Modeling lifetime greenhouse gas emissions associated with materials for various end-of-life treatments.

This research has developed mathematical models for computing lifetime greenhouse gas (GHG) emissions associated with materials. The models include embodied carbon (EC) emissions from the manufacture of materials, and GHG emissions from incineration, or landfill gas (LFG) production from landfill disposal of the material beyond their service lives. The models are applicable to all materials; however, their applications here are demonstrated for the lumber from a residential building with 50- and 100-year service lives, and with incineration, landfill, and deconstruction as end-of-life treatments.

Penicillin-binding protein 7/8 contributes to the survival of Acinetobacter baumannii in vitro and in vivo.

Background: Acinetobacter baumannii is a bacterial pathogen of increasing medical importance. Little is known about genes important for its survival in vivo.

Methods And Results: Screening of random transposon mutants of the model pathogen AB307-0294 identified the mutant AB307.

Comparative genome sequence analysis of multidrug-resistant Acinetobacter baumannii.

The recent emergence of multidrug resistance (MDR) in Acinetobacter baumannii has raised concern in health care settings worldwide. In order to understand the repertoire of resistance determinants and their organization and origins, we compared the genome sequences of three MDR and three drug-susceptible A. baumannii isolates.

Heat shock proteins and scavenger receptors: role in adaptive immune responses.

Tumor-derived heat shock proteins have shown promise as anti-cancer vaccines in clinical trials. Heat shock proteins (HSPs) can generate potent anti-tumor immunity and elicit antigen-specific CD8+ T cell responses in murine studies. Antigen presenting cells (APC), such as macrophages and dendritic cells (DCs), can elicit antigen-specific CD8+ T cell responses mediated by HSPs.

Heat shock proteins HSP70 and GP96: structural insights.

Several heat shock proteins (HSPs) act as potent adjuvants for eliciting anti-tumor immunity. HSP-based tumor vaccine strategies have been highly successful in animal models and are undergoing testing in clinical trials. It is generally accepted that HSPs, functioning as chaperones for tumor antigens, elicit tumor-specific adaptive immune responses.

Cancer immunotherapy and heat-shock proteins: promises and challenges.

Recent mechanistic studies on the role of heat-shock proteins (HSPs) to induce innate and adaptive immune responses have resulted in conflicting reports. Whereas some groups reported that HSPs have direct immunological function, others emphasised the endotoxin contamination of HSP preparations and questioned the antigen-specificity of HSP vaccines. The present review will discuss these issues and suggest that HSPs have diverse and distinct immunological functions that could be superimposed on effects resulting from endotoxin contamination or misunderstood by using experimental procedures with inadequate controls.

The chaperoning properties of mouse grp170, a member of the third family of hsp70 related proteins.

The 170 kDa glucose-regulated protein (grp170) is an endoplasmic reticulum resident protein that shares some sequence homology with both the hsp70 and hsp110 heat shock protein (hsp) families, yet is representative of a third and unique family of stress proteins. Despite observations indicating important roles in normal cellular functions, the in vitro chaperone properties of grp170 have not been rigorously examined. We have cloned mouse grp170 and expressed the recombinant protein in a baculovirus expression system.