Cells | Research | Insulin-like growth factor 1 | crystal structure | Biological Sciences | insulin-binding site | ectodomain
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4. Full Text Antibodies Specifically Targeting a Locally Misfolded Region of Tumor Associated EGFR
by Thomas P. J. Garrett and Antony W. Burgess and Hui K. Gan and Rod B. Luwor and Glenn Cartwright and Francesca Walker and Suzanne G. Orchard and Andrew H. A. Clayton and Edouard C. Nice and Julie Rothacker and Bruno Catimel and Webster K. Cavenee and Lloyd J. Old and Elisabeth Stockert and Gerd Ritter and Timothy E. Adams and Peter A. Hoyne and Dane Wittrup and Ginger Chao and Jennifer R. Cochran and Cindy Luo and Mezhen Lou and Trevor Huyton and Yibin Xu and W. Douglas Fairlie and Shenggen Yao and Andrew M. Scott and Terrance G. Johns and Jerry M. Adams
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 3/2009, Volume 106, Issue 13, pp. 5082 - 5087
Epidermal Growth Factor Receptor (EGFR) is involved in stimulating the growth of many human tumors, but the success of therapeutic agents has been limited in... 
Medical research | Receptors | Disulfides | Cell lines | Antibodies | Monoclonal antibodies | Epitopes | Growth factor receptors | Heterologous transplantation | Tumors | Epitope | Structure | Therapeutic antibody | Cancer | Cryptic | MULTIDISCIPLINARY SCIENCES | cryptic | DIMERIZATION | COMBINATION | structure | FACTOR-ALPHA | RECEPTOR MONOCLONAL-ANTIBODY | INHIBITION | STRUCTURAL BASIS | MONOCLONAL-ANTIBODY-806 | EPIDERMAL-GROWTH-FACTOR | therapeutic antibody | cancer | epitope | XENOGRAFTS | Receptor, Epidermal Growth Factor - immunology | Antibodies, Neoplasm - immunology | Antibodies, Neoplasm - therapeutic use | Humans | Neoplasm Proteins - immunology | Antibodies, Monoclonal - therapeutic use | Crystallography, X-Ray | Antineoplastic Agents - therapeutic use | Xenograft Model Antitumor Assays | Animals | Antigen-Antibody Complex - chemistry | Mice, Nude | Protein Conformation | Antineoplastic Agents - pharmacology | Mice | Protein Denaturation - immunology | Antibodies, Monoclonal - immunology | Research | Biological Sciences
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5. Full Text Identification of the Epitope for the Epidermal Growth Factor Receptor-specific Monoclonal Antibody 806 Reveals That It Preferentially Recognizes an Untethered Form of the Receptor
by Terrance G. Johns and Timothy E. Adams and Jennifer R. Cochran and Nathan E Hall and Peter A. Hoyne and Mark J. Olsen and Yong-Sung Kim and Julie Rothacker and Edouard C. Nice and Francesca Walker and Gerd Ritter and Achim A. Jungbluth and Lloyd J. Old and Colin W. Ward and Antony W. Burgess and K. Dane Wittrup and Andrew M. Scott
Journal of Biological Chemistry, ISSN 0021-9258, 07/2004, Volume 279, Issue 29, pp. 30375 - 30384
The epidermal growth factor receptor (EGFR) is overexpressed in many epithelial cancers, an observation often correlated with poor clinical outcome.... 
MUTANT | DOMAIN | GENE | HUMAN GLIOBLASTOMAS | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | MALIGNANT GLIOMAS | MONOCLONAL-ANTIBODY | YEAST SURFACE DISPLAY | CANCER | EGF RECEPTOR | Surface Plasmon Resonance | Humans | Molecular Sequence Data | Immunoblotting | Dose-Response Relationship, Drug | Genetic Variation | Flow Cytometry | Transfection | Time Factors | Gene Deletion | Antineoplastic Agents - pharmacology | Cell Membrane - metabolism | Antibodies, Monoclonal - chemistry | Protein Structure, Tertiary | Amino Acid Sequence | Cell Line | Receptor, Epidermal Growth Factor - immunology | Enzyme-Linked Immunosorbent Assay | Peptides - chemistry | Signal Transduction | Models, Molecular | Plasmids - metabolism | Blotting, Western | Receptor, Epidermal Growth Factor - chemistry | Cell Line, Tumor | Protein Binding | Ligands | Protein Conformation | Epitopes - chemistry | Genetic Vectors
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6. Full Text CR1/CR2 Interactions Modulate the Functions of the Cell Surface Epidermal Growth Factor Receptor
by Francesca Walker and Suzanne G. Orchard and Robert N. Jorissen and Nathan E. Hall and Hui-Hua Zhang and Peter A. Hoyne and Timothy E. Adams and Terrance G. Johns and Colin Ward and Thomas P. J. Garrett and Hong-Jian Zhu and Maureen Nerrie and Andrew M. Scott and Edouard C. Nice and Antony W. Burgess
Journal of Biological Chemistry, ISSN 0021-9258, 05/2004, Volume 279, Issue 21, pp. 22387 - 22398
Recent crystallographic data on the isolated extracellular domain of the epidermal growth factor receptor (EGFR) have suggested a model for its activation by... 
CARCINOMA-CELLS | EXTRACELLULAR REGION | ACTIVATION | DOMAIN | LIGAND-BINDING | PROTEIN | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | HIGH-AFFINITY BINDING | EGF RECEPTOR | IMAGING MICROSCOPY | Phosphorylation | Protein-Tyrosine Kinases - metabolism | Cross-Linking Reagents - pharmacology | MAP Kinase Signaling System | Receptor, Epidermal Growth Factor - metabolism | Transfection | Cell Membrane - metabolism | Receptor, Epidermal Growth Factor - physiology | Dimerization | Tyrosine - chemistry | Protein Structure, Tertiary | Cell Line | Protein Structure, Secondary | Signal Transduction | Models, Molecular | Epidermal Growth Factor - metabolism | Point Mutation | Tyrosine - metabolism | Animals | Models, Biological | Protein Binding | Ligands | Protein Conformation | Mice | Enzyme Activation | Kinetics | Mutation
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7. The first three domains of the insulin receptor differ structurally from the insulin-like growth factor 1 receptor in the regions governing ligand specificity
by Meizhen Lou and Thomas P J Garrett and Neil M McKern and Peter A Hoyne
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 08/2006, Volume 103, Issue 33, p. 12429
  The insulin receptor (IR) and the type-1 insulin-like growth factor receptor (IGF1R) are homologous multidomain proteins that bind insulin and IGF with... 
Studies | Proteins | Insulin | Binding sites | Crystal structure
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8. Full Text Molecular Characterization of a Secreted Enzyme with Phospholipase B Activity from Moraxella bovis
by Jacinta L. Farn and Richard A. Strugnell and Peter A. Hoyne and Wojtek P. Michalski and Jan M. Tennent
Journal of Bacteriology, ISSN 0021-9193, 11/2001, Volume 183, Issue 22, pp. 6717 - 6720
Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley... 
PHASES | MUTAGENESIS | GENE | CLONING | PSEUDOMONAS-AERUGINOSA | MEMBRANE | MICROBIOLOGY | KERATOCONJUNCTIVITIS | VIRULENCE | EXPRESSION | FAMILY | Recombinant Proteins - metabolism | Genes, Bacterial | Moraxella (Moraxella) bovis - genetics | Lysophospholipase - metabolism | Molecular Sequence Data | Antigens, Bacterial - isolation & purification | Antigens, Bacterial - genetics | Blotting, Western | Sequence Analysis, Protein | Moraxella (Moraxella) bovis - enzymology | Cloning, Molecular | Lysophospholipase - genetics | Lysophospholipase - isolation & purification | Antigens, Bacterial - metabolism | plb gene | Enzymes and Proteins
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9. Full Text Identification of a Determinant of Epidermal Growth Factor Receptor Ligand-Binding Specificity Using a Truncated, High-Affinity Form of the Ectodomain
by Elleman, Thomas C and Domagala, Teresa and McKern, Neil M and Nerrie, Maureen and Lönnqvist, Björn and Adams, Timothy E and Lewis, Jennifer and Lovrecz, George O and Hoyne, Peter A and Richards, Kim M and Howlett, Geoffrey J and Rothacker, Julie and Jorissen, Robert N and Lou, Meizhen and Garrett, Thomas P. J and Burgess, Antony W and Nice, Edouard C and Ward, Colin W
Biochemistry, ISSN 0006-2960, 07/2001, Volume 40, Issue 30, pp. 8930 - 8939
Murine and human epidermal growth factor receptors (EGFRs) bind human EGF (hEGF), mouse EGF (mEGF), and human transforming growth factor α (hTGF-α) with high... 
INSTRUMENTAL BIOSENSORS | FACTOR EGF RECEPTOR | FIRST 3 DOMAINS | DIRECTED MUTAGENESIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | KINETIC-ANALYSIS | EXTRACELLULAR DOMAIN | CONFORMATIONAL CHANGE | DIMERIZATION | OPTICAL BIOSENSOR | FACTOR-ALPHA | Sequence Deletion | Protein Binding - genetics | Humans | ErbB Receptors - genetics | ErbB Receptors - isolation & purification | Transfection | Growth Inhibitors - genetics | Transforming Growth Factor alpha - metabolism | Dimerization | Peptide Fragments - genetics | Plasmids - biosynthesis | CHO Cells | Cell Line | Cricetinae | Peptide Fragments - metabolism | ErbB Receptors - metabolism | Mutagenesis, Site-Directed | Peptide Fragments - isolation & purification | Epidermal Growth Factor - metabolism | Protein Structure, Tertiary - genetics | Peptide Fragments - biosynthesis | Plasmids - metabolism | Growth Inhibitors - metabolism | Animals | Chickens | ErbB Receptors - biosynthesis | Biosensing Techniques | Epidermal Growth Factor - antagonists & inhibitors | Binding, Competitive - genetics | Ligands | Mice | Physiological aspects | Amino acids | Biochemistry | Epidermal growth factor | Research | Ligands (Biochemistry)
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10. Full Text Expression, purification and characterization of recombinant phospholipase B from Moraxella bovis with anomalous electrophoretic behavior
by Shiell, Brian J and Tachedjian, Mary and Bruce, Kerri and Beddome, Gary and Farn, Jacinta L and Hoyne, Peter A and Michalski, Wojtek P
Protein Expression and Purification, ISSN 1046-5928, 2007, Volume 55, Issue 2, pp. 262 - 272
is the causative agent of infectious bovine keratoconjunctivitis (IBK) also known as pinkeye, a highly contagious and painful eye disease that is common in... 
Electrophoretic behavior | Moraxella bovis | Phospholipase B | Expression | phospholipase B | expression | PROTEIN | electrophoretic behavior | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | BIOCHEMICAL RESEARCH METHODS | GEL-ELECTROPHORESIS | BACTERIAL AUTOTRANSPORTER | CIRCULAR-DICHROISM | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | PSEUDOMONAS-AERUGINOSA | IN-VIVO | POLYACRYLAMIDE GELS | KERATOCONJUNCTIVITIS | KINETIC STABILITY | Recombinant Proteins - metabolism | Lysophospholipase - metabolism | Electrophoresis, Polyacrylamide Gel | Computational Biology | Electrophoresis, Gel, Two-Dimensional - methods | Recombinant Proteins - genetics | Chromatography, High Pressure Liquid | Recombinant Proteins - isolation & purification | Tandem Mass Spectrometry | Moraxella (Moraxella) bovis - enzymology | Cloning, Molecular | Lysophospholipase - genetics | Lysophospholipase - isolation & purification | Lipase | Esterases
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11. Structure of the insulin receptor ectodomain reveals a folded-over conformation
by McKern, Neil M and Lawrence, Michael C and Streltsov, Victor A and Lou, Mei-Zhen and Adams, Timothy E and Lovrecz, George O and Elleman, Thomas C and Richards, Kim M and Bentley, John D and Pilling, Patricia A and Hoyne, Peter A and Cartledge, Kellie A and Pham, Tam M and Lewis, Jennifer L
Nature, ISSN 0028-0836, 09/2006, Volume 443, Issue 7108, pp. 218 - 221
The insulin receptor is a phylogenetically ancient tyrosine kinase receptor found in organisms as primitive as cnidarians and insects. In higher organisms it... 
Journal Article
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12. Full Text Molecular characterization of a selected enzyme with phospholipase B activity from Moraxella bovis
by Farn, Jacinta L and Strugnell, Richard A and Hoyne, Peter A and Michalski, Wojtek P and Tennent, Jan M
Journal of Bacteriology, ISSN 0021-9193, 11/2001, Volume 183, Issue 21-22, p. 6717
Enzymes | Cloning | Research | Vaccines | Bacteriology | Molecules | Keratoconjunctivitis | Analysis | Physiological aspects | Causes of | Bacteria | Genetic aspects | Phospholipases
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13. Molecular characterization of a secreted enzyme with phospholipase B activity from Moraxella bovis
by Jacinta L Farn and Richard A Strugnell and Peter A Hoyne and Wojtek P Michaelski and Jan M Tennent
Journal of Bacteriology, ISSN 0021-9193, 11/2001, Volume 183, Issue 22, p. 6717
  A candidate for a baccine against infectious bovine keratoconjunctivitis (IBK) has been cloned and characterized from Moraxella bovis. The plb gene encodes a... 
Enzymes | Microbiology | Disease | Cattle | Bacteria | Vaccines
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14. Full Text Mutational analysis of the N-linked glycosylation sites of the human insulin receptor
by Elleman, Thomas C and Frenkel, Maurice J and Hoyne, Peter A and McKern, Neil M and Cosgrove, Leah and Hewish, Dean R and Jachno, Kim M and Bentley, John D and Sankovich, Sonia E and Ward, Colin W
Biochemical Journal, ISSN 0264-6021, 05/2000, Volume 347, Issue 3, pp. 771 - 779
Site-directed mutagenesis has been used to remove 15 of the 18 potential N-linked glycosylation sites, in 16 combinations, from the human exon 11-minus... 
Insulin binding | Autophosphorylation | Biosynthesis | Mutagenesis | Protein folding | insulin binding | LIGAND-BINDING | III DOMAIN | ALPHA-SUBUNIT | DIRECTED MUTAGENESIS | TYROSINE KINASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | EPIDERMAL GROWTH-FACTOR | mutagenesis | FAMILY | autophosphorylation | biosynthesis | ECTODOMAIN | protein folding | BETA-SUBUNIT
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15. Full Text High affinity insulin binding by soluble insulin receptor extracellular domain fused to a leucine zipper
by Hoyne, Peter A and Cosgrove, Leah J and McKern, Neil M and Bentley, John D and Ivancic, Neva and Elleman, Thomas C and Ward, Colin W
FEBS Letters, ISSN 0014-5793, 2000, Volume 479, Issue 1, pp. 15 - 18
Insulin receptors (IRs) that are truncated at the end of the ectodomain form dimers that bind insulin with different characteristics to wild type receptors.... 
Leucine zipper | Insulin receptor | Ectodomain chimera | Expression | High affinity binding | DISULFIDE BONDS | COMPLEX | expression | BIOCHEMISTRY & MOLECULAR BIOLOGY | ectodomain chimera | IDENTIFICATION | CELL BIOLOGY | NEGATIVE COOPERATIVITY | BIOPHYSICS | leucine zipper | ECTODOMAIN | high affinity binding | FRAGMENT | insulin receptor | LIGAND | Protein Structure, Tertiary | Cell Line | Cricetinae | Saccharomyces cerevisiae - genetics | Humans | Solubility | DNA Primers - genetics | Recombinant Fusion Proteins | Leucine Zippers - genetics | Insulin - metabolism | Animals | Transfection | Receptor, Insulin - chemistry | Receptor, Insulin - genetics | Base Sequence | Protein Structure, Quaternary | Receptor, Insulin - metabolism | Kinetics | In Vitro Techniques | Dimerization | CHO Cells
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16. Identification of the Epitope for the Epidermal Growth Factor Receptor- specific Monoclonal Antibody 806 Reveals That It Preferentially Recognizes an Untethered Form of the Receptor
by Johns, Terrance G and Adams, Timothy E and Cochran, Jennifer R and Hall, Nathan E and Hoyne, Peter A and Olsen, Mark J and Kim, Yong-Sung and Rothacker, Julie and Nice, Edouard C and Walker, Francesca and Ritter, Gerd and Jungbluth, Achim A and Old, Lloyd J and Ward, Colin W and Burgess, Antony W and Wittrup, KDane and Scott, Andrew M
Journal of Biological Chemistry, ISSN 0021-9258, 07/2004, Volume 279, Issue 29, pp. 30375 - 30384
The epidermal growth factor receptor (EGFR) is overexpressed in many epithelial cancers, an observation often correlated with poor clinical outcome.... 
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17. Full Text Properties of an insulin receptor with an IGF-1 receptor loop exchange in the cysteine-rich region
by Hoyne, Peter A and Elleman, Thomas C and Adams, Timothy E and Richards, Kim M and Ward, Colin W
FEBS Letters, ISSN 0014-5793, 2000, Volume 469, Issue 1, pp. 57 - 60
The insulin receptor (IR) and the insulin‐like growth factor‐I receptor (IGF‐1R) show differential binding of insulin and IGFs. The specificity determinants... 
Loop exchange | Cysteine | IGF-1 | Insulin receptor | BINDING-SPECIFICITY | SITE | DOMAIN | ALPHA-SUBUNIT | TYROSINE KINASE | DIRECTED MUTAGENESIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | cysteine | CELL BIOLOGY | lop exchange | BIOPHYSICS | insulin receptor | LIGAND | MONOCLONAL-ANTIBODIES | GROWTH-FACTOR-I | EPITOPES | Binding, Competitive | Recombinant Fusion Proteins - immunology | Amino Acid Sequence | Receptor, IGF Type 1 - metabolism | Iodine Radioisotopes | Humans | Molecular Sequence Data | Epitopes | Receptor, IGF Type 1 - genetics | Recombinant Fusion Proteins - metabolism | Insulin - metabolism | Receptor, Insulin - genetics | Receptor, Insulin - metabolism | Antibodies, Monoclonal - immunology
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18. Full Text Mutational analysis of the N-linked glycosylation sites of the human insulin receptor
by ELLEMAN, Thomas C and FRENKEL, Maurice J and HOYNE, Peter A and MCKERN, Neil M and COSGROVE, Leah and HEWISH, Dean R and JACHNO, Kim M and BENTLEY, John D and SANKOVICH, Sonia E and WARD, Colin W
Biochemical Journal, ISSN 0264-6021, 05/2000, Volume 347, Issue 3, pp. 771 - 779
Site-directed mutagenesis has been used to remove 15 of the 18 potential N-linked glycosylation sites, in 16 combinations, from the human exon 11-minus... 
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19. Full Text Production of Neisseria gonorrhoeae pili (fimbriae) in Pseudomonas aeruginosa
by P A Hoyne and R Haas and T F Meyer and J K Davies and T C Elleman
Journal of Bacteriology, ISSN 0021-9193, 11/1992, Volume 174, Issue 22, pp. 7321 - 7327
Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley... 
BACTEROIDES-NODOSUS FIMBRIAE | MORPHOGENETIC EXPRESSION | GENE | MORAXELLA-BOVIS | GONOCOCCAL PILI | CLONING | ESCHERICHIA-COLI | SEQUENCE | PROTEIN SECRETION | MICROBIOLOGY | VIBRIO-CHOLERAE | Amino Acid Sequence | Genes, Bacterial | Cell Fractionation | Fimbriae Proteins | Electrophoresis, Polyacrylamide Gel | Bacterial Outer Membrane Proteins - analysis | Molecular Sequence Data | Immunoblotting | Fimbriae, Bacterial - ultrastructure | Neisseria gonorrhoeae - ultrastructure | Microscopy, Immunoelectron | Transformation, Bacterial | Pseudomonas aeruginosa - genetics | Plasmids | Neisseria gonorrhoeae - genetics | Pseudomonas aeruginosa - ultrastructure | Bacterial Outer Membrane Proteins - genetics | Pseudomonas aeruginosa | Genetic aspects | Neisseria gonorrhoeae
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