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1. Full Text Rap1 binding and a lipid-dependent helix in talin F1 domain promote integrin activation in tandem
by Gingras, Alexandre R and Lagarrigue, Frederic and Cuevas, Monica N and Valadez, Andrew J and Zorovich, Marcus and McLaughlin, Wilma and Lopez-Ramirez, Miguel Alejandro and Seban, Nicolas and Ley, Klaus and Kiosses, William B and Ginsberg, Mark H
The Journal of cell biology, ISSN 0021-9525, 04/2019, Volume 218, Issue 6, pp. 1799 - 1809
Rap1 GTPases bind effectors, such as RIAM, to enable talin1 to induce integrin activation. In addition, Rap1 binds directly to the talin1 F0 domain (F0);... 
Rap1 protein | Charge reversal | Lipids | Talin | Activation | Mutation | Platelets | Binding sites
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2. Full Text Transmission of integrin ß7 transmembrane domain topology enables gut lymphoid tissue development
by Hao Sun and Frederic Lagarrigue and Alexandre R Gingras and Zhichao Fan and Klaus Ley and Mark H Ginsberg
The Journal of Cell Biology, ISSN 0021-9525, 04/2018, Volume 217, Issue 4, p. 1453
Integrin activation regulates adhesion, extracellular matrix assembly, and cell migration, thereby playing an indispensable role in development and in many... 
Leukocyte migration | Proline | Talin | Activation | Topology | Lymphoid tissue | Cell adhesion & migration | Homing | White blood cells | Leucocytes | Biological effects | Cell activation | Lymphocytes | Gut-associated lymphoid tissues | Extracellular matrix | Mutation | Cell migration
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3. Full Text Integrin activation
by Ginsberg, Mark H
BMB reports, ISSN 1976-670X, 2014, Volume 47, Issue 12, pp. 655 - 659
Integrin-mediated cell adhesion is important for development, immune responses, hemostasis and wound healing. Integrins also function as signal transducing... 
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4. Full Text The final steps of integrin activation: the end game
by Shattil, Sanford J and Ginsberg, Mark H and Kim, Chungho
Nature Reviews Molecular Cell Biology, ISSN 1471-0072, 04/2010, Volume 11, Issue 4, pp. 288 - 300
Cell-directed changes in the ligand-binding affinity ('activation') of integrins regulate cell adhesion and migration, extracellular matrix assembly and... 
CYTOPLASMIC DOMAIN | TYROSINE PHOSPHORYLATION | ALPHA-SUBUNIT | STRUCTURAL BASIS | GPIIB-IIIA | OUTSIDE-IN | TRANSMEMBRANE DOMAIN | BINDING-LIKE DOMAIN | LEUKOCYTE ADHESION | MEMBRANE-PROXIMAL REGION | CELL BIOLOGY | Cytoplasm - metabolism | Animals | Signal Transduction | Talin - metabolism | Integrins - metabolism | Humans | Physiological aspects | Embryonic development | Research | Integrins
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5. Full Text Regulation of Integrin Activation
by Kim, Chungho and Ye, Feng and Ginsberg, Mark H
Annual Review of Cell and Developmental Biology, ISSN 1081-0706, 11/2011, Volume 27, Issue 1, pp. 321 - 345
Regulation of cell-cell and cell-matrix interaction is essential for the normal physiology of metazoans and is important in many diseases. Integrin adhesion... 
cell migration | integrin | signal transduction | transmembrane domain | cell adhesion | nanodisc | Transmembrane domain | Nanodisc | Signal transduction | Integrin | Cell migration | Cell adhesion | PHOSPHOLIPID-BILAYER NANODISCS | LINKED KINASE | TALIN HEAD | CRYSTAL-STRUCTURE | PLATELET-FUNCTION | DEVELOPMENTAL BIOLOGY | CELL BIOLOGY | ADHESION DEFICIENCY-III | LEUKOCYTE ADHESION | EXTRACELLULAR SEGMENT | SUBUNIT CYTOPLASMIC DOMAINS | Humans | Integrins - chemistry | Integrins - genetics | Molecular Sequence Data | Intracellular Signaling Peptides and Proteins - metabolism | Cytoskeletal Proteins - metabolism | Membrane Proteins - metabolism | Microfilament Proteins - metabolism | Contractile Proteins - metabolism | Protein-Serine-Threonine Kinases - metabolism | Calcium-Binding Proteins - metabolism | Integrins - physiology | Protein Structure, Tertiary | Amino Acid Sequence | rap1 GTP-Binding Proteins - metabolism | Models, Molecular | Talin - metabolism | Cell Adhesion Molecules - metabolism | Filamins | Sequence Alignment | Animals | Membrane Proteins - chemistry | Cell Adhesion - physiology | Protein Binding | Protein Conformation | Signal Transduction - physiology | Physiological aspects | Research | Integrins
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6. Full Text Thrombospondin1 (TSP1) replacement prevents cerebral cavernous malformations
by Lopez-Ramirez, Miguel Alejandro and Fonseca, Gregory and Zeineddine, Hussein A and Girard, Romuald and Moore, Thomas and Pham, Angela and Cao, Ying and Shenkar, Robert and de Kreuk, Bart-Jan and Lagarrigue, Frederic and Lawler, Jack and Glass, Christopher K and Awad, Issam A and Ginsberg, Mark H
The Journal of experimental medicine, 11/2017, Volume 214, Issue 11, p. 3331
mutations are the most common cause of cerebral cavernous malformation (CCM). Acute gene inactivation in mouse brain microvascular endothelial cells (BMECs)... 
Hemangioma, Cavernous, Central Nervous System - therapy | Endothelial Cells - metabolism | Humans | KRIT1 Protein - metabolism | Mice, Inbred C57BL | Cells, Cultured | Gene Expression Profiling - methods | Mice, Transgenic | KRIT1 Protein - genetics | Hemangioma, Cavernous, Central Nervous System - genetics | Hemangioma, Cavernous, Central Nervous System - metabolism | Mice, Knockout | Animals | RNA Interference | Kruppel-Like Transcription Factors - metabolism | Thrombospondin 1 - genetics | HEK293 Cells | Thrombospondin 1 - metabolism | Kruppel-Like Transcription Factors - genetics | Genetic Therapy - methods
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7. Full Text Invited Mini Review : Integrin activation
by Mark H Ginsberg
BMB Reports, ISSN 1976-6696, 2014, Volume 47, Issue 12, p. 655
Integrin-mediated cell adhesion is important for development, immune responses, hemostasis and wound healing. Integrins also function as signal transducing... 
Nanodisc | Signal transduction | Integrin | Cell adhesion | Transmembrane domain | Talin
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8. Loss of T Cell CD98 H Chain Specifically Ablates T Cell Clonal Expansion and Protects from Autoimmunity
by Cantor, Joseph and Slepak, Marina and Ege, Nil and Chang, John T and Ginsberg, Mark H
Journal of Immunology, ISSN 0022-1767, 07/2011, Volume 187, Issue 2, pp. 851 - 860
CD98 H chain (4F2 Ag, Slc3a2) was discovered as a lymphocyte-activation Ag. Deletion of CD98 H chain in B cells leads to complete failure of B cell... 
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9. Full Text Integrin activation
by Ginsberg, Mark H
BMB Reports, ISSN 1976-6696, 2014, Volume 47, Issue 12, pp. 655 - 659
Integrin-mediated cell adhesion is important for development, immune responses, hemostasis and wound healing. Integrins also function as signal transducing... 
Transmembrane domain | Nanodisc | Signal transduction | Talin | Integrin | Cell adhesion | ALPHA(IIB)BETA | ALPHA-IIB-BETA-3 | COMPLEX | LIGAND-BINDING | TALIN HEAD | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRANSDUCTION | STRUCTURAL BASIS | AFFINITY | PLATELETS | Protein Structure, Tertiary | Talin - chemistry | Allosteric Regulation | Humans | Integrins - chemistry | Protein Binding | Talin - metabolism | Cell Adhesion | Integrins - metabolism | Invited Mini Review
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10. Full Text Interactions of platelet integrin αIIb and β3 transmembrane domains in mammalian cell membranes and their role in integrin activation
by Kim, Chungho and Lau, Tong-Lay and Ulmer, Tobias S and Ginsberg, Mark H
Blood, ISSN 0006-4971, 2009, Volume 113, Issue 19, pp. 4747 - 4753
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11. CD98 at the crossroads of adaptive immunity and cancer
by Cantor, Joseph M and Ginsberg, Mark H
Journal of Cell Science, ISSN 0021-9533, 03/2012, Volume 125, Issue 6, pp. 1373 - 1382
Adaptive immunity, a vertebrate specialization, adds memory and exquisite specificity to the basic innate immune responses present in invertebrates while... 
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12. Full Text α4 integrins and the immune response
by Rose, David M and Han, Jaewon and Ginsberg, Mark H
Immunological Reviews, ISSN 0105-2896, 2002, Volume 186, pp. 118 - 124
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13. Full Text Recreation of the Terminal Events in Physiological Integrin Activation
by Feng Ye and Guiqing Hu and Dianne Taylor and Boris Ratnikov and Andrey A. Bobkov and Mark A. McLean and Stephen G. Sligar and Kenneth A. Taylor and Mark H. Ginsberg
The Journal of Cell Biology, ISSN 0021-9525, 1/2010, Volume 188, Issue 1, pp. 157 - 173
Increased affinity of integrins for the extracellular matrix (activation) regulates cell adhesion and migration, extracellular matrix assembly, and... 
Teeth | Antibodies | Lipids | Ligands | Phospholipids | Liposomes | Platelets | Density | Integrins | Image classification | CYTOPLASMIC DOMAIN | PHOSPHOLIPID-BILAYER NANODISCS | CONFORMATIONAL-CHANGES | PLATELET GPIIB-IIIA | CRYSTAL-STRUCTURE | TALIN-BINDING | CALPAIN CLEAVAGE | EXTRACELLULAR SEGMENT | GLYCOPROTEIN-IIB-IIIA | ELECTRON TOMOGRAPHY | CELL BIOLOGY | Nanostructures - ultrastructure | Cricetinae | Cricetulus | Humans | Models, Molecular | Cryoelectron Microscopy | Animals | Protein Structure, Quaternary | Platelet Glycoprotein GPIIb-IIIa Complex - physiology | Protein Binding | Mutation | Platelet Glycoprotein GPIIb-IIIa Complex - ultrastructure | Platelet Glycoprotein GPIIb-IIIa Complex - genetics | Platelet Glycoprotein GPIIb-IIIa Complex - chemistry | CHO Cells | Physiological aspects | Analysis | Membrane proteins | Proteins | Membranes | Molecular biology | Cells | Cell adhesion & migration
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