Vinod Subramaniam
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Explore the profile of Vinod Subramaniam including associated specialties, affiliations and a list of published articles.
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147
Citations
3028
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Recent Articles
1.
Iyer A, Sidhu A, Subramaniam V
Front Neurosci
. 2022 Dec;
16:1003997.
PMID: 36466161
N-α-acetylation is a frequently occurring post-translational modification in eukaryotic proteins. It has manifold physiological consequences on the regulation and function of several proteins, with emerging studies suggesting that it is...
2.
Braun T, Stehle J, Kacprzak S, Carl P, Hofer P, Subramaniam V, et al.
J Phys Chem Lett
. 2021 Mar;
12(9):2471-2475.
PMID: 33663214
Protein-membrane interactions play key roles in essential cellular processes; studying these interactions in the cell is a challenging task of modern biophysical chemistry. A prominent example is the interaction of...
3.
Prangsma J, Molenaar R, van Weeren L, Bindels D, Haarbosch L, Stouthamer J, et al.
J Phys Chem B
. 2020 Feb;
124(8):1383-1391.
PMID: 32011884
The fluorescence quantum yield of four representative red fluorescent proteins mCherry, mKate2, mRuby2, and the recently introduced mScarlet was investigated. The excited state lifetimes were measured as a function of...
4.
Abbandonato G, Storti B, Tonazzini I, Stockl M, Subramaniam V, Montis C, et al.
Biophys J
. 2019 Feb;
116(3):477-486.
PMID: 30709620
The plasma membrane of cells has a complex architecture based on the bidimensional liquid-crystalline bilayer arrangement of phospho- and sphingolipids, which in turn embeds several proteins and is connected to...
5.
Sidhu A, Vaneyck J, Blum C, Segers-Nolten I, Subramaniam V
Amyloid
. 2018 Nov;
25(3):189-196.
PMID: 30486688
Thioflavin-T (ThT) is the most commonly used fluorescent dye for following amyloid formation semi-quantitatively in vitro, specifically probing the fibrillar cross-β-sheet content. In recent years, structural polymorphism of amyloid fibrils...
6.
Semerdzhiev S, Lindhoud S, Stefanovic A, Subramaniam V, van der Schoot P, Claessens M
Phys Rev Lett
. 2018 Jun;
120(20):208102.
PMID: 29864360
In water, networks of semiflexible fibrils of the protein α-synuclein stiffen significantly with increasing temperature. We make plausible that this reversible stiffening is a result of hydrophobic contacts between the...
7.
Iyer A, Roeters S, Kogan V, Woutersen S, Claessens M, Subramaniam V
J Am Chem Soc
. 2017 Oct;
139(43):15392-15400.
PMID: 28968082
C-terminal truncations of monomeric wild-type alpha-synuclein (henceforth WT-αS) have been shown to enhance the formation of amyloid aggregates both in vivo and in vitro and have been associated with accelerated...
8.
Kumar P, Schilderink N, Subramaniam V, Huber M
Isr J Chem
. 2017 Sep;
57(7-8):762-770.
PMID: 28919642
Human α-synuclein, a protein relevant in the brain with so-far unknown function, plays an important role in Parkinson's disease. The phosphorylation state of αS was related to the disease, prompting...
9.
Wasserberg D, Cabanas-Danes J, Prangsma J, OMahony S, Cazade P, Tromp E, et al.
ACS Nano
. 2017 Aug;
11(9):9068-9083.
PMID: 28850777
We report oriented immobilization of proteins using the standard hexahistidine (His)-Ni:NTA (nitrilotriacetic acid) methodology, which we systematically tuned to give control of surface coverage. Fluorescence microscopy and surface plasmon resonance...
10.
Non-uniform self-assembly: On the anisotropic architecture of α-synuclein supra-fibrillar aggregates
Semerdzhiev S, Shvadchak V, Subramaniam V, Claessens M
Sci Rep
. 2017 Aug;
7(1):7699.
PMID: 28794461
Although the function of biopolymer hydrogels in nature depends on structural anisotropy at mesoscopic length scales, the self-assembly of such anisotropic structures in vitro is challenging. Here we show that...