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animals (54) 54
humans (49) 49
beta cytoplasmic domain (46) 46
cell biology (39) 39
biochemistry & molecular biology (36) 36
beta-cytoplasmic domains (30) 30
index medicus (27) 27
integrins - metabolism (25) 25
tyrosine phosphorylation (25) 25
activation (22) 22
integrins (22) 22
phosphorylation (21) 21
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integrin (20) 20
hematology (19) 19
protein binding (19) 19
focal adhesion kinase (18) 18
amino acid sequence (16) 16
cell adhesion (16) 16
molecular sequence data (15) 15
protein structure, tertiary (14) 14
signal transduction - physiology (14) 14
beta cytoplasmic domains (13) 13
integrins - chemistry (13) 13
mice (13) 13
protein-tyrosine kinase (13) 13
signal-transduction (13) 13
talin (13) 13
talin - metabolism (13) 13
structural basis (12) 12
models, molecular (11) 11
proteins (11) 11
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glycoprotein-iib-iiia (10) 10
inside-out (10) 10
platelets (10) 10
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protein-tyrosine kinases - metabolism (10) 10
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cell movement (9) 9
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syk (9) 9
article (8) 8
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immunology (8) 8
ligand-binding (8) 8
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peripheral vascular disease (8) 8
receptor (8) 8
signaling (8) 8
src family kinases (8) 8
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cell-adhesion (7) 7
cho cells (7) 7
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integrin activation (7) 7
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src (7) 7
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actin (6) 6
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integrins - physiology (6) 6
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platelet glycoprotein gpiib-iiia complex - metabolism (6) 6
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cells (5) 5
chicken-embryo fibroblasts (5) 5
environment and public health (5) 5
extracellular-matrix (5) 5
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intracellular signaling peptides and proteins - metabolism (5) 5
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1. Full Text The Phosphotyrosine Binding-like Domain of Talin Activates Integrins
by David A. Calderwood and Boxu Yan and Jose M. de Pereda and Begoña Garcı́a Alvarez and Yosuke Fujioka and Robert C. Liddington and Mark H. Ginsberg
Journal of Biological Chemistry, ISSN 0021-9258, 06/2002, Volume 277, Issue 24, pp. 21749 - 21758
Cellular regulation of the ligand binding affinity of integrin adhesion receptors (integrin activation) depends on the integrin β cytoplasmic domains (tails).... 
FERM DOMAIN | TYROSINE PHOSPHORYLATION | PTB DOMAIN | STRUCTURAL BASIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | AMYLOID PRECURSOR PROTEIN | SURFACE-PLASMON RESONANCE | BETA-CYTOPLASMIC DOMAINS | PHORBOL ESTER | MULTIPLE SEQUENCE ALIGNMENT | CHICKEN-EMBRYO FIBROBLASTS | Surface Plasmon Resonance | Talin - chemistry | Integrins - chemistry | Molecular Sequence Data | Cytoplasm - metabolism | Flow Cytometry | Time Factors | CHO Cells | Cytoplasm - chemistry | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Amino Acid Sequence | Cricetinae | Cell Separation | Models, Molecular | Recombinant Fusion Proteins - chemistry | Cell Adhesion | Phosphotyrosine - chemistry | Protein Folding | Amino Acid Motifs | Sequence Homology, Amino Acid | Animals | Protein Binding | Ligands | Kinetics | Mutation | DNA, Complementary - metabolism
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2. Full Text Role of the Helix in Talin F3 Domain (F3 Helix) in Talin-Mediated Integrin Activation
by Li, Ang and Guo, Qiang and Wei, Ailin and Zhou, Yaliang and Hu, Weiming
Cell Biochemistry and Biophysics, ISSN 1085-9195, 3/2017, Volume 75, Issue 1, pp. 79 - 86
Increases in ligand binding to cellular integrins (activation) play an important role in platelet and leukocyte function. Talin is necessary in vivo and... 
Life Sciences | Biochemistry, general | Biotechnology | Integrin | Talin | Integrin activation | Biological and Medical Physics, Biophysics | Pharmacology/Toxicology | Cell Biology | F3 helix | ALPHA(IIB)BETA | FERM DOMAIN | COMPLEX | ALPHA-IIB-BETA-3 | MECHANISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | BETA CYTOPLASMIC DOMAIN | CYTOSKELETAL PROTEIN TALIN | CELL BIOLOGY | BIOPHYSICS | STRUCTURAL BASIS | LIPOSOMAL MEMBRANES | BINDING | Amino Acid Sequence | Protein Conformation, alpha-Helical | Cricetinae | Cricetulus | Talin - chemistry | Models, Molecular | Platelet Membrane Glycoprotein IIb - chemistry | Integrin beta3 - metabolism | Animals | Protein Interaction Domains and Motifs | Talin - physiology | Platelet Membrane Glycoprotein IIb - metabolism | CHO Cells | Membrane lipids | Analysis | Integrins | Index Medicus
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3. Full Text The N-terminal SH2 domain of Syk is required for (hem)ITAM, but not integrin, signaling in mouse platelets
by Hughes, Craig E and Finney, Brenda A and Koentgen, Frank and Lowe, Kate L and Watson, Steve P
Blood, ISSN 0006-4971, 01/2015, Volume 125, Issue 1, pp. 144 - 154
We have used a novel knockin mouse to investigate the effect of disruption of phosphotyrosine binding of the N-terminal SH2 domain of Syk on platelet... 
ACTIVATION MOTIF | GLYCOPROTEIN-VI | STIMULATED PLATELETS | RECEPTOR GAMMA-CHAIN | IN-VIVO | PROTEIN-TYROSINE KINASE | BETA-CYTOPLASMIC DOMAINS | IIB-IIIA | LYMPHATIC VASCULATURE | HEMATOLOGY | SRC KINASES | Protein Structure, Tertiary | Purpura, Thrombocytopenic, Idiopathic - metabolism | Amino Acid Sequence | Phosphorylation | Protein-Tyrosine Kinases - metabolism | Mice, Transgenic | Intracellular Signaling Peptides and Proteins - metabolism | Phosphoproteins - metabolism | Amino Acid Motifs | Phosphotyrosine - metabolism | src Homology Domains | Platelet Aggregation | Lectins, C-Type - metabolism | Protein-Tyrosine Kinases - genetics | Animals | Signal Transduction - drug effects | Blood Platelets - metabolism | Platelet Activation | Platelet Glycoprotein GPIIb-IIIa Complex - metabolism | Platelet Membrane Glycoproteins - metabolism | Mice | Intracellular Signaling Peptides and Proteins - genetics | Syk Kinase | Platelets and Thrombopoiesis
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4. Full Text Evidence for the Requirement of ITAM Domains but Not SLP-76/Gads Interaction for Integrin Signaling in Hematopoietic Cells
by Farhad Abtahian and Natalie Bezman and Regina Clemens and Eric Sebzda and Lan Cheng and Sanford J. Shattil and Mark L. Kahn and Gary A. Koretzky
Molecular and Cellular Biology, ISSN 0270-7306, 09/2006, Volume 26, Issue 18, pp. 6936 - 6949
Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley... 
AFFINITY IGE RECEPTOR | FC-EPSILON-RI | DIFFERENTIAL REQUIREMENT | HUMAN NEUTROPHILS | BIOCHEMISTRY & MOLECULAR BIOLOGY | MAST-CELLS | PROTEIN-TYROSINE KINASE | BETA-CYTOPLASMIC DOMAINS | PHOSPHORYLATED SLP-76 | PLATELET ACTIVATION | ADAPTER PROTEIN | CELL BIOLOGY | Blood Vessels - pathology | Humans | Phosphoproteins - metabolism | Protein-Tyrosine Kinases - deficiency | Integrins - metabolism | Phosphotyrosine - metabolism | Intracellular Signaling Peptides and Proteins - deficiency | Cell Membrane - metabolism | Syk Kinase | CHO Cells | Protein Structure, Tertiary | Cricetinae | Signal Transduction | Cells, Cultured | Mutation - genetics | Blood Vessels - cytology | Hematopoietic System - cytology | src Homology Domains | Animals | Hematopoietic System - metabolism | Phosphoproteins - deficiency | Protein Binding | Mice | Adaptor Proteins, Signal Transducing - metabolism | Blood Vessels - physiology | Receptors, Immunologic - metabolism
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5. Full Text Distinct Domains of CD98hc Regulate Integrins and Amino Acid Transport
by Csilla A. Fenczik and Roy Zent and Melissa Dellos and David A. Calderwood and Joe Satriano and Carolyn Kelly and Mark H. Ginsberg
Journal of Biological Chemistry, ISSN 0021-9258, 03/2001, Volume 276, Issue 12, pp. 8746 - 8752
CD98 is a cell surface heterodimer formed by the covalent linkage of CD98 heavy chain (CD98hc) with several different light chains to form amino acid... 
SYSTEM | 4F2 | OUT SIGNAL-TRANSDUCTION | HEAVY-CHAIN | ACTIVATION | SPECIFICITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRANSMEMBRANE | BETA-CYTOPLASMIC DOMAINS | MONOCLONAL-ANTIBODIES | PROTEINS | Carrier Proteins - physiology | Fusion Regulatory Protein-1 | Amino Acids - metabolism | Cell Line | Cricetinae | Animals | Biological Transport | Antigens, CD - physiology | Carrier Proteins - chemistry | Antigens, CD - chemistry | Structure-Activity Relationship | Integrins - metabolism
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6. Full Text Structure of the PTB domain of tensin1 and a model for its recruitment to fibrillar adhesions
by McCleverty, Clare J and Lin, Diane C and Liddington, Robert C
Protein Science, ISSN 0961-8368, 06/2007, Volume 16, Issue 6, pp. 1223 - 1229
Tensin is a cytoskeletal protein that links integrins to the actin cytoskeleton at sites of cell‐matrix adhesion. Here we describe the crystal structure of the... 
mutagenesis (site‐directed and general) | docking proteins | structure/function studies | crystallography | calorimetry | surface plasmon resonance | mutagenesis (site-directed and general) | PHOSPHOTYROSINE BINDING DOMAIN | PROTEIN | TYROSINE PHOSPHORYLATION | RECOGNITION | BIOCHEMISTRY & MOLECULAR BIOLOGY | BETA CYTOPLASMIC DOMAIN | RECEPTOR | INTEGRIN ACTIVATION | CELL-MATRIX ADHESIONS | TALIN | KINASE ACTIVATION | Phosphorylation | Talin - chemistry | Integrins - chemistry | Integrins - genetics | Molecular Sequence Data | Crystallography, X-Ray | Integrins - metabolism | Phosphotyrosine - metabolism | Talin - genetics | Microfilament Proteins - metabolism | Microfilament Proteins - genetics | Phosphotyrosine - genetics | Tyrosine - chemistry | Protein Structure, Tertiary | Amino Acid Sequence | Microfilament Proteins - chemistry | Talin - metabolism | Phosphotyrosine - chemistry | Sequence Homology, Amino Acid | Tensins | Tyrosine - metabolism | Animals | Chickens | Protein Binding | Tyrosine - genetics | Protein Structure Report | function studies | structure
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7. Full Text Structure and mechanics of integrin-based cell adhesion
by Arnaout, M Amin and Goodman, Simon L and Xiong, Jian-Ping
Current Opinion in Cell Biology, ISSN 0955-0674, 2007, Volume 19, Issue 5, pp. 495 - 507
Integrins are α/β heterodimeric adhesion glycoprotein receptors that regulate a wide variety of dynamic cellular processes such as cell migration,... 
Internal Medicine | I-LIKE DOMAIN | MIGRATING CELLS | LIGAND-BINDING | CRYSTAL-STRUCTURE | CD11B A-DOMAIN | BETA CYTOPLASMIC DOMAIN | PHOSPHATIDYLINOSITOL PHOSPHATE KINASE | MEDIATES RAP1-INDUCED ADHESION | ALPHA-ACTININ | FOCAL ADHESIONS | CELL BIOLOGY | Integrins - chemistry | Models, Molecular | Molecular Sequence Data | Crystallography, X-Ray | Cytoskeletal Proteins - chemistry | Talin - metabolism | Integrins - metabolism | Integrins - ultrastructure | Protein Subunits - metabolism | Animals | Cell Adhesion - physiology | Focal Adhesions - metabolism | Nuclear Magnetic Resonance, Biomolecular | Cytoskeletal Proteins - metabolism | Ligands | Protein Conformation | Signal Transduction - physiology | Protein Subunits - chemistry
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8. Full Text Integrin bi‐directional signaling across the plasma membrane
by Hu, Ping and Luo, Bing‐Hao
Journal of Cellular Physiology, ISSN 0021-9541, 02/2013, Volume 228, Issue 2, pp. 306 - 312
Integrins are heterodimeric cell adhesion molecules that are important in many biological functions, such as cell migration, proliferation, differentiation,... 
FERM DOMAIN | PHYSIOLOGY | ALPHA-SUBUNIT | LINKED KINASE | STRUCTURAL BASIS | ALPHA(IIB)BETA INTEGRIN | BETA CYTOPLASMIC DOMAIN | TRANSMEMBRANE DOMAIN | CELL-MEMBRANES | FOCAL ADHESION KINASE | FILAMIN BINDING | CELL BIOLOGY | Animals | Signal Transduction - drug effects | Focal Adhesion Protein-Tyrosine Kinases - metabolism | Humans | Integrins - agonists | Protein Conformation | Signal Transduction - physiology | Cell Membrane - metabolism | Mice | Integrins - metabolism | Integrins - antagonists & inhibitors | Cell membranes | Integrins
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9. Full Text Integrin regulation
by Ginsberg, Mark H and Partridge, Anthony and Shattil, Sanford J
Current Opinion in Cell Biology, ISSN 0955-0674, 2005, Volume 17, Issue 5, pp. 509 - 516
Integrin signaling is bidirectional. ‘Inside-out’ signals regulate integrin affinity for adhesive ligands, and ligand-dependent ‘outside-in’ signals regulate... 
SIGNAL-TRANSDUCTION | CONFORMATIONAL REGULATION | LINKED KINASE | CRYSTAL-STRUCTURE | TRANSMEMBRANE DOMAIN | CELL-ADHESION | TYROSINE KINASES | BETA-CYTOPLASMIC DOMAINS | EXTRACELLULAR SEGMENT | SRC FAMILY KINASES | CELL BIOLOGY | Integrins - physiology | Protein Kinases - metabolism | Protein Structure, Tertiary | Amino Acid Sequence | Humans | Models, Molecular | Molecular Sequence Data | Cell Membrane - physiology | Talin - metabolism | Integrins - metabolism | Phosphates - metabolism | Protein Conformation | Signal Transduction - physiology | Cell Membrane - metabolism | Integrins
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10. Full Text Genetic and cell biological analysis of integrin outside-in signaling
by Legate, Kyle R and Wickström, Sara A and Fässler, Reinhard
Genes and Development, ISSN 0890-9369, 02/2009, Volume 23, Issue 4, pp. 397 - 418
Integrins are cell surface transmembrane receptors that recognize and bind to extracellular matrix proteins and counter receptors. Binding of activated... 
Growth factor receptors | Actin cytoskeleton | Integrin signaling | Cell adhesion | RHO-FAMILY GTPASES | IGF-I | DYSTROPHIC MDX MICE | BETA CYTOPLASMIC DOMAIN | DEVELOPMENTAL BIOLOGY | GTPASE-ACTIVATING PROTEIN | CELL BIOLOGY | actin cytoskeleton | cell adhesion | growth factor receptors | GENETICS & HEREDITY | SMOOTH-MUSCLE-CELLS | PHOSPHOTYROSINE-BINDING DOMAIN | FOCAL ADHESION KINASE | GLYCOPROTEIN-IIB-IIIA | GROWTH-FACTOR-I | Receptor, IGF Type 1 - metabolism | Animals | Humans | Actins - metabolism | Cell Physiological Phenomena | Gene Expression Regulation | Cytoskeleton - metabolism | Integrins - genetics | Signal Transduction - physiology | Integrins - metabolism | Insulin-Like Growth Factor I - metabolism | Analysis | Cytology | Chemical properties | Research | Gene expression | Integrins
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11. Full Text Maintenance of murine platelet homeostasis by the kinase Csk and phosphatase CD148
by Mori, Jun and Nagy, Zoltan and Di Nunzio, Giada and Smith, Christopher W and Geer, Mitchell J and Al Ghaithi, Rashid and van Geffen, Johanna P and Heising, Silke and Boothman, Luke and Tullemans, Bibian M. E and Correia, Joao N and Tee, Louise and Kuijpers, Marijke J. E and Harrison, Paul and Heemskerk, Johan W. M and Jarvis, Gavin E and Tarakhovsky, Alexander and Weiss, Arthur and Mazharian, Alexana and Senis, Yotis A
Blood, ISSN 0006-4971, 03/2018, Volume 131, Issue 10, pp. 1122 - 1144
Src family kinases (SFKs) coordinate the initiating and propagating activation signals in platelets, but it remains unclear how they are regulated. Here, we... 
GLYCOPROTEIN-VI | T-LINEAGE CELLS | TANDEM SH2 DOMAINS | IN-VIVO | ADHESION MOLECULE-1 PECAM-1 | BETA CYTOPLASMIC DOMAIN | SRC FAMILY KINASES | VON-WILLEBRAND-FACTOR | PROTEIN-TYROSINE-PHOSPHATASE | RECEPTOR-GAMMA-CHAIN | HEMATOLOGY | Thrombosis and Hemostasis
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12. Full Text The Tail of Integrins, Talin, and Kindlins
by Markus Moser and Kyle R. Legate and Roy Zent and Reinhard Fässler
Science, ISSN 0036-8075, 5/2009, Volume 324, Issue 5929, pp. 895 - 899
Integrins are transmembrane cell-adhesion molecules that carry signals from the outside to the inside of the cell and vice versa. Like other cell surface... 
Proteins | Phosphorylation | Ligands | Amino acids | Focal adhesions | Gene expression regulation | Physiological regulation | Review | Platelets | Genetic mutation | Integrins | I/LWEQ MODULE | STRUCTURAL BASIS | PLATELET-AGGREGATION | MULTIDISCIPLINARY SCIENCES | BETA CYTOPLASMIC DOMAIN | BINDING-LIKE DOMAIN | LEUKOCYTE ADHESION | CELL-MATRIX ADHESION | GLYCOPROTEIN-IIB-IIIA | TRANSMEMBRANE SEGMENT | FOCAL ADHESIONS | Protein Structure, Tertiary | Signal Transduction | Talin - chemistry | Humans | Integrins - chemistry | Talin - metabolism | Cell Adhesion | Integrins - metabolism | Animals | Membrane Proteins - chemistry | Protein Binding | Protein Conformation | Membrane Proteins - metabolism | Ligand binding (Biochemistry) | Properties | Observations | Signal transduction | Molecular biology | Binding sites | Cell adhesion & migration
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