Samuel E Lux
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Explore the profile of Samuel E Lux including associated specialties, affiliations and a list of published articles.
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12
Citations
262
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Recent Articles
1.
Gross C, OHalloran C, Winn A, Lux S, Michelson C, Sectish T, et al.
Acad Pediatr
. 2020 Apr;
20(7):1007-1012.
PMID: 32268217
Objective: Our goal was to identify aspects of residency applications predictive of subsequent performance during pediatric internship. Methods: We conducted a retrospective cohort study of graduates of US medical schools...
2.
Stewart A, Shmukler B, Vandorpe D, Rivera A, Heneghan J, Li X, et al.
Am J Physiol Cell Physiol
. 2011 Aug;
301(6):C1325-43.
PMID: 21849667
Four patients with overhydrated cation leak stomatocytosis (OHSt) exhibited the heterozygous RhAG missense mutation F65S. OHSt erythrocytes were osmotically fragile, with elevated Na and decreased K contents and increased cation...
3.
Korsgren C, Lux S
Blood
. 2010 Jun;
116(14):2600-7.
PMID: 20585040
Spectrin and protein 4.1R crosslink F-actin, forming the membrane skeleton. Actin and 4.1R bind to one end of β-spectrin. The adjacent end of α-spectrin, called the EF domain, is calmodulin-like,...
4.
Stankewich M, Gwynn B, Ardito T, Ji L, Kim J, Robledo R, et al.
Proc Natl Acad Sci U S A
. 2010 Mar;
107(13):6022-7.
PMID: 20231455
The spectrin membrane skeleton controls the disposition of selected membrane channels, receptors, and transporters. In the brain betaIII spectrin binds directly to the excitatory amino acid transporter (EAAT4), the glutamate...
5.
Robledo R, Lambert A, Birkenmeier C, Cirlan M, Cirlan A, Campagna D, et al.
Blood
. 2010 Jan;
115(9):1804-14.
PMID: 20056793
Five spontaneous, allelic mutations in the alpha-spectrin gene, Spna1, have been identified in mice (spherocytosis [sph], sph(1J), sph(2J), sph(2BC), sph(Dem)). All cause severe hemolytic anemia. Here, analysis of 3 new...
6.
Korsgren C, Peters L, Lux S
J Biol Chem
. 2009 Dec;
285(7):4757-70.
PMID: 20007969
Spectrin and protein 4.1 cross-link F-actin protofilaments into a network called the membrane skeleton. Actin and 4.1 bind to one end of beta-spectrin. The adjacent end of alpha-spectrin, called the...
7.
8.
An X, Debnath G, Guo X, Liu S, Lux S, Baines A, et al.
Biochemistry
. 2005 Aug;
44(31):10681-8.
PMID: 16060676
The ternary complex of spectrin, F-actin, and protein 4.1R defines the erythrocyte membrane skeletal network, which governs the stability and elasticity of the membrane. It has been shown that both...
9.
Eber S, Lux S
Semin Hematol
. 2004 Apr;
41(2):118-41.
PMID: 15071790
The molecular causes of hereditary spherocytosis (HS) have been unraveled in the past decade. No frequent defect is found, and nearly every family has a unique mutation. In dominant HS,...
10.
Peters L, Swearingen R, Andersen S, Gwynn B, Lambert A, Li R, et al.
Blood
. 2004 Apr;
103(8):3233-40.
PMID: 15070709
Defects in red blood cell (RBC) membrane skeleton components cause hereditary spherocytosis (HS). Clinically, HS varies significantly even among individuals with identical gene defects, illustrating the profound effects of genetic...