F G Rathjen - JoVE Visualize

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Neuron|May 1, 1992

The chicken neural extracellular matrix molecule restrictin: similarity with EGF-, fibronectin type III-, and fibrinogen-like motifsU Nörenberg, H Wille, J M Wolff, et al.

The Journal of Cell Biology|February 1, 1987

Membrane glycoproteins involved in neurite fasciculationF G Rathjen, J M Wolff, R Frank, et al.

Journal of Neurocytology|March 5, 2002

Tenascin-R associates extracellularly with parvalbumin immunoreactive neurones but is synthesised by another neuronal population in the adult rat cerebral cortexE S Wintergerst, F G Rathjen, B Schwaller, et al.

Neuron|April 1, 1993

The axonal recognition molecule F11 is a multifunctional protein: specific domains mediate interactions with Ng-CAM and restrictinT Brümmendorf, M Hubert, U Treubert, et al.

Cell|December 4, 1987

Neurofascin: a novel chick cell-surface glycoprotein involved in neurite-neurite interactionsF G Rathjen, J M Wolff, S Chang, et al.

The Journal of Cell Biology|November 1, 1991

Neurite outgrowth on immobilized axonin-1 is mediated by a heterophilic interaction with L1(G4)T B Kuhn, E T Stoeckli, M A Condrau, et al.

Neuron|December 1, 1993

Induction of axonal growth by heterophilic interactions between the cell surface recognition proteins F11 and Nr-CAM/BravoG Morales, M Hubert, T Brümmendorf, et al.

The Journal of Cell Biology|February 24, 1997

Chicken acidic leucine-rich EGF-like domain containing brain protein (CALEB), a neural member of the EGF family of differentiation factors, is implicated in neurite formationS Schumacher, H Volkmer, F Buck, et al.

The Journal of Biological Chemistry|August 25, 1988

A human brain glycoprotein related to the mouse cell adhesion molecule L1J M Wolff, R Frank, K Mujoo, et al.

The Journal of Biological Chemistry|November 9, 2000

CALEB binds via its acidic stretch to the fibrinogen-like domain of tenascin-C or tenascin-R and its expression is dynamically regulated after optic nerve lesionS Schumacher, M Jung, U Nörenberg, et al.

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Showing results (31-40 of 43) with videos related to

Sort By:

Pageof 5

Neuron|May 1, 1992

The chicken neural extracellular matrix molecule restrictin: similarity with EGF-, fibronectin type III-, and fibrinogen-like motifsU Nörenberg, H Wille, J M Wolff, et al.

The Journal of Cell Biology|February 1, 1987

Membrane glycoproteins involved in neurite fasciculationF G Rathjen, J M Wolff, R Frank, et al.

Journal of Neurocytology|March 5, 2002

Tenascin-R associates extracellularly with parvalbumin immunoreactive neurones but is synthesised by another neuronal population in the adult rat cerebral cortexE S Wintergerst, F G Rathjen, B Schwaller, et al.

Neuron|April 1, 1993

The axonal recognition molecule F11 is a multifunctional protein: specific domains mediate interactions with Ng-CAM and restrictinT Brümmendorf, M Hubert, U Treubert, et al.

Cell|December 4, 1987

Neurofascin: a novel chick cell-surface glycoprotein involved in neurite-neurite interactionsF G Rathjen, J M Wolff, S Chang, et al.

The Journal of Cell Biology|November 1, 1991

Neurite outgrowth on immobilized axonin-1 is mediated by a heterophilic interaction with L1(G4)T B Kuhn, E T Stoeckli, M A Condrau, et al.

Neuron|December 1, 1993

Induction of axonal growth by heterophilic interactions between the cell surface recognition proteins F11 and Nr-CAM/BravoG Morales, M Hubert, T Brümmendorf, et al.

The Journal of Cell Biology|February 24, 1997

Chicken acidic leucine-rich EGF-like domain containing brain protein (CALEB), a neural member of the EGF family of differentiation factors, is implicated in neurite formationS Schumacher, H Volkmer, F Buck, et al.

The Journal of Biological Chemistry|August 25, 1988

A human brain glycoprotein related to the mouse cell adhesion molecule L1J M Wolff, R Frank, K Mujoo, et al.

The Journal of Biological Chemistry|November 9, 2000

CALEB binds via its acidic stretch to the fibrinogen-like domain of tenascin-C or tenascin-R and its expression is dynamically regulated after optic nerve lesionS Schumacher, M Jung, U Nörenberg, et al.

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