MAL Is a Regulator of the Recruitment of Myelin Protein PLP to Membrane Microdomains

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The Differentiation of Rat Oligodendroglial Cells Is Highly Influenced by the Oxygen Tension: In Vitro Model Mimicking Physiologically Normoxic Conditions.

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MAL Is a Regulator of the Recruitment of Myelin Protein PLP to Membrane Microdomains

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MAL Is a Regulator of the Recruitment of Myelin Protein PLP to Membrane Microdomains

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MAL Is a Regulator of the Recruitment of Myelin Protein PLP to Membrane Microdomains

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MAL Is a Regulator of the Recruitment of Myelin Protein PLP to Membrane Microdomains

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MAL Is a Regulator of the Recruitment of Myelin Protein PLP to Membrane Microdomains

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MAL Is a Regulator of the Recruitment of Myelin Protein PLP to Membrane Microdomains

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MAL Is a Regulator of the Recruitment of Myelin Protein PLP to Membrane Microdomains

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MAL Is a Regulator of the Recruitment of Myelin Protein PLP to Membrane Microdomains

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MAL Is a Regulator of the Recruitment of Myelin Protein PLP to Membrane Microdomains

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MAL Is a Regulator of the Recruitment of Myelin Protein PLP to Membrane Microdomains

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P1476

MAL Is a Regulator of the Recruitment of Myelin Protein PLP to Membrane Microdomains

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Anita Nomden

http://www.w3.org/2001/XMLSchema#string

Bert Klunder

http://www.w3.org/2001/XMLSchema#string

Dick Hoekstra

http://www.w3.org/2001/XMLSchema#string

Jenny C de Jonge

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Marjolein Bijlard

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Wia Baron

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P2860

Interaction of PLP with GFP-MAL2 in the human oligodendroglial cell line HOG

Developmental expression pattern of the myelin proteolipid MAL indicates different functions of MAL for immature Schwann cells and in a late step of CNS myelinogenesis

MAL, a proteolipid in glycosphingolipid enriched domains: functional implications in myelin and beyond

MAL, an integral element of the apical sorting machinery, is an itinerant protein that cycles between the trans-Golgi network and the plasma membrane

Functional rafts in cell membranes

Fiji: an open-source platform for biological-image analysis.

Expression of the MAL gene in the thyroid: the MAL proteolipid, a component of glycolipid-enriched membranes, is apically distributed in thyroid follicles

The lateral membrane organization and dynamics of myelin proteins PLP and MBP are dictated by distinct galactolipids and the extracellular matrix

Characterization of a rat gene, rMAL, encoding a protein with four hydrophobic domains in central and peripheral myelin

rMAL is a glycosphingolipid-associated protein of myelin and apical membranes of epithelial cells in kidney and stomach

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e0155317

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scholarly article

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1692582

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10.1371/JOURNAL.PONE.0155317

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English

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P478

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P577

2016-01-01T00:00:00Z

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27171274

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P932

4865042

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MAL Is a Regulator of the Recruitment of Myelin Protein PLP to Membrane Microdomains

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MAL Is a Regulator of the Recruitment of Myelin Protein PLP to Membrane Microdomains

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P1476

P2093

P2860

P304

P31

P3181

P356

P407

P433

P478

P577

P698

P932

P3181

P356

P1433

P1476

P2093

P2860

P304

P31

P3181

P356

P407

P433

P478

P577

P698

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