Sandra L Harper
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Explore the profile of Sandra L Harper including associated specialties, affiliations and a list of published articles.
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16
Citations
233
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Recent Articles
11.
Sriswasdi S, Harper S, Tang H, Speicher D
J Proteome Res
. 2013 Dec;
13(2):898-914.
PMID: 24369724
Chemical cross-linking coupled to mass spectrometry provides structural information that is useful for probing protein conformations and providing experimental support for molecular models. "Zero-length" cross-links have greater value for these...
12.
Harper S, Sriswasdi S, Tang H, Gaetani M, Gallagher P, Speicher D
Blood
. 2013 Aug;
122(17):3045-53.
PMID: 23974198
Hereditary elliptocytosis (HE) and hereditary pyropoikilocytosis (HPP) are common disorders of erythrocyte shape primarily because of mutations in spectrin. The most common HE/HPP mutations are located distant from the critical...
13.
Li D, Harper S, Tang H, Maksimova Y, Gallagher P, Speicher D
J Biol Chem
. 2010 Jul;
285(38):29535-45.
PMID: 20610390
Spectrin dimer-tetramer interconversion is a critical contributor to red cell membrane stability, but some properties of spectrin tetramer formation cannot be studied effectively using monomeric recombinant domains. To address these...
14.
Ipsaro J, Harper S, Messick T, Marmorstein R, Mondragon A, Speicher D
Blood
. 2010 Mar;
115(23):4843-52.
PMID: 20197550
As the principal component of the membrane skeleton, spectrin confers integrity and flexibility to red cell membranes. Although this network involves many interactions, the most common hemolytic anemia mutations that...
15.
Harper S, Li D, Maksimova Y, Gallagher P, Speicher D
J Biol Chem
. 2010 Feb;
285(14):11003-12.
PMID: 20139081
Head-to-head assembly of two spectrin heterodimers to form an actin-cross-linking tetramer is a physiologically dynamic interaction that contributes to red cell membrane integrity. Recombinant beta-spectrin C-terminal and alpha-spectrin N-terminal peptides...
16.
Peng H, Gibson L, Capili A, Borden K, Osborne M, Harper S, et al.
J Mol Biol
. 2007 May;
370(2):269-89.
PMID: 17512541
The KRAB domain is a 75 amino acid transcriptional repression module that is encoded by more than 400 zinc finger protein genes, making it the most abundant repression domain in...