K. Wyatt

发表

Gene duplication and separation of functions in alphaB-crystallin from zebrafish (Danio rerio).

M. Posner, G. Wistow, J. Zigler, 2006, The FEBS journal.

Lengsin is a survivor of an ancient family of class I glutamine synthetases in eukaryotes that has undergone evolutionary re-engineering for a role in the vertebrate eye lens.

H. White, K. Wyatt, 2008 .

The P23T Cataract Mutation Causes Loss of Solubility of Folded γD-Crystallin

B. Wallace, G. Wistow, C. Slingsby, 2004 .

A single destabilizing mutation (F9S) promotes concerted unfolding of an entire globular domain in gammaS-crystallin.

Soojin Lee, G. Wistow, Lijin Dong, 2010, Journal of molecular biology.

The klotho‐related protein KLPH (lctl) has preferred expression in lens and is essential for expression of clic5 and normal lens suture formation

Jianguo Fan, G. Wistow, Lijin Dong, 2018, Experimental eye research.

A Role for Lengsin, a Recruited Enzyme, in Terminal Differentiation in the Vertebrate Lens*

R. Fariss, G. Wistow, C. Gao, 2008, Journal of Biological Chemistry.

Endogenous retroviral insertion in Cryge in the mouse No3 cataract mutant.

M. Lyon, Nabanita Nag, G. Wistow, 2007, Genomics.

Lengsin is a survivor of an ancient family of class I glutamine synthetases re-engineered by evolution for a role in the vertebrate lens.

Graeme Wistow, Elena V Orlova, Christine Slingsby, 2006, Structure.

γN‐crystallin and the evolution of the βγ‐crystallin superfamily in vertebrates

L. Segovia, S. Bernstein, L. David, 2005, The FEBS journal.

Platelet-derived Growth Factor D, Tissue-specific Expression in the Eye, and a Key Role in Control of Lens Epithelial Cell Proliferation*

R. Fariss, G. Wistow, P. Zelenka, 2005, Journal of Biological Chemistry.

Gene duplication and separation of functions in αB‐crystallin from zebrafish (Danio rerio)

M. Posner, G. Wistow, T. Vihtelic, 2006 .

Solution structure of γS‐crystallin by molecular fragment replacement NMR

Graeme Wistow, Ad Bax, Frank Delaglio, 2005 .

Solution structure of (gamma)S-crystallin by molecular fragment replacement NMR.

A. Bax, F. Delaglio, G. Wistow, 2005, Protein science : a publication of the Protein Society.

The P23T cataract mutation causes loss of solubility of folded gammaD-crystallin.

B. Wallace, G. Wistow, C. Slingsby, 2004, Journal of molecular biology.

Biophysical properties of gammaC-crystallin in human and mouse eye lens: the role of molecular dipoles.

L. David, A. Purkiss, P. Wilmarth, 2007, Journal of molecular biology.