Ghent University Academic Bibliography

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Your filters: cql: author="VANCOMPERNOLLE, K" or (type any "bookEditor issueEditor" and editor="VANCOMPERNOLLE, K")

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Tumor necrosis factor-induced microtubule stabilization mediated by hyperphosphorylated oncoprotein 18 promotes cell death.

K VANCOMPERNOLLE, Tom Boonefaes, M MANN, Walter Fiers and Johan Grooten (UGent)

(2000) JOURNAL OF BIOLOGICAL CHEMISTRY. 275(43). p.33876-33882
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- Journal Article
- A1
- open access
Tumor necrosis factor induces hyperphosphorylation of kinesin light chain and inhibits kinesin-mediated transport of mitochondria.

Kurt De Vos, F SEVERIN, F VAN HERREWEGHE, K VANCOMPERNOLLE, Vera Goossens (UGent) , A HYMAN and Johan Grooten (UGent)

(2000) JOURNAL OF CELL BIOLOGY. 149(6). p.1207-1214
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Redox regulation of TNF signaling.

Vera Goossens (UGent) , Kurt De Vos, D VERCAMMEN, Margino Steemans, K VANCOMPERNOLLE, Walter Fiers, Peter Vandenabeele (UGent) and Johan Grooten (UGent)

(1999) BIOFACTORS. 10(2-3). p.145-156
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The 55-kDa tumor necrosis factor receptor induces clustering of mitochondria through its membrane-proximal region.

Kurt De Vos, Vera Goossens (UGent) , Elke Boone, Dominique Vercammen (UGent) , K VANCOMPERNOLLE, Peter Vandenabeele (UGent) , Guy Haegeman (UGent) , Walter Fiers and Johan Grooten (UGent)

(1998) JOURNAL OF BIOLOGICAL CHEMISTRY. 273(16). p.9673-9680
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- Journal Article
- A1
An actin-binding site containing a conserved motif of charged amino acid residues is essential for the morphogenic effect of villin.

E FRIEDERICH, K VANCOMPERNOLLE, C HUET, M GOETHALS, J FINIDORI, Joël Vandekerckhove (UGent) and D LOUVARD

(1992) CELL. 70(1). p.81-92

Academic Bibliography

Tumor necrosis factor-induced microtubule stabilization mediated by hyperphosphorylated oncoprotein 18 promotes cell death.

Tumor necrosis factor induces hyperphosphorylation of kinesin light chain and inhibits kinesin-mediated transport of mitochondria.

Redox regulation of TNF signaling.

The 55-kDa tumor necrosis factor receptor induces clustering of mitochondria through its membrane-proximal region.

An actin-binding site containing a conserved motif of charged amino acid residues is essential for the morphogenic effect of villin.

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