scispace - formally typeset
M

Maxim N. Zhmak

Researcher at Russian Academy of Sciences

Publications -  58
Citations -  1179

Maxim N. Zhmak is an academic researcher from Russian Academy of Sciences. The author has contributed to research in topics: Nicotinic acetylcholine receptor & Nicotinic agonist. The author has an hindex of 16, co-authored 58 publications receiving 1058 citations.

Papers
More filters
Journal ArticleDOI

Crystal structure of nicotinic acetylcholine receptor homolog AChBP in complex with an alpha-conotoxin PnIA variant.

TL;DR: The structure at a resolution of 2.4 Å of α-Ctx PnIA (A10L D14K), a potent blocker of the α7-nAChR, bound with high affinity to acetylcholine binding protein (AChBP), the prototype for the ligand-binding domains of the nA ChR superfamily is presented.
Journal ArticleDOI

Differential involvement of α4β2, α7 and α9α10 nicotinic acetylcholine receptors in B lymphocyte activation in vitro.

TL;DR: It is concluded that α7 nA ChR fulfills inhibitory CD40-related mitogenic function, α4β2 nAChR produces a stimulatory IgM-related effect, while α9α10 nAchR is a "reserve" receptor, which partly compensates the absence of α7nAChr in α7(-/-) cells.
Journal ArticleDOI

Mitochondria express several nicotinic acetylcholine receptor subtypes to control various pathways of apoptosis induction.

TL;DR: It is concluded that cholinergic regulation in mitochondria is realized through multiple nicotinic receptor subtypes, which control various pathways inducing mitochondrial type of apoptosis.
Journal ArticleDOI

NMR spatial structure of α-conotoxin ImI reveals a common scaffold in snail and snake toxins recognizing neuronal nicotinic acetylcholine receptors1

TL;DR: When depicted with opposite directions of the polypeptide chains, the ImI helix and the tip of the central loop of long chain snake neurotoxins demonstrate a common scaffold and similar positioning of the functional side chains, both of these structural elements appearing essential for binding to the neuronal nAChRs.