Structural and Functional Changes in Neuronal Intranuclear Inclusion Disease(NIID)

2019-08-17 19:30:49 | BioPortfolio


To discover the microstructure, macrostructure and functional changes with 7T multi-modal magnetic resonance imaging of Neuronal Intranuclear Inclusion Disease, and to explore new biomarkers for evaluating the severity and the progression of Neuronal Intranuclear Inclusion Disease.

Study Design


Neuronal Intranuclear Inclusion Disease


Siemens 7T MR




First Affiliated Hospital of Zhejiang University

Results (where available)

View Results


Published on BioPortfolio: 2019-08-17T19:30:49-0400

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Medical and Biotech [MESH] Definitions

Circumscribed masses of foreign or metabolically inactive materials, within the CELL NUCLEUS. Some are VIRAL INCLUSION BODIES.

A highly-conserved AAA ATPase that functions in the biogenesis of the transitional ENDOPLASMIC RETICULUM and fragmentation and reassembly of the GOLGI APPARATUS during MITOSIS. It also functions in a complex with UFD1L and NPLOC4 proteins to export misfolded ubiquitinated proteins from the endoplasmic reticulum and outer mitochondrial membrane to the cytoplasm for degradation by the PROTEASOME and also plays a role in AUTOPHAGY of ubiquitinated proteins. It occurs in neuronal INCLUSION BODIES from patients with AMYOTROPHIC LATERAL SCLEROSIS and LEWY BODIES from PARKINSON DISEASE patients.

Transection or severing of an axon. This type of denervation is used often in experimental studies on neuronal physiology and neuronal death or survival, toward an understanding of nervous system disease.

Clusters of neuronal cell bodies in invertebrates. Invertebrate ganglia may also contain neuronal processes and non-neuronal supporting cells. Many invertebrate ganglia are favorable subjects for research because they have small numbers of functional neuronal types which can be identified from one animal to another.

A member of the immunoglobulin superfamily of neuronal cell adhesion molecules that is required for proper nervous system development. Neural cell adhesion molecule L1 consists of six Ig domains, five fibronectin domains, a transmembrane region and an intracellular domain. Two splicing variants are known: a neuronal form that contains a four-amino acid RSLE sequence in the cytoplasmic domain, and a non-neuronal form that lacks the RSLE sequence. Mutations in the L1 gene result in L1 disease. Neural cell adhesion molecule L1 is predominantly expressed during development in neurons and Schwann cells; involved in cell adhesion, neuronal migration, axonal growth and pathfinding, and myelination.

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