Nuclear-Cytoplasmic Transport [electronic resource] / edited by Weidong Yang.

Colaborador(es): Yang, Weidong [editor.] | SpringerLink (Online service)Tipo de material: TextoTextoSeries Nucleic Acids and Molecular Biology ; 33Editor: Cham : Springer International Publishing : Imprint: Springer, 2018Edición: 1st ed. 2018Descripción: VI, 274 p. 44 illus., 40 illus. in color. online resourceTipo de contenido: text Tipo de medio: computer Tipo de portador: online resourceISBN: 9783319773094Tema(s): Nucleic acids | Microbiology | Evolutionary biology | Nucleic Acid Chemistry | Applied Microbiology | Eukaryotic Microbiology | Evolutionary BiologyFormatos físicos adicionales: Printed edition:: Sin título; Printed edition:: Sin título; Printed edition:: Sin títuloClasificación CDD: 572.84 Clasificación LoC:QD433-436Recursos en línea: Libro electrónicoTexto
Contenidos:
Assembly of the nuclear pore complex -- Structure of Yeast nuclear pore complexes -- Structure and function of nucleoporins in nuclear transport -- Dynamic structures of the nuclear pore complex and their roles in nucleo-cytoplasmic transport -- Non-canonical roles of nuclear pore proteins -- On the role of the channel nucleoporins in nuclear transport -- Structures of Importins and Exportins -- Navigating the Nuclear Envelope: one or multiple transport mechanisms for integral membrane proteins? -- mRNA export and its dysregulation in disease -- Coarse-grained molecular dynamics of the natively-unfolded domain of the NPC -- On the effects of leukemogenic nucleoporin fusion proteins on nucleocytoplasmic transport and gene expression -- Structure and Function of the Nuclear Pore Complex Revealed by Advanced Fluorescence Microscopy.
En: Springer Nature eBookResumen: Dysfunction of nuclear-cytoplasmic transport systems has been associated with many human diseases. Thus, understanding of how functional this transport system maintains, or through dysfunction fails to maintain remains the core question in cell biology. In eukaryotic cells, the nuclear envelope (NE) separates the genetic transcription in the nucleus from the translational machinery in the cytoplasm. Thousands of nuclear pore complexes (NPCs) embedded on the NE selectively mediate the bidirectional trafficking of macromolecules such as RNAs and proteins between these two cellular compartments. In this book, the authors integrate recent progress on the structure of NPC and the mechanism of nuclear-cytoplasmic transport system in vitro and in vivo.
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Assembly of the nuclear pore complex -- Structure of Yeast nuclear pore complexes -- Structure and function of nucleoporins in nuclear transport -- Dynamic structures of the nuclear pore complex and their roles in nucleo-cytoplasmic transport -- Non-canonical roles of nuclear pore proteins -- On the role of the channel nucleoporins in nuclear transport -- Structures of Importins and Exportins -- Navigating the Nuclear Envelope: one or multiple transport mechanisms for integral membrane proteins? -- mRNA export and its dysregulation in disease -- Coarse-grained molecular dynamics of the natively-unfolded domain of the NPC -- On the effects of leukemogenic nucleoporin fusion proteins on nucleocytoplasmic transport and gene expression -- Structure and Function of the Nuclear Pore Complex Revealed by Advanced Fluorescence Microscopy.

Dysfunction of nuclear-cytoplasmic transport systems has been associated with many human diseases. Thus, understanding of how functional this transport system maintains, or through dysfunction fails to maintain remains the core question in cell biology. In eukaryotic cells, the nuclear envelope (NE) separates the genetic transcription in the nucleus from the translational machinery in the cytoplasm. Thousands of nuclear pore complexes (NPCs) embedded on the NE selectively mediate the bidirectional trafficking of macromolecules such as RNAs and proteins between these two cellular compartments. In this book, the authors integrate recent progress on the structure of NPC and the mechanism of nuclear-cytoplasmic transport system in vitro and in vivo.

UABC ; Temporal ; 01/01/2021-12/31/2023.

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