The Experts below are selected from a list of 103134 Experts worldwide ranked by ideXlab platform
Benjamin Vollmer - One of the best experts on this subject based on the ideXlab platform.
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in situ structural analysis of the human nuclear pore complex
Nature, 2015Co-Authors: Alexander Von Appen, Jan Kosinski, Lenore Sparks, Amanda L Diguilio, Benjamin Vollmer, Marietherese Mackmull, Niccolo Banterle, Luca Parca, Panagiotis L KastritisAbstract:The most comprehensive architectural model to date of the nuclear pore complex reveals previously unknown local interactions, and a role for nucleoporin 358 in Y-complex oligomerization. The Transport of materials between the nucleus and cytoplasm in eukaryotic cells is controlled by the nuclear pore complex. Martin Beck and colleagues have used cryo-electron tomography, mass spectrometry and other analyses to generate the most comprehensive architectural model of the human nuclear pore complex to date. The model reveals previously unknown local interactions, and a role for the Transport Channel nucleoporin 358 (Nup358) in mediating oligomerization of the Y-complex within the nuclear pore complex. Nuclear pore complexes are fundamental components of all eukaryotic cells that mediate nucleocytoplasmic exchange. Determining their 110-megadalton structure imposes a formidable challenge and requires in situ structural biology approaches. Of approximately 30 nucleoporins (Nups), 15 are structured and form the Y and inner-ring complexes. These two major scaffolding modules assemble in multiple copies into an eight-fold rotationally symmetric structure that fuses the inner and outer nuclear membranes to form a central Channel of ~60 nm in diameter1. The scaffold is decorated with Transport-Channel Nups that often contain phenylalanine-repeat sequences and mediate the interaction with cargo complexes. Although the architectural arrangement of parts of the Y complex has been elucidated, it is unclear how exactly it oligomerizes in situ. Here we combine cryo-electron tomography with mass spectrometry, biochemical analysis, perturbation experiments and structural modelling to generate, to our knowledge, the most comprehensive architectural model of the human nuclear pore complex to date. Our data suggest previously unknown protein interfaces across Y complexes and to inner-ring complex members. We show that the Transport-Channel Nup358 (also known as Ranbp2) has a previously unanticipated role in Y-complex oligomerization. Our findings blur the established boundaries between scaffold and Transport-Channel Nups. We conclude that, similar to coated vesicles, several copies of the same structural building block—although compositionally identical—engage in different local sets of interactions and conformations.
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in situ structural analysis of the human nuclear pore complex
Nature, 2015Co-Authors: Alexander Von Appen, Jan Kosinski, Lenore Sparks, Amanda L Diguilio, Benjamin Vollmer, Marietherese Mackmull, Niccolo Banterle, Alessandro Ori, Luca ParcaAbstract:Nuclear pore complexes are fundamental components of all eukaryotic cells that mediate nucleocytoplasmic exchange. Determining their 110-megadalton structure imposes a formidable challenge and requires in situ structural biology approaches. Of approximately 30 nucleoporins (Nups), 15 are structured and form the Y and inner-ring complexes. These two major scaffolding modules assemble in multiple copies into an eight-fold rotationally symmetric structure that fuses the inner and outer nuclear membranes to form a central Channel of ~60 nm in diameter. The scaffold is decorated with Transport-Channel Nups that often contain phenylalanine-repeat sequences and mediate the interaction with cargo complexes. Although the architectural arrangement of parts of the Y complex has been elucidated, it is unclear how exactly it oligomerizes in situ. Here we combine cryo-electron tomography with mass spectrometry, biochemical analysis, perturbation experiments and structural modelling to generate, to our knowledge, the most comprehensive architectural model of the human nuclear pore complex to date. Our data suggest previously unknown protein interfaces across Y complexes and to inner-ring complex members. We show that the Transport-Channel Nup358 (also known as Ranbp2) has a previously unanticipated role in Y-complex oligomerization. Our findings blur the established boundaries between scaffold and Transport-Channel Nups. We conclude that, similar to coated vesicles, several copies of the same structural building block--although compositionally identical--engage in different local sets of interactions and conformations.
Luca Parca - One of the best experts on this subject based on the ideXlab platform.
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in situ structural analysis of the human nuclear pore complex
Nature, 2015Co-Authors: Alexander Von Appen, Jan Kosinski, Lenore Sparks, Amanda L Diguilio, Benjamin Vollmer, Marietherese Mackmull, Niccolo Banterle, Luca Parca, Panagiotis L KastritisAbstract:The most comprehensive architectural model to date of the nuclear pore complex reveals previously unknown local interactions, and a role for nucleoporin 358 in Y-complex oligomerization. The Transport of materials between the nucleus and cytoplasm in eukaryotic cells is controlled by the nuclear pore complex. Martin Beck and colleagues have used cryo-electron tomography, mass spectrometry and other analyses to generate the most comprehensive architectural model of the human nuclear pore complex to date. The model reveals previously unknown local interactions, and a role for the Transport Channel nucleoporin 358 (Nup358) in mediating oligomerization of the Y-complex within the nuclear pore complex. Nuclear pore complexes are fundamental components of all eukaryotic cells that mediate nucleocytoplasmic exchange. Determining their 110-megadalton structure imposes a formidable challenge and requires in situ structural biology approaches. Of approximately 30 nucleoporins (Nups), 15 are structured and form the Y and inner-ring complexes. These two major scaffolding modules assemble in multiple copies into an eight-fold rotationally symmetric structure that fuses the inner and outer nuclear membranes to form a central Channel of ~60 nm in diameter1. The scaffold is decorated with Transport-Channel Nups that often contain phenylalanine-repeat sequences and mediate the interaction with cargo complexes. Although the architectural arrangement of parts of the Y complex has been elucidated, it is unclear how exactly it oligomerizes in situ. Here we combine cryo-electron tomography with mass spectrometry, biochemical analysis, perturbation experiments and structural modelling to generate, to our knowledge, the most comprehensive architectural model of the human nuclear pore complex to date. Our data suggest previously unknown protein interfaces across Y complexes and to inner-ring complex members. We show that the Transport-Channel Nup358 (also known as Ranbp2) has a previously unanticipated role in Y-complex oligomerization. Our findings blur the established boundaries between scaffold and Transport-Channel Nups. We conclude that, similar to coated vesicles, several copies of the same structural building block—although compositionally identical—engage in different local sets of interactions and conformations.
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in situ structural analysis of the human nuclear pore complex
Nature, 2015Co-Authors: Alexander Von Appen, Jan Kosinski, Lenore Sparks, Amanda L Diguilio, Benjamin Vollmer, Marietherese Mackmull, Niccolo Banterle, Alessandro Ori, Luca ParcaAbstract:Nuclear pore complexes are fundamental components of all eukaryotic cells that mediate nucleocytoplasmic exchange. Determining their 110-megadalton structure imposes a formidable challenge and requires in situ structural biology approaches. Of approximately 30 nucleoporins (Nups), 15 are structured and form the Y and inner-ring complexes. These two major scaffolding modules assemble in multiple copies into an eight-fold rotationally symmetric structure that fuses the inner and outer nuclear membranes to form a central Channel of ~60 nm in diameter. The scaffold is decorated with Transport-Channel Nups that often contain phenylalanine-repeat sequences and mediate the interaction with cargo complexes. Although the architectural arrangement of parts of the Y complex has been elucidated, it is unclear how exactly it oligomerizes in situ. Here we combine cryo-electron tomography with mass spectrometry, biochemical analysis, perturbation experiments and structural modelling to generate, to our knowledge, the most comprehensive architectural model of the human nuclear pore complex to date. Our data suggest previously unknown protein interfaces across Y complexes and to inner-ring complex members. We show that the Transport-Channel Nup358 (also known as Ranbp2) has a previously unanticipated role in Y-complex oligomerization. Our findings blur the established boundaries between scaffold and Transport-Channel Nups. We conclude that, similar to coated vesicles, several copies of the same structural building block--although compositionally identical--engage in different local sets of interactions and conformations.
P. A. Piminov - One of the best experts on this subject based on the ideXlab platform.
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A New System for Measuring the Beam Position in the Electron– Positron Transport Channel from the VEPP-3 Storage Ring of the VEPP-4M Collider
Instruments and Experimental Techniques, 2020Co-Authors: G. V. Karpov, E. A. Bekhtenev, A. N. Zhuravlev, P. A. PiminovAbstract:A new system for measuring the position of the beam in a pulsed Transport Channel from the VEPP-3 storage ring to the VEPP-4M collider is discussed, which provides measurement of the position and intensity of an electron or positron beam in one span. For reliable operation of the experimental complex, it is necessary to continuously monitor the beam trajectory in a non-destructive manner, as well as to measure the possible losses of the beam charge. In 2018, new sensors and new electronics of the beam position measurement system were developed, manufactured, and installed in the Transportation Channel, which provide much greater accuracy compared to the old system. In the new system, it was possible to almost completely eliminate interference and to achieve measurement accuracy better than 0.02 mm, which is more than enough for optimal tuning of the Channel optics and achieving high bypass efficiency. The design of the sensor, the structure and the main features of the construction of electronics are described, the accuracy of measurements is analyzed, and some results of the operation of the new system in the Channel are given.
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A New System for Measuring the Beam Position in the Electron– Positron Transport Channel from the VEPP-3 Storage Ring of the VEPP-4M Collider
Instruments and Experimental Techniques, 2020Co-Authors: G. V. Karpov, E. A. Bekhtenev, A. N. Zhuravlev, P. A. PiminovAbstract:A new system for measuring the position of the beam in a pulsed Transport Channel from the VEPP-3 storage ring to the VEPP-4M collider is discussed, which provides measurement of the position and intensity of an electron or positron beam in one span. For reliable operation of the experimental complex, it is necessary to continuously monitor the beam trajectory in a non-destructive manner, as well as to measure the possible losses of the beam charge. In 2018, new sensors and new electronics of the beam position measurement system were developed, manufactured, and installed in the Transportation Channel, which provide much greater accuracy compared to the old system. In the new system, it was possible to almost completely eliminate interference and to achieve measurement accuracy better than 0.02 mm, which is more than enough for optimal tuning of the Channel optics and achieving high bypass efficiency. The design of the sensor, the structure and the main features of the construction of electronics are described, the accuracy of measurements is analyzed, and some results of the operation of the new system in the Channel are given.
Panagiotis L Kastritis - One of the best experts on this subject based on the ideXlab platform.
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in situ structural analysis of the human nuclear pore complex
Nature, 2015Co-Authors: Alexander Von Appen, Jan Kosinski, Lenore Sparks, Amanda L Diguilio, Benjamin Vollmer, Marietherese Mackmull, Niccolo Banterle, Luca Parca, Panagiotis L KastritisAbstract:The most comprehensive architectural model to date of the nuclear pore complex reveals previously unknown local interactions, and a role for nucleoporin 358 in Y-complex oligomerization. The Transport of materials between the nucleus and cytoplasm in eukaryotic cells is controlled by the nuclear pore complex. Martin Beck and colleagues have used cryo-electron tomography, mass spectrometry and other analyses to generate the most comprehensive architectural model of the human nuclear pore complex to date. The model reveals previously unknown local interactions, and a role for the Transport Channel nucleoporin 358 (Nup358) in mediating oligomerization of the Y-complex within the nuclear pore complex. Nuclear pore complexes are fundamental components of all eukaryotic cells that mediate nucleocytoplasmic exchange. Determining their 110-megadalton structure imposes a formidable challenge and requires in situ structural biology approaches. Of approximately 30 nucleoporins (Nups), 15 are structured and form the Y and inner-ring complexes. These two major scaffolding modules assemble in multiple copies into an eight-fold rotationally symmetric structure that fuses the inner and outer nuclear membranes to form a central Channel of ~60 nm in diameter1. The scaffold is decorated with Transport-Channel Nups that often contain phenylalanine-repeat sequences and mediate the interaction with cargo complexes. Although the architectural arrangement of parts of the Y complex has been elucidated, it is unclear how exactly it oligomerizes in situ. Here we combine cryo-electron tomography with mass spectrometry, biochemical analysis, perturbation experiments and structural modelling to generate, to our knowledge, the most comprehensive architectural model of the human nuclear pore complex to date. Our data suggest previously unknown protein interfaces across Y complexes and to inner-ring complex members. We show that the Transport-Channel Nup358 (also known as Ranbp2) has a previously unanticipated role in Y-complex oligomerization. Our findings blur the established boundaries between scaffold and Transport-Channel Nups. We conclude that, similar to coated vesicles, several copies of the same structural building block—although compositionally identical—engage in different local sets of interactions and conformations.
Marietherese Mackmull - One of the best experts on this subject based on the ideXlab platform.
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in situ structural analysis of the human nuclear pore complex
Nature, 2015Co-Authors: Alexander Von Appen, Jan Kosinski, Lenore Sparks, Amanda L Diguilio, Benjamin Vollmer, Marietherese Mackmull, Niccolo Banterle, Luca Parca, Panagiotis L KastritisAbstract:The most comprehensive architectural model to date of the nuclear pore complex reveals previously unknown local interactions, and a role for nucleoporin 358 in Y-complex oligomerization. The Transport of materials between the nucleus and cytoplasm in eukaryotic cells is controlled by the nuclear pore complex. Martin Beck and colleagues have used cryo-electron tomography, mass spectrometry and other analyses to generate the most comprehensive architectural model of the human nuclear pore complex to date. The model reveals previously unknown local interactions, and a role for the Transport Channel nucleoporin 358 (Nup358) in mediating oligomerization of the Y-complex within the nuclear pore complex. Nuclear pore complexes are fundamental components of all eukaryotic cells that mediate nucleocytoplasmic exchange. Determining their 110-megadalton structure imposes a formidable challenge and requires in situ structural biology approaches. Of approximately 30 nucleoporins (Nups), 15 are structured and form the Y and inner-ring complexes. These two major scaffolding modules assemble in multiple copies into an eight-fold rotationally symmetric structure that fuses the inner and outer nuclear membranes to form a central Channel of ~60 nm in diameter1. The scaffold is decorated with Transport-Channel Nups that often contain phenylalanine-repeat sequences and mediate the interaction with cargo complexes. Although the architectural arrangement of parts of the Y complex has been elucidated, it is unclear how exactly it oligomerizes in situ. Here we combine cryo-electron tomography with mass spectrometry, biochemical analysis, perturbation experiments and structural modelling to generate, to our knowledge, the most comprehensive architectural model of the human nuclear pore complex to date. Our data suggest previously unknown protein interfaces across Y complexes and to inner-ring complex members. We show that the Transport-Channel Nup358 (also known as Ranbp2) has a previously unanticipated role in Y-complex oligomerization. Our findings blur the established boundaries between scaffold and Transport-Channel Nups. We conclude that, similar to coated vesicles, several copies of the same structural building block—although compositionally identical—engage in different local sets of interactions and conformations.
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in situ structural analysis of the human nuclear pore complex
Nature, 2015Co-Authors: Alexander Von Appen, Jan Kosinski, Lenore Sparks, Amanda L Diguilio, Benjamin Vollmer, Marietherese Mackmull, Niccolo Banterle, Alessandro Ori, Luca ParcaAbstract:Nuclear pore complexes are fundamental components of all eukaryotic cells that mediate nucleocytoplasmic exchange. Determining their 110-megadalton structure imposes a formidable challenge and requires in situ structural biology approaches. Of approximately 30 nucleoporins (Nups), 15 are structured and form the Y and inner-ring complexes. These two major scaffolding modules assemble in multiple copies into an eight-fold rotationally symmetric structure that fuses the inner and outer nuclear membranes to form a central Channel of ~60 nm in diameter. The scaffold is decorated with Transport-Channel Nups that often contain phenylalanine-repeat sequences and mediate the interaction with cargo complexes. Although the architectural arrangement of parts of the Y complex has been elucidated, it is unclear how exactly it oligomerizes in situ. Here we combine cryo-electron tomography with mass spectrometry, biochemical analysis, perturbation experiments and structural modelling to generate, to our knowledge, the most comprehensive architectural model of the human nuclear pore complex to date. Our data suggest previously unknown protein interfaces across Y complexes and to inner-ring complex members. We show that the Transport-Channel Nup358 (also known as Ranbp2) has a previously unanticipated role in Y-complex oligomerization. Our findings blur the established boundaries between scaffold and Transport-Channel Nups. We conclude that, similar to coated vesicles, several copies of the same structural building block--although compositionally identical--engage in different local sets of interactions and conformations.
