Jenny C de Jonge
Overview
Explore the profile of Jenny C de Jonge including associated specialties, affiliations and a list of published articles.
Author names and details appear as published. Due to indexing inconsistencies, multiple individuals may share a name, and a single author may have variations. MedLuna displays this data as publicly available, without modification or verification
Snapshot
Snapshot
Articles
12
Citations
257
Followers
0
Related Specialties
Related Specialties
Top 10 Co-Authors
Top 10 Co-Authors
Published In
Published In
Affiliations
Affiliations
Soon will be listed here.
Recent Articles
1.
Gorter R, Arreguin A, Oost W, de Jonge J, Kampinga H, Amor S, et al.
Glia
. 2025 Mar;
PMID: 40059514
In multiple sclerosis (MS), an influx of immune cells into the central nervous system leads to focal demyelinating lesions in the brain, optic nerve, and spinal cord. As MS progresses,...
2.
Werkman I, Kovilein J, de Jonge J, Baron W
J Neurochem
. 2020 Jul;
156(5):624-641.
PMID: 32602556
Remyelination is a regenerative process that is essential to recover saltatory conduction and to prevent neurodegeneration upon demyelination. The formation of new myelin involves the differentiation of oligodendrocyte progenitor cells...
3.
Espitia Pinzon N, van Mierlo H, de Jonge J, Breve J, Bol J, Drukarch B, et al.
Front Cell Neurosci
. 2019 Jul;
13:281.
PMID: 31312122
Demyelinated lesions of the central nervous system are characteristic for multiple sclerosis (MS). Remyelination is not very effective, particular at later stages of the disease, which results in a chronic...
4.
Wang P, Gorter R, de Jonge J, Nazmuddin M, Zhao C, Amor S, et al.
Glia
. 2018 Mar;
66(8):1625-1643.
PMID: 29600597
Upon demyelination, transient expression of fibronectin precedes successful remyelination. However, in chronic demyelination observed in multiple sclerosis (MS), aggregates of fibronectin persist and contribute to remyelination failure. Accordingly, removing fibronectin...
5.
Qin J, Sikkema A, van der Bij K, de Jonge J, Klappe K, Nies V, et al.
J Neurosci
. 2017 Sep;
37(41):9925-9938.
PMID: 28899916
Remyelination failure by oligodendrocytes contributes to the functional impairment that characterizes the demyelinating disease multiple sclerosis (MS). Since incomplete remyelination will irreversibly damage axonal connections, treatments effectively promoting remyelination are...
6.
Bijlard M, de Jonge J, Klunder B, Nomden A, Hoekstra D, Baron W
PLoS One
. 2016 May;
11(5):e0155317.
PMID: 27171274
In oligodendrocytes (OLGs), an indirect, transcytotic pathway is mediating transport of de novo synthesized PLP, a major myelin specific protein, from the apical-like plasma membrane to the specialized basolateral-like myelin...
7.
Bijlard M, Klunder B, de Jonge J, Nomden A, Tyagi S, de Vries H, et al.
Mol Cell Biol
. 2014 Dec;
35(4):675-87.
PMID: 25512606
Myelination of axons by oligodendrocytes is essential for saltatory nerve conduction. To form myelin membranes, a coordinated synthesis and subsequent polarized transport of myelin components are necessary. Here, we show...
8.
Baron W, Ozgen H, Klunder B, de Jonge J, Nomden A, Plat A, et al.
Mol Cell Biol
. 2014 Nov;
35(1):288-302.
PMID: 25368380
Myelin membranes are sheet-like extensions of oligodendrocytes that can be considered membrane domains distinct from the cell's plasma membrane. Consistent with the polarized nature of oligodendrocytes, we demonstrate that transcytotic...
9.
Ozgen H, Schrimpf W, Hendrix J, de Jonge J, Lamb D, Hoekstra D, et al.
PLoS One
. 2014 Jul;
9(7):e101834.
PMID: 25003183
In the central nervous system, lipid-protein interactions are pivotal for myelin maintenance, as these interactions regulate protein transport to the myelin membrane as well as the molecular organization within the...
10.
Baron W, Bijlard M, Nomden A, de Jonge J, Teunissen C, Hoekstra D
Glia
. 2014 Mar;
62(6):927-42.
PMID: 24578319
In the central nervous system, the extracellular matrix (ECM) compound laminin-2, present on developing axons, is essential in regulating oligodendrocyte (OLG) maturation. For example, laminin-2 is involved in mediating interactions...