Functional electrical stimulation for foot drop in multiple sclerosis: a systematic review and meta-analysis of the effect on gait speed

Objective: To review the efficacy of functional electrical stimulation (FES) used for foot drop in people with multiple sclerosis (pwMS) on gait speed in short and long walking performance tests. Data sources: Five databases (Cochrane Library, CINAHL, Embase, MEDLINE, Pubmed) and reference lists were searched. Study selection: Studies of both observational and experimental design where gait speed data in pwMS could be extracted were included. Data extraction: Data were independently extracted and recorded. Methodological quality was assessed using the Effective Public Health Practice Project (EPHPP) tool. Data synthesis: Nineteen studies (described in 20 articles) recruiting 490 pwMS were identified and rated moderate or weak, with none gaining a strong rating. All studies rated weak for blinding. Initial and ongoing orthotic and therapeutic effects were assessed with regards to the impact of FES on gait speed in short and long walking tests. Meta-analyses of the short walk tests revealed a significant initial orthotic effect (t = 2.14, p = 0.016) with a mean increase in gait speed of 0.05 meters per second (m/s) and ongoing orthotic effect (t = 2.81, p = 0.003) with a mean increase of 0.08m/s. There were no initial or ongoing effect on gait speed in long walk tests and no therapeutic effect on gait speed in either short or long walk tests. Conclusions: FES used for foot drop has a positive initial and ongoing effect on gait speed in short walking tests. Further fully-powered randomized controlled trials comparing FES with alternative treatments are required

The Grizzly, September 17, 1982

New Ursinus Students Welcomed • Lantern Needs Associate Editor • Vandalism at Myrin • Administration Alterations • Committee Needs Chairmen • Folk Festival Summer Fun • Forum Preview • Lewis on Wall Street • Fencing Anyone? • Sendai Students at UC • Changes in Wismer • USGA Notes • Field Hockey Falls to Trenton State • The Bear Pack is in Top Form, Again • Volleyball Dumps Del Val • Grizzlies Drop Football Opener • Soccer Team Loses Two Close Oneshttps://digitalcommons.ursinus.edu/grizzlynews/1081/thumbnail.jp

The Grizzly, October 1, 1982

Professors Leave on Sabbatical • New Record Breaker Theme is Photograph • McNamara Displays Hoop Skill • Letter to a Confused Freshman • Ursinus Welcomes New Dean • Letters to the Editor • Opinion: Campus Crime has got to Stop! • It Takes a Trained Eye • GOP\u27s Strategy in \u2782 • The Who Rock JFK • Magnificent Noise • Roving Reporter: What do You Consider to be the Most Positive Aspect of Ursinus College? • I\u27m Turning Japanese • Field Hockey Team Wins 5th Straight • 1982 Ursinus Grizzly Football Stats • Grizzlies Capture First Win! • Grizzlies to Play in Newly Formed Conference • X-Country Streak Broken • Soccer Suffers Setback • Girls\u27 Volleyball Lose Twohttps://digitalcommons.ursinus.edu/grizzlynews/1083/thumbnail.jp

Accurate computational design of multipass transmembrane proteins

The computational design of transmembrane proteins with more than one membrane-spanning region remains a major challenge. We report the design of transmembrane monomers, homodimers, trimers, and tetramers with 76 to 215 residue subunits containing two to four membrane-spanning regions and up to 860 total residues that adopt the target oligomerization state in detergent solution. The designed proteins localize to the plasma membrane in bacteria and in mammalian cells, and magnetic tweezer unfolding experiments in the membrane indicate that they are very stable. Crystal structures of the designed dimer and tetramer-a rocket-shaped structure with a wide cytoplasmic base that funnels into eight transmembrane helices-are very close to the design models. Our results pave the way for the design of multispan membrane proteins with new functions

Accurate computational design of multipass transmembrane proteins

The computational design of transmembrane proteins with more than one membrane-spanning region remains a major challenge. We report the design of transmembrane monomers, homodimers, trimers, and tetramers with 76 to 215 residue subunits containing two to four membrane-spanning regions and up to 860 total residues that adopt the target oligomerization state in detergent solution. The designed proteins localize to the plasma membrane in bacteria and in mammalian cells, and magnetic tweezer unfolding experiments in the membrane indicate that they are very stable. Crystal structures of the designed dimer and tetramer-a rocket-shaped structure with a wide cytoplasmic base that funnels into eight transmembrane helices-are very close to the design models. Our results pave the way for the design of multispan membrane proteins with new functions