University of Nebraska–Lincoln

About: University of Nebraska–Lincoln is a education organization based out in Lincoln, Nebraska, United States. It is known for research contribution in the topics: Population & Poison control. The organization has 28059 authors who have published 61544 publications receiving 2139104 citations. The organization is also known as: Nebraska & UNL.

Life with carbon monoxide.

Abstract: This review focuses on how microbes live on CO as a sole source of carbon and energy and with CO by generating carbon monoxide as a metabolic intermediate. The use of CO is a property of organisms that use the Wood-L jungdahl pathway of autotrophic growth. The review discusses when CO metabolism originated, when and how it was discovered, and what properties of CO are ideal for microbial growth. How CO sensing by a heme-containing transcriptional regulatory protein activates the expression of CO metabolism-linked genes is described. Two metalloenzymes are the cornerstones of growth with CO: CO dehydrogenase (CODH) and acetyl-CoA synthase (ACS). CODH oxidizes CO to CO2, providing low-potential electrons for the cell, or alternatively reduces CO2 to CO. The latter reaction, when coupled to ACS, forms a machine for generating acetyl-CoA from CO2 for cell carbon synthesis. The recently solved crystal structures of CODH and ACS along with spectroscopic measurements and computational studies provide insights into novel bio-organometallic catalytic mechanisms and into the nature of a 140 A gas channel that coordinates the generation and utilization of CO. The enzymes that are coupled to CODH/ACS are also described, with a focus on a corrinoid protein, a methyltransferase, and pyruvate ferredoxin oxidoreductase.

Antibodies to citrullinated alpha-enolase peptide 1 are specific for rheumatoid arthritis and cross-react with bacterial enolase.

Abstract: Objective To map the antibody response to human citrullinated α-enolase, a candidate autoantigen in rheumatoid arthritis (RA), and to examine cross-reactivity with bacterial enolase. Methods Serum samples obtained from patients with RA, disease control subjects, and healthy control subjects were tested by enzyme-linked immunosorbent assay (ELISA) for reactivity with citrullinated α-enolase peptides. Antibodies specific for the immunodominant epitope were raised in rabbits or were purified from RA sera. Cross-reactivity with other citrullinated epitopes was investigated by inhibition ELISAs, and cross-reactivity with bacterial enolase was investigated by immunoblotting. Results An immunodominant peptide, citrullinated α-enolase peptide 1, was identified. Antibodies to this epitope were observed in 37–62% of sera obtained from patients with RA, 3% of sera obtained from disease control subjects, and 2% of sera obtained from healthy control subjects. Binding was inhibited with homologous peptide but not with the arginine-containing control peptide or with 4 citrullinated peptides from elsewhere on the molecule, indicating that antibody binding was dependent on both citrulline and flanking amino acids. The immunodominant peptide showed 82% homology with enolase from Porphyromonas gingivalis, and the levels of antibodies to citrullinated α-enolase peptide 1 correlated with the levels of antibodies to the bacterial peptide (r2 = 0.803, P < 0.0001). Affinity-purified antibodies to the human peptide cross-reacted with citrullinated recombinant P gingivalis enolase. Conclusion We have identified an immunodominant epitope in citrullinated α-enolase, to which antibodies are specific for RA. Our data on sequence similarity and cross-reactivity with bacterial enolase may indicate a role for bacterial infection, particularly with P gingivalis, in priming autoimmunity in a subset of patients with RA.

Incorporating varying test costs and fault severities into test case prioritization

Abstract: Test case prioritization techniques schedule test cases for regression testing in an order that increases their ability to meet some performance goal. One performance goal, rate of fault detection, measures how quickly faults are detected within the testing process. In previous work (S. Elbaum et al., 2000; G. Rothermel et al., 1999), we provided a metric, APFD, for measuring rate of fault detection, and techniques for prioritizing test cases to improve APFD, and reported the results of experiments using those techniques. This metric and these techniques, however, applied only in cases in which test costs and fault severity are uniform. We present a new metric for assessing the rate of fault detection of prioritized test cases that incorporates varying test case and fault costs. We present the results of a case study illustrating the application of the metric. This study raises several practical questions that might arise in applying test case prioritization; we discuss how practitioners could go about answering these questions.