Idaira M. Guerrero-Fonseca
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View article: Author response: Arpin deficiency increases actomyosin contractility and vascular permeability
Author response: Arpin deficiency increases actomyosin contractility and vascular permeability Open
View article: Arpin deficiency increases actomyosin contractility and vascular permeability
Arpin deficiency increases actomyosin contractility and vascular permeability Open
Arpin was discovered as an inhibitor of the Arp2/3 complex localized at the lamellipodial tip of fibroblasts, where it regulated migration steering. Recently, we showed that arpin stabilizes the epithelial barrier in an Arp2/3-dependent ma…
View article: Author response: Arpin deficiency increases actomyosin contractility and vascular permeability
Author response: Arpin deficiency increases actomyosin contractility and vascular permeability Open
Arpin was discovered as an inhibitor of the Arp2/3 complex localized at the lamellipodial tip of fibroblasts, where it regulated migration steering. Recently, we showed that arpin stabilizes the epithelial barrier in an Arp2/3-dependent ma…
View article: Arpin deficiency increases actomyosin contractility and vascular permeability
Arpin deficiency increases actomyosin contractility and vascular permeability Open
Arpin was discovered as an inhibitor of the Arp2/3 complex localized at the lamellipodial tip of fibroblasts, where it regulated migration steering. Recently, we showed that arpin stabilizes the epithelial barrier in an Arp2/3-dependent ma…
View article: Reviewer #2 (Public Review): Arpin deficiency increases actomyosin contractility and vascular permeability
Reviewer #2 (Public Review): Arpin deficiency increases actomyosin contractility and vascular permeability Open
Arpin was discovered as an inhibitor of the Arp2/3 complex localized at the lamellipodial tip of fibroblasts, where it regulated migration steering. Recently, we showed that arpin stabilizes the epithelial barrier in an Arp2/3-dependent ma…
View article: Arpin deficiency increases actomyosin contractility and vascular permeability
Arpin deficiency increases actomyosin contractility and vascular permeability Open
Arpin was discovered as an inhibitor of the Arp2/3 complex localized at the lamellipodial tip of fibroblasts, where it regulated migration steering. Recently, we showed that arpin stabilizes the epithelial barrier in an Arp2/3-dependent ma…
View article: Arpin deficiency increases actomyosin contractility and vascular permeability
Arpin deficiency increases actomyosin contractility and vascular permeability Open
Arpin was discovered as an inhibitor of the Arp2/3 complex localized at the lamellipodial tip of fibroblasts, where it regulated migration steering. Recently, we showed that arpin stabilizes the epithelial barrier in an Arp2/3-dependent ma…
View article: Reviewer #1 (Public Review): Arpin deficiency increases actomyosin contractility and vascular permeability
Reviewer #1 (Public Review): Arpin deficiency increases actomyosin contractility and vascular permeability Open
Arpin was discovered as an inhibitor of the Arp2/3 complex localized at the lamellipodial tip of fibroblasts, where it regulated migration steering. Recently, we showed that arpin stabilizes the epithelial barrier in an Arp2/3-dependent ma…
View article: Arpin deficiency increases actomyosin contractility and vascular permeability
Arpin deficiency increases actomyosin contractility and vascular permeability Open
Arpin was discovered as an inhibitor of the Arp2/3 complex localized at the lamellipodial tip of fibroblasts, where it regulated migration steering. Recently, we showed that arpin stabilizes the epithelial barrier in an Arp2/3-dependent ma…
View article: Neutrophil breaching of the blood vessel pericyte layer during diapedesis requires mast cell-derived IL-17A
Neutrophil breaching of the blood vessel pericyte layer during diapedesis requires mast cell-derived IL-17A Open
View article: T cell activation, immune synapse formation, and organ infiltration by leukemic T cells require cortactin
T cell activation, immune synapse formation, and organ infiltration by leukemic T cells require cortactin Open
T cell acute lymphoblastic leukemia (T-ALL) is an aggressive hematological malignancy that is still fatal in many cases. T cell blasts are characterized by hyperactivation and strong proliferative and migratory capacities. The chemokine re…
View article: The Actin-Binding Protein Cortactin Promotes Sepsis Severity by Supporting Excessive Neutrophil Infiltration into the Lung
The Actin-Binding Protein Cortactin Promotes Sepsis Severity by Supporting Excessive Neutrophil Infiltration into the Lung Open
Sepsis is a systemic infection that can lead to multi-organ failure. It is characterised by an uncontrolled immune response with massive neutrophil influx into peripheral organs. Neutrophil extravasation into tissues depends on actin remod…
View article: HS1 deficiency protects against sepsis by attenuating neutrophil-inflicted lung damage
HS1 deficiency protects against sepsis by attenuating neutrophil-inflicted lung damage Open
View article: Intermittent rolling is a defect of the extravasation cascade caused by Myosin1e-deficiency in neutrophils
Intermittent rolling is a defect of the extravasation cascade caused by Myosin1e-deficiency in neutrophils Open
Significance Myosin1e is a protein regulating actin cytoskeleton functions, which has not been studied in the context of neutrophil recruitment during inflammation. Using intravital microscopy of inflamed tissue in WT and myosin1e-deficien…
View article: Hematopoietic cell-specific lyn substrate (HCLS1 or HS1): A versatile actin-binding protein in leukocytes
Hematopoietic cell-specific lyn substrate (HCLS1 or HS1): A versatile actin-binding protein in leukocytes Open
Leukocytes are constantly produced in the bone marrow and released into the circulation. Many different leukocyte subpopulations exist that exert distinct functions. Leukocytes are recruited to sites of inflammation and combat the cause of…