Kim N Ha
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Explore the profile of Kim N Ha including associated specialties, affiliations and a list of published articles.
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Recent Articles
1.
Olivieri C, Wang Y, Walker C, Veliparambil Subrahmanian M, Ha K, Bernlohr D, et al.
Elife
. 2024 Jun;
12.
PMID: 38913408
Allosteric cooperativity between ATP and substrates is a prominent characteristic of the cAMP-dependent catalytic subunit of protein kinase A (PKA-C). This long-range synergistic action is involved in substrate recognition and...
2.
Olivieri C, Wang Y, Walker C, Subrahmanian M, Ha K, Bernlohr D, et al.
bioRxiv
. 2023 Sep;
PMID: 37745542
Allosteric cooperativity between ATP and substrates is a prominent characteristic of the cAMP-dependent catalytic (C) subunit of protein kinase A (PKA). Not only this long-range synergistic action is involved in...
3.
Nelson S, Ha K, Gopinath T, Exline M, Mascioni A, Thomas D, et al.
Biochim Biophys Acta Biomembr
. 2018 Mar;
1860(6):1335-1341.
PMID: 29501609
Approximately, 70% of the Ca ion transport into the sarcoplasmic reticulum is catalyzed by the sarcoplasmic reticulum Ca-ATPase (SERCA), whose activity is endogenously regulated by phospholamban (PLN). PLN comprises a...
4.
Vostrikov V, Soller K, Ha K, Gopinath T, Veglia G
Biochim Biophys Acta
. 2014 Sep;
1848(1 Pt B):315-22.
PMID: 25251363
Phospholamban (PLN) is a single-pass membrane protein that regulates the sarco(endo)plasmic reticulum Ca²⁺-ATPase (SERCA). Phosphorylation of PLN at Ser16 reverses its inhibitory function under β-adrenergic stimulation, augmenting Ca²⁺ uptake in...
5.
Ha K, Gustavsson M, Veglia G
J Muscle Res Cell Motil
. 2012 Sep;
33(6):485-92.
PMID: 22971924
Phospholamban (PLN) is the endogenous inhibitor of the sarco(endo)plasmic reticulum Ca(2+)-ATPase (SERCA), the integral membrane enzyme responsible for 70 % of the removal of Ca(2+) from the cytosol, inducing cardiac...
6.
Ha K, Masterson L, Hou Z, Verardi R, Walsh N, Veglia G, et al.
Proc Natl Acad Sci U S A
. 2011 Feb;
108(7):2735-40.
PMID: 21282613
The regulatory interaction of phospholamban (PLN) with Ca(2+)-ATPase controls the uptake of calcium into the sarcoplasmic reticulum, modulating heart muscle contractility. A missense mutation in PLN cytoplasmic domain (R9C) triggers...
7.
Veglia G, Ha K, Shi L, Verardi R, Traaseth N
Methods Mol Biol
. 2010 Jul;
654:303-19.
PMID: 20665273
This chapter reviews the molecular biology, biochemical, and NMR methods that we used to study the structural dynamics, membrane topology, and interaction of phospholamban (PLN), a small regulatory membrane protein...
8.
Masterson L, Bortone N, Yu T, Ha K, Gaffarogullari E, Nguyen O, et al.
Protein Expr Purif
. 2008 Nov;
64(2):231-6.
PMID: 19027069
Extensive X-ray crystallographic studies carried out on the catalytic-subunit of protein kinase A (PKA-C) enabled the atomic characterization of inhibitor and/or substrate peptide analogues trapped at its active site. Yet,...
9.
Traaseth N, Ha K, Verardi R, Shi L, Buffy J, Masterson L, et al.
Biochemistry
. 2007 Dec;
47(1):3-13.
PMID: 18081313
Phospholamban (PLN) and sarcolipin (SLN) are two single-pass membrane proteins that regulate Ca2+-ATPase (SERCA), an ATP-driven pump that translocates calcium ions into the lumen of the sarcoplasmic reticulum, initiating muscle...
10.
Ha K, Traaseth N, Verardi R, Zamoon J, Cembran A, Karim C, et al.
J Biol Chem
. 2007 Oct;
282(51):37205-14.
PMID: 17908690
Cardiac contraction and relaxation are regulated by conformational transitions of protein complexes that are responsible for calcium trafficking through cell membranes. Central to the muscle relaxation phase is a dynamic...