The N-Terminal Peptides of the Three Human Isoforms of the Mitochondrial Voltage-Dependent Anion Channel Have Different Helical Propensities.
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N-helix and Cysteines Inter-regulate Human Mitochondrial VDAC-2 Function and Biochemistry.VDAC3 As a Potential Marker of Mitochondrial Status Is Involved in Cancer and Pathology.VDAC-2: Mitochondrial outer membrane regulator masquerading as a channel?Protein-protein interaction networks as a new perspective to evaluate distinct functional roles of voltage-dependent anion channel isoforms.Mitochondrial VDAC2 and cell homeostasis: highlighting hidden structural features and unique functionalities.Folded Structure and Membrane Affinity of the N-Terminal Domain of the Three Human Isoforms of the Mitochondrial Voltage-Dependent Anion-Selective Channel
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The N-Terminal Peptides of the Three Human Isoforms of the Mitochondrial Voltage-Dependent Anion Channel Have Different Helical Propensities.
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2015 թվականի օգոստոսին հրատարակված գիտական հոդված
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2015年論文
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2015年論文
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2015年論文
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2015年论文
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name
The N-Terminal Peptides of the ...... ifferent Helical Propensities.
@ast
The N-Terminal Peptides of the ...... ifferent Helical Propensities.
@en
type
label
The N-Terminal Peptides of the ...... ifferent Helical Propensities.
@ast
The N-Terminal Peptides of the ...... ifferent Helical Propensities.
@en
prefLabel
The N-Terminal Peptides of the ...... ifferent Helical Propensities.
@ast
The N-Terminal Peptides of the ...... ifferent Helical Propensities.
@en
P2093
P50
P1433
P1476
The N-Terminal Peptides of the ...... ifferent Helical Propensities.
@en
P2093
Carlo Guardiani
Giuseppe Federico Amodeo
Joze Grdadolnik
Mariano Casu
Matteo Ceccarelli
P304
P356
10.1021/ACS.BIOCHEM.5B00469
P407
P577
2015-08-24T00:00:00Z