Literature DB >> 36070178

Nuclear Pore Dysfunction in Neurodegeneration.

Olivia Spead1,2, Benjamin L Zaepfel1,2, Jeffrey D Rothstein3,4.   

Abstract

The nuclear pore complex (NPC) is a large multimeric structure that is interspersed throughout the membrane of the nucleus and consists of at least 33 protein components. Individual components cooperate within the nuclear pore to facilitate selective passage of materials between the nucleus and cytoplasm while simultaneously performing pore-independent roles throughout the cell. NPC dysfunction is a hallmark of neurodegenerative disorders including Alzheimer's disease, Huntington's disease, and amyotrophic lateral sclerosis (ALS). NPC components can become mislocalized or altered in expression in neurodegeneration. These alterations in NPC structure are often detrimental to the neuronal function and ultimately lead to neuronal loss. This review highlights the importance of nucleocytoplasmic transport and NPC integrity and how dysfunction of such may contribute to neurodegeneration.
© 2022. The American Society for Experimental Neurotherapeutics, Inc.

Entities:  

Keywords:  ALS; Alzheimer’s disease; Huntington’s disease; Neurodegeneration; Nuclear pore complex; Nucleocytoplasmic transport

Year:  2022        PMID: 36070178     DOI: 10.1007/s13311-022-01293-w

Source DB:  PubMed          Journal:  Neurotherapeutics        ISSN: 1878-7479            Impact factor:   6.088


  93 in total

1.  Extremely long-lived nuclear pore proteins in the rat brain.

Authors:  Jeffrey N Savas; Brandon H Toyama; Tao Xu; John R Yates; Martin W Hetzer
Journal:  Science       Date:  2012-02-02       Impact factor: 47.728

Review 2.  Dynamics and diverse functions of nuclear pore complex proteins.

Authors:  Guillaume Chatel; Birthe Fahrenkrog
Journal:  Nucleus       Date:  2012-03-01       Impact factor: 4.197

Review 3.  Nucleocytoplasmic transport: signals, mechanisms and regulation.

Authors:  E A Nigg
Journal:  Nature       Date:  1997-04-24       Impact factor: 49.962

4.  Human Nup98 regulates the localization and activity of DExH/D-box helicase DHX9.

Authors:  Juliana S Capitanio; Ben Montpetit; Richard W Wozniak
Journal:  Elife       Date:  2017-02-21       Impact factor: 8.140

Review 5.  The Structure of the Nuclear Pore Complex (An Update).

Authors:  Daniel H Lin; André Hoelz
Journal:  Annu Rev Biochem       Date:  2019-03-18       Impact factor: 23.643

Review 6.  Nucleocytoplasmic transport.

Authors:  D Görlich; I W Mattaj
Journal:  Science       Date:  1996-03-15       Impact factor: 47.728

Review 7.  Compartmentalization of eukaryotic gene expression: causes and effects.

Authors:  R H Singer; M R Green
Journal:  Cell       Date:  1997-10-31       Impact factor: 41.582

Review 8.  Nuclear pore complexes in development and tissue homeostasis.

Authors:  Valeria Guglielmi; Stephen Sakuma; Maximiliano A D'Angelo
Journal:  Development       Date:  2020-12-15       Impact factor: 6.868

9.  Nuclear shield: a multi-enzyme task-force for nucleus protection.

Authors:  Raffaele Fabrini; Alessio Bocedi; Valentina Pallottini; Lorena Canuti; Michele De Canio; Andrea Urbani; Valeria Marzano; Tommaso Cornetta; Pasquale Stano; Anna Giovanetti; Lorenzo Stella; Antonella Canini; Giorgio Federici; Giorgio Ricci
Journal:  PLoS One       Date:  2010-12-10       Impact factor: 3.240

Review 10.  Role of Nucleoporins and Transport Receptors in Cell Differentiation.

Authors:  Asmat Ullah Khan; Rongmei Qu; Jun Ouyang; Jingxing Dai
Journal:  Front Physiol       Date:  2020-04-03       Impact factor: 4.566

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.