Suchergebnisse - "Treharne, Kate J"

PubPharm (35)

1

Expression of wild-type CFTR suppresses NF-kappaB-driven inflammatory signalling

enthalten in: PloS one | 2010

von Hunter, M. | Treharne, K. | Winter, A. | +3

2

Cystic fibrosis transmembrane regulator fragments with the Phe508 deletion exert a dual allosteric control over the master kinase CK2

enthalten in: The Biochemical journal | 2010

von Pagano, M. | Marin, O. | Cozza, G. | +5

3

Poly(A)-binding protein (PABP): a common viral target

enthalten in: The biochemical journal | 2010

von Pagano, M. | Marin, O. | Cozza, G. | +5

4

The phosphorylation status of membrane-bound nucleoside diphosphate kinase in epithelia and the role of AMP

enthalten in: Molecular and cellular biochemistry | 2009

von Treharne, K. | Best, O. | Mehta, A.

5

Transglutaminase 2 and nucleoside diphosphate kinase activity are correlated in epithelial membranes and are abnormal in cystic fibrosis

enthalten in: FEBS letters | 2009

von Treharne, K. | Giles Best, O. | Mehta, A.

6

Epithelial IgG and its relationship to the loss of F508 in the common mutant form of the cystic fibrosis transmembrane conductance regulator

enthalten in: FEBS letters | 2009

von Treharne, K. | Cassidy, D. | Goddard, C. | +3

7

The phosphorylation status of membrane-bound nucleoside diphosphate kinase in epithelia and the role of AMP

enthalten in: Molecular and cellular biochemistry | 2009

von Treharne, K. | Best, O. | Mehta, A.

8

The phosphorylation status of membrane-bound nucleoside diphosphate kinase in epithelia and the role of AMP

enthalten in: Molecular and cellular biochemistry | 2009

von Treharne, K. | Best, O. | Mehta, A.

9

The phosphorylation status of membrane-bound nucleoside diphosphate kinase in epithelia and the role of AMP

enthalten in: Molecular and cellular biochemistry | 2009

von Treharne, K. | Best, O. | Mehta, A.

10

Mechanistic insight into control of CFTR by AMPK

enthalten in: The Journal of biological chemistry | 2009

von Kongsuphol, P. | Cassidy, D. | Hieke, B. | +4