Alexander S Maltsev
Overview
Explore the profile of Alexander S Maltsev including associated specialties, affiliations and a list of published articles.
Author names and details appear as published. Due to indexing inconsistencies, multiple individuals may share a name, and a single author may have variations. MedLuna displays this data as publicly available, without modification or verification
Snapshot
Snapshot
Articles
14
Citations
550
Followers
0
Related Specialties
Related Specialties
Top 10 Co-Authors
Top 10 Co-Authors
Published In
Published In
Affiliations
Affiliations
Soon will be listed here.
Recent Articles
1.
Ptak C, Hsieh C, Lin Y, Maltsev A, Raman R, Sharma Y, et al.
Biochemistry
. 2014 Jul;
53(32):5249-60.
PMID: 25068811
A number of surface proteins specific to pathogenic strains of Leptospira have been identified. The Lig protein family has shown promise as a marker in typing leptospiral isolates for pathogenesis...
2.
Mantsyzov A, Maltsev A, Ying J, Shen Y, Hummer G, Bax A
Protein Sci
. 2014 Jul;
23(9):1275-90.
PMID: 24976112
α-Synuclein is an intrinsically disordered protein of 140 residues that switches to an α-helical conformation upon binding phospholipid membranes. We characterize its residue-specific backbone structure in free solution with a...
3.
Maltsev A, Grishaev A, Roche J, Zasloff M, Bax A
J Am Chem Soc
. 2014 Feb;
136(10):3752-5.
PMID: 24568736
The antibiotic squalamine forms a lyotropic liquid crystal at very low concentrations in water (0.3-3.5% w/v), which remains stable over a wide range of temperature (1-40 °C) and pH (4-8)....
4.
Roche J, Ying J, Maltsev A, Bax A
Chembiochem
. 2013 Jul;
14(14):1754-61.
PMID: 23813793
The impact of pressure on the backbone (15) N, (1) H and (13) C chemical shifts in N-terminally acetylated α-synuclein has been evaluated over a pressure range 1-2500 bar. Even...
5.
Gruschus J, Yap T, Pistolesi S, Maltsev A, Lee J
Biochemistry
. 2013 Apr;
52(20):3436-45.
PMID: 23607618
Calmodulin (CaM) is a calcium binding protein that plays numerous roles in Ca-dependent cellular processes, including uptake and release of neurotransmitters in neurons. α-Synuclein (α-syn), one of the most abundant...
6.
Lorieau J, Maltsev A, Louis J, Bax A
J Biomol NMR
. 2013 Mar;
55(4):369-77.
PMID: 23508769
We demonstrate that alignment of a structured peptide or small protein solubilized in mixed phospholipid:detergent micelles or bicelles, when embedded in a compressed gel or liquid crystalline medium, can be...
7.
Maltsev A, Chen J, Levine R, Bax A
J Am Chem Soc
. 2013 Feb;
135(8):2943-6.
PMID: 23398174
α-Synuclein (αS) is an intrinsically disordered protein that is water-soluble but also can bind negatively charged lipid membranes while adopting an α-helical conformation. Membrane affinity is increased by post-translational N-terminal...
8.
Maltsev A, Ying J, Bax A
J Biomol NMR
. 2012 Sep;
54(2):181-91.
PMID: 22960996
Intrinsically disordered proteins (IDPs) are abundant in nature and characterization of their potential structural propensities remains a widely pursued but challenging task. Analysis of NMR secondary chemical shifts plays an...
9.
Maltsev A, Ying J, Bax A
Biochemistry
. 2012 Jun;
51(25):5004-13.
PMID: 22694188
N-Terminal acetylation of α-synuclein (aS), a protein implicated in the etiology of Parkinson's disease, is common in mammals. The impact of this modification on the protein's structure and dynamics in...
10.
Depth of α-synuclein in a bilayer determined by fluorescence, neutron reflectometry, and computation
Pfefferkorn C, Heinrich F, Sodt A, Maltsev A, Pastor R, Lee J
Biophys J
. 2012 Feb;
102(3):613-21.
PMID: 22325285
α-Synuclein (α-syn) membrane interactions are implicated in the pathogenesis of Parkinson's disease. Fluorescence and neutron reflectometry (NR) measurements reveal that α-syn penetrates ∼9-14 Å into the outer leaflet of the...