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Institution

University of British Columbia

EducationVancouver, British Columbia, Canada
About: University of British Columbia is a education organization based out in Vancouver, British Columbia, Canada. It is known for research contribution in the topics: Population & Health care. The organization has 89939 authors who have published 209679 publications receiving 9226862 citations. The organization is also known as: UBC & The University of British Columbia.


Papers
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Journal ArticleDOI
TL;DR: In this article, advanced computer assisted design strategies that address the difficult problem of relating primary sequence to peptide structure, and are delivering more potent, cost-effective, broad-spectrum peptides as potential next-generation antibiotics.
Abstract: Multidrug-resistant bacteria are a severe threat to public health. Conventional antibiotics are becoming increasingly ineffective as a result of resistance, and it is imperative to find new antibacterial strategies. Natural antimicrobials, known as host defence peptides or antimicrobial peptides, defend host organisms against microbes but most have modest direct antibiotic activity. Enhanced variants have been developed using straightforward design and optimization strategies and are being tested clinically. Here, we describe advanced computer-assisted design strategies that address the difficult problem of relating primary sequence to peptide structure, and are delivering more potent, cost-effective, broad-spectrum peptides as potential next-generation antibiotics.

1,543 citations

Journal ArticleDOI
TL;DR: Intraocular pressure is part of the pathogenic process in normal-tension glaucoma and therapy that is effective in lowering intraocular pressure and free of adverse effects would be expected to be beneficial in patients who are at risk of disease progression.

1,542 citations

Journal ArticleDOI
01 Jul 1994-Science
TL;DR: This work has shown that with the use of the bacteriophage-derived, site-specific recombinase Cre in a transgenic approach, the same mutation can be selectively introduced into a particular cellular compartment-in this case, T cells.
Abstract: Deletion of the promoter and the first exon of the DNA polymerase beta gene (pol beta) in the mouse germ line results in a lethal phenotype. With the use of the bacteriophage-derived, site-specific recombinase Cre in a transgenic approach, the same mutation can be selectively introduced into a particular cellular compartment-in this case, T cells. The impact of the mutation on those cells can then be analyzed because the mutant animals are viable.

1,542 citations

Journal ArticleDOI
TL;DR: Characterization of unannotated and uncharacterized protein segments is expected to lead to the discovery of novel functions as well as provide important insights into existing biological processes and is likely to shed new light on molecular mechanisms of diseases that are not yet fully understood.
Abstract: 1.1. Uncharacterized Protein Segments Are a Source of Functional Novelty Over the past decade, we have observed a massive increase in the amount of information describing protein sequences from a variety of organisms.1,2 While this may reflect the diversity in sequence space, and possibly also in function space,3 a large proportion of the sequences lacks any useful function annotation.4,5 Often these sequences are annotated as putative or hypothetical proteins, and for the majority their functions still remain unknown.6,7 Suggestions about potential protein function, primarily molecular function, often come from computational analysis of their sequences. For instance, homology detection allows for the transfer of information from well-characterized protein segments to those with similar sequences that lack annotation of molecular function.8−10 Other aspects of function, such as the biological processes proteins participate in, may come from genetic- and disease-association studies, expression and interaction network data, and comparative genomics approaches that investigate genomic context.11−17 Characterization of unannotated and uncharacterized protein segments is expected to lead to the discovery of novel functions as well as provide important insights into existing biological processes. In addition, it is likely to shed new light on molecular mechanisms of diseases that are not yet fully understood. Thus, uncharacterized protein segments are likely to be a large source of functional novelty relevant for discovering new biology.

1,540 citations

Journal ArticleDOI
TL;DR: The first-order differential-difference factorization method as mentioned in this paper is an operational procedure which enables us to answer, in a direct manner, questions about eigenvalue problems which are of importance to physicists.
Abstract: The factorization method is an operational procedure which enables us to answer, in a direct manner, questions about eigenvalue problems which are of importance to physicists. The underlying idea is to consider a pair of first-order differential-difference equations which are equivalent to a given second-order differential equation with boundary conditions. For a large class of such differential equations the method enables us to find immediately the eigenvalues and a manufacturing process for the normalized eigenfunctions. These results are obtained merely by consulting a table of the six possible factorization types.The manufacturing process is also used for the calculation of transition probabilities.The method is generalized so that it will handle perturbation problems.

1,536 citations


Authors

Showing all 90682 results

NameH-indexPapersCitations
Gordon H. Guyatt2311620228631
John C. Morris1831441168413
Douglas Scott1781111185229
John R. Yates1771036129029
Deborah J. Cook173907148928
Richard A. Gibbs172889249708
Evan E. Eichler170567150409
James F. Sallis169825144836
Michael Snyder169840130225
Jiawei Han1681233143427
Michael Kramer1671713127224
Bruce L. Miller1631153115975
Peter A. R. Ade1621387138051
Marc W. Kirschner162457102145
Kaj Blennow1601845116237
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Performance
Metrics
No. of papers from the Institution in previous years
YearPapers
20241
2023307
20221,209
202113,228
202012,052
201910,934