Topography of Thebes, and general view of Egypt : being a short account of the principal objects worthy of notice in the valley of the Nile... ; with remarks on the manners and customs of the ancient Egyptians and the productions of the country /

Mode of access: Internet.

Livingstone and his African explorations: together with a full account of the Young, Stanley, and Dawson search expeditions; chapters on ancient & modern Nile discovery; on the central African slave trade, &c., &c.

Mode of access: Internet.

My winter on the Nile /

Includes index.

Notes for the Nile, together with a metrical rendering of the hymns of ancient Egypt and of the Precepts of Ptah-hotep (the oldest book in the world)

Mode of access: Internet.

Journal of the discovery of the source of the Nile.

Photocopy.

Through the Dark Continent : or, The sources of the Nile around the Great Lakes of equatorial Africa and down the Livingstone River to the Atlantic Ocean /

Includes index.

Moses: a story of the Nile.

Photocopy.

Valley of the Nile ...

Includes bibliography.

The Nile boat; or, glimpses of the land of Egypt.

Mode of access: Internet.

A master-builder on the Nile : being a record of the life and aims of John Hogg, D. D., Christian missionary /

Includes index.

The lotus of the Nile, and other poems.

Mode of access: Internet.

Travels to discover the source of the Nile in the years 1768, 1769, 1770, 1771, 1772, & 1773.

Vol. 8 contains the plates and maps.

West nile virus core protein: Tetramer structure and ribbon formation

We have determined the crystal structure of the core (C) protein from the Kunjin subtype of West Nile virus (WNV), closely related to the NY99 strain of WNV, currently a major health threat in the U.S. WNV is a member of the Flaviviridae family of enveloped RNA viruses that contains many important human pathogens. The C protein is associated with the RNA genome and forms the internal core which is surrounded by the envelope in the virion. The C protein structure contains four a. helices and forms dimers that are organized into tetramers. The tetramers form extended filamentous ribbons resembling the stacked alpha helices seen in HEAT protein structures.

West Nile virus vaccines

West Nile virus (WNV) is a mosquito-borne flavivirus that is emerging as a global pathogen. In the last decade, virulent strains of the virus have been associated with significant outbreaks of human and animal disease in Europe, the Middle East and North America. Efforts to develop human and veterinary vaccines have taken both traditional and novel approaches. A formalin-inactivated whole virus vaccine has been approved for use in horses. DNA vaccines coding for the structural WNV proteins have also been assessed for veterinary use and have been found to be protective in mice, horses and birds. Live attenuated yellow fever WNV chimeric vaccines have also been successful in animals and are currently undergoing human trials. Additional studies have shown that immunisation with a relatively benign Australian variant of WNV, the Kunjin virus, also provides protective immunity against the virulent North American strain. Levels of efficacy and safety, as well as logistical, economic and environmental issues, must all be carefully considered before vaccine candidates are approved and selected for large-scale manufacture and distribution.

Enzymatic characterization and homology model of a catalytically active recombinant West Nile virus NS3 protease

West Nile Virus (WNV) is a mosquito-borne flavivirus with a rapidly expanding global distribution. Infection causes severe neurological disease and fatalities in both human and animal hosts. The West Nile viral protease (NS2B-NS3) is essential for post-translational processing in host-infected cells of a viral polypeptide precursor into structural and functional viral proteins, and its inhibition could represent a potential treatment for viral infections. This article describes the design, expression, and enzymatic characterization of a catalytically active recombinant WNV protease, consisting of a 40-residue component of cofactor NS2B tethered via a noncleavable nonapeptide (G(4)SG(4)) to the N-terminal 184 residues of NS3. A chromogenic assay using synthetic para-nitroanilide (pNA) hexapeptide substrates was used to identify optimal enzyme-processing conditions (pH 9.5, I < 0.1 M, 30% glycerol, 1 mM CHAPS), preferred substrate cleavage sites, and the first competitive inhibitor (Ac-FASGKR- H, IC50 &SIM; 1 μM). A putative three-dimensional structure of WNV protease, created through homology modeling based on the crystal structures of Dengue-2 and Hepatitis C NS3 viral proteases, provides some valuable insights for structure-based design of potent and selective inhibitors of WNV protease.