I. Charlestown ferry bound volume, 1707-1806

This series contains sixty-nine documents related to the College's interest in the Charlestown ferry between 1707 and 1806 that were gathered together, arranged in chronological order, and pasted into a bound volume at an undetermined date. The majority of documents are leases and bonds with the ferrymen, as well as handwritten copies of Corporation petitions to the General Court regarding ferry fares and bridge development. The series also includes handwritten legal opinions composed by Levi Lincoln and Nathan Dane for the College analyzing the rights of the College to transportation-related income.

Buildings records, bound volume, 1811-1838

This bound volume, likely assembled by the Corporation in the 1850s, contains documents related to Harvard buildings which have been pasted onto the pages. The volume consists of correspondence and memoranda pertaining to the construction of Holworthy Hall, 1811-1812; contracts and correspondence relating to the construction of University Hall, 1813-1814; and correspondence regarding repairs to Massachusetts Hall overseen by Loammi Baldwin in 1812. Additional records pertaining to the construction of Gore Hall, 1834-1838; and the repairs to the Medical College on Mason Street in Boston, 1824 are also located in this volume.

The Structure of theCyprinid herpesvirus 3ORF112-Zα·Z-DNA Complex Reveals a Mechanism of Nucleic Acids Recognition Conserved with E3L, a Poxvirus Inhibitor of Interferon Response

In vertebrate species, the innate immune system down-regulates protein translation in response to viral infection through the action of the double-stranded RNA (dsRNA)-activated protein kinase (PKR). In some teleost species another protein kinase, Z-DNA-dependent protein kinase (PKZ), plays a similar role but instead of dsRNA binding domains, PKZ has Zα domains. These domains recognize the left-handed conformer of dsDNA and dsRNA known as Z-DNA/Z-RNA. Cyprinid herpesvirus 3 infects common and koi carp, which have PKZ, and encodes the ORF112 protein that itself bears a Zα domain, a putative competitive inhibitor of PKZ. Here we present the crystal structure of ORF112-Zα in complex with an 18-bp CpG DNA repeat, at 1.5 Å. We demonstrate that the bound DNA is in the left-handed conformation and identify key interactions for the specificity of ORF112. Localization of ORF112 protein in stress granules induced in Cyprinid herpesvirus 3-infected fish cells suggests a functional behavior similar to that of Zα domains of the interferon-regulated, nucleic acid surveillance proteins ADAR1 and DAI.

Counseling Hispanic college-bound high school students /

Distributed to depository libraries in microfiche.