21 research outputs found
ROBERT LORWAY , Namibia's Rainbow Project: gay rights in an African nation. Bloomington IN: Indiana University Press (hb 24 – 978 0 253 01520 4). 2015, 155 pp.
Collected Presentations of the CIC ILL Directors Meeting at the University of Maryland, October 21-22, 2015
Collected presentations from the in-person meeting of the CIC ILL Directors at the University of Maryland, October 21-22, 2015. Presentations cover such topics as interlibrary loan and special collections, course reserves and interlibrary loan services for textbooks, data analysis of interlibrary borrowing and lending among CIC institutions, and Relais Web Services implementation. Presenters' affiliations include: University of Maryland, University of Illinois Urbana-Champaign, Northwestern University, University of Minnesota, Michigan State University, and OCLC.Committee on Institutional Cooperation
University of Maryland Librarie
Morphine drug discrimination testing and substitution assessments in adult male Sprague–Dawley rats
The THC Tetrad Test: Characterization, Evaluation, and Screening of WIN55 212-2 and Other Test Substances in Wistar Han Rats
Morphine Drug Discrimination Testing and Substitution Assessments in Adult Male Sprague–Dawley Rats
Team Scaffolds: How Mesolevel Structures Enable Role-Based Coordination in Temporary Groups
Short and Long-Term Delayed Reassessment of Drug Discrimination Testing in Adult Female SD Rats
Calpain 3, the "gatekeeper" of proper sarcomere assembly, turnover and maintenance.
Calpain 3 is a member of the calpain family of calcium-dependent intracellular proteases. Thirteen years ago it was discovered that mutations in calpain 3 (CAPN3) result in an autosomal recessive and progressive form of limb girdle muscular dystrophy called limb girdle muscular dystrophy type 2A. While calpain 3 mRNA is expressed at high levels in muscle and appears to have some role in developmental processes, muscles of patients and mice lacking calpain 3 still form apparently normal muscle during prenatal development; thus, a functional calpain 3 protease is not mandatory for muscle to form in vivo but it is a pre-requisite for muscle to remain healthy. Despite intensive research in this field, the physiological substrates of the calpain 3 protein (hereafter referred to as CAPN3) and its alternatively spliced isoforms remain elusive. The existence of these multiple isoforms complicates the search for the physiological functions of CAPN3 and its pathophysiological role. In this review, we summarize the genetic and biochemical evidence that point to loss of function of the full-length isoform of CAPN3, also known as p94, as the pathogenic isoform. We also argue that its natural substrates must reside in its proximity within the sarcomere where it is stored in an inactive state anchored to titin. We further propose that CAPN3 has many attributes that make it ideally suited as a sensor of sarcomeric integrity and function, involved in its repair and maintenance. Loss of these CAPN3-mediated activities can explain the "progressive" development of muscular dystrophy