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Centre for Misfolding Diseases

Research Associate

Publications

Receptor protein tyrosine phosphatases are novel components of a polycystin complex.
CA Boucher, HH Ward, RL Case, KS Thurston, X Li, A Needham, E Romero, D Hyink, S Qamar, T Roitbak, S Powell, C Ward, PD Wilson, A Wandinger-Ness, RN Sandford
– Biochimica et Biophysica Acta - Molecular Basis of Disease
(2010)
1812,
1225
Non-native interactions are critical for mechanical strength in PKD domains.
JR Forman, ZT Yew, S Qamar, RN Sandford, E Paci, J Clarke
– Structure (London, England : 1993)
(2009)
17,
1582
Identification of arginine 331 as an important active site residue in the Class II fructose‐1,6‐bisphosphate aldolase of Escherichia coli
S Qamar, K Marsh, A Berry
– Protein Sci
(2008)
5,
154
Human H+ATPase a4 subunit mutations causing renal tubular acidosis reveal a role for interaction with phosphofructokinase-1
Y Su, KG Blake-Palmer, S Sorrell, B Javid, K Bowers, A Zhou, SH Chang, S Qamar, FE Karet
– American Journal of Physiology - Renal Physiology
(2008)
295,
f950
TRP channels and kidney disease: lessons from polycystic kidney disease.
S Qamar, M Vadivelu, R Sandford
– Biochemical Society transactions
(2007)
35,
124
The Remarkable Mechanical Strength of Polycystin-1 Supports a Direct Role in Mechanotransduction
JR Forman, S Qamar, E Paci, RN Sandford, J Clarke
– Journal of molecular biology
(2005)
349,
861
The remarkable mechanical strength of polycystin-1 suggests a novel mechanism for mechanotransduction
JR Forman, S Qamar, RN Sandford, J Clarke
– BIOPHYSICAL JOURNAL
(2005)
88,
585A
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Postdoctoral researcher

Telephone number

01223 336359

Email address