Hochschulschrift

The role of VE-cadherin tyrosine phosphorylation for the control of endothelial cell contacts

to related objects

Location: Deutsche Nationalbibliothek Frankfurt am Main

Dimensions: 30 cm

Extent: XII, 164 S.

Language: Englisch

Notes: Ill., graph. Darst.
Münster (Westfalen), Univ., Diss., 2013 (Nur beschränkt für den Austausch)

Keyword: Signaltransduktion
Membrantransport
Biomembran
Endothel
Tierphysiologie
Maus
Immunologie
Immunsystem
Lymphozyt
Immunbiologie
Leukozyt
Immunität
Resistenz
Immunozyt
Immunozyt
Gedächtniszelle

Creator: Wessel, Florian

Table of contents: https://d-nb.info/1032978775/04

Rights: Bei diesem Objekt liegt nur das Inhaltsverzeichnis digital vor. Der Zugriff darauf ist unbeschränkt möglich.

Last update: 11.06.2025, 1:50 PM CEST

Data provider

This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.

Object type

Hochschulschrift

Associated

Wessel, Florian

Other Objects (12)

Hochschulschrift

The proteine tyrosine phosphatase VE-PTP controls endothelial cell contacts via VE-cadherin and Tie-2

Tyrosine-protein kinase Yes controls endothelial junctional plasticity and barrier integrity by regulating VE-cadherin phosphorylation and endocytosis

Hochschulschrift

Regulation of VE-cadherin tyrosine 731 phosphorylation under basal and inflammatory conditions

Correction to: Disruption of endothelial adherens junctions by high glucose is mediated by protein kinase C-β–dependent vascular endothelial cadherin tyrosine phosphorylation

Angiotensin II impairs endothelial function via tyrosine phosphorylation of the endothelial nitric oxide synthase

VE-PTP and VE-cadherin ectodomains interact to facilitate regulation of phosphorylation and cell contacts

Hochschulschrift

ESAM controls opening of endothelial junctions via phosphorylation of VE-cadherin at Y685 residue

Tyrosine phosphorylation of Grb14 by Tie2

Tyrosine phosphorylation of NO-sensitive guanylyl cyclase

Interplay between neural-cadherin and vascular endothelial-cadherin in breast cancer progression

Vascular endothelial cadherin is an endostatin receptor

Hochschulschrift

The proteine tyrosine phosphatase VE-PTP controls endothelial cell contacts via VE-cadherin and Tie-2

Tyrosine-protein kinase Yes controls endothelial junctional plasticity and barrier integrity by regulating VE-cadherin phosphorylation and endocytosis

Hochschulschrift

Regulation of VE-cadherin tyrosine 731 phosphorylation under basal and inflammatory conditions

Correction to: Disruption of endothelial adherens junctions by high glucose is mediated by protein kinase C-β–dependent vascular endothelial cadherin tyrosine phosphorylation

Angiotensin II impairs endothelial function via tyrosine phosphorylation of the endothelial nitric oxide synthase

VE-PTP and VE-cadherin ectodomains interact to facilitate regulation of phosphorylation and cell contacts

Hochschulschrift

ESAM controls opening of endothelial junctions via phosphorylation of VE-cadherin at Y685 residue

Tyrosine phosphorylation of Grb14 by Tie2

Tyrosine phosphorylation of NO-sensitive guanylyl cyclase

Interplay between neural-cadherin and vascular endothelial-cadherin in breast cancer progression

Vascular endothelial cadherin is an endostatin receptor

Hochschulschrift

The proteine tyrosine phosphatase VE-PTP controls endothelial cell contacts via VE-cadherin and Tie-2

Tyrosine-protein kinase Yes controls endothelial junctional plasticity and barrier integrity by regulating VE-cadherin phosphorylation and endocytosis

Hochschulschrift

Regulation of VE-cadherin tyrosine 731 phosphorylation under basal and inflammatory conditions

Correction to: Disruption of endothelial adherens junctions by high glucose is mediated by protein kinase C-β–dependent vascular endothelial cadherin tyrosine phosphorylation

Angiotensin II impairs endothelial function via tyrosine phosphorylation of the endothelial nitric oxide synthase

VE-PTP and VE-cadherin ectodomains interact to facilitate regulation of phosphorylation and cell contacts

Hochschulschrift

ESAM controls opening of endothelial junctions via phosphorylation of VE-cadherin at Y685 residue

Tyrosine phosphorylation of Grb14 by Tie2

Tyrosine phosphorylation of NO-sensitive guanylyl cyclase

Interplay between neural-cadherin and vascular endothelial-cadherin in breast cancer progression

Vascular endothelial cadherin is an endostatin receptor

Cultural heritage institutions wishing to register will find more information here.

Fields marked * need to be filled in.

Username*

Please enter your username

Email*

Please enter your email address

Please do not fill this field

First name

Last name

Password*

Please enter your password

Confirm password*

Please enter the same password

I have read the terms of use and the privacy policy for the collection of personal data and accept them. *

This field is required.

I would like to subscribe to the newsletter of the Deutsche Digitale Bibliothek. See newsletter subscription info.

Account created

Your "My DDB" account has been successfully created. Before you can log in to your account, you must click the confirmation link in the message we just sent to the email address you provided.

The role of VE-cadherin tyrosine phosphorylation for the control of endothelial cell contacts

Object Details

Classification and Topics

Contributors, Places and Time

Further information

Data provider

Object type

Associated

Other Objects (12)

The proteine tyrosine phosphatase VE-PTP controls endothelial cell contacts via VE-cadherin and Tie-2

Tyrosine-protein kinase Yes controls endothelial junctional plasticity and barrier integrity by regulating VE-cadherin phosphorylation and endocytosis

Regulation of VE-cadherin tyrosine 731 phosphorylation under basal and inflammatory conditions

Correction to: Disruption of endothelial adherens junctions by high glucose is mediated by protein kinase C-β–dependent vascular endothelial cadherin tyrosine phosphorylation

Angiotensin II impairs endothelial function via tyrosine phosphorylation of the endothelial nitric oxide synthase

VE-PTP and VE-cadherin ectodomains interact to facilitate regulation of phosphorylation and cell contacts

ESAM controls opening of endothelial junctions via phosphorylation of VE-cadherin at Y685 residue

Tyrosine phosphorylation of Grb14 by Tie2

Tyrosine phosphorylation of NO-sensitive guanylyl cyclase

Tyrosine phosphorylation of NO-sensitive guanylyl cyclase

Interplay between neural-cadherin and vascular endothelial-cadherin in breast cancer progression

Vascular endothelial cadherin is an endostatin receptor

The proteine tyrosine phosphatase VE-PTP controls endothelial cell contacts via VE-cadherin and Tie-2

Tyrosine-protein kinase Yes controls endothelial junctional plasticity and barrier integrity by regulating VE-cadherin phosphorylation and endocytosis

Regulation of VE-cadherin tyrosine 731 phosphorylation under basal and inflammatory conditions

Correction to: Disruption of endothelial adherens junctions by high glucose is mediated by protein kinase C-β–dependent vascular endothelial cadherin tyrosine phosphorylation

Angiotensin II impairs endothelial function via tyrosine phosphorylation of the endothelial nitric oxide synthase

VE-PTP and VE-cadherin ectodomains interact to facilitate regulation of phosphorylation and cell contacts

ESAM controls opening of endothelial junctions via phosphorylation of VE-cadherin at Y685 residue

Tyrosine phosphorylation of Grb14 by Tie2

Tyrosine phosphorylation of NO-sensitive guanylyl cyclase

Tyrosine phosphorylation of NO-sensitive guanylyl cyclase

Interplay between neural-cadherin and vascular endothelial-cadherin in breast cancer progression

Vascular endothelial cadherin is an endostatin receptor

The proteine tyrosine phosphatase VE-PTP controls endothelial cell contacts via VE-cadherin and Tie-2

Tyrosine-protein kinase Yes controls endothelial junctional plasticity and barrier integrity by regulating VE-cadherin phosphorylation and endocytosis

Regulation of VE-cadherin tyrosine 731 phosphorylation under basal and inflammatory conditions

Correction to: Disruption of endothelial adherens junctions by high glucose is mediated by protein kinase C-β–dependent vascular endothelial cadherin tyrosine phosphorylation

Angiotensin II impairs endothelial function via tyrosine phosphorylation of the endothelial nitric oxide synthase

VE-PTP and VE-cadherin ectodomains interact to facilitate regulation of phosphorylation and cell contacts

ESAM controls opening of endothelial junctions via phosphorylation of VE-cadherin at Y685 residue

Tyrosine phosphorylation of Grb14 by Tie2

Tyrosine phosphorylation of NO-sensitive guanylyl cyclase

Tyrosine phosphorylation of NO-sensitive guanylyl cyclase

Interplay between neural-cadherin and vascular endothelial-cadherin in breast cancer progression

Vascular endothelial cadherin is an endostatin receptor

Related objects

Reset password