Human annexins A1, A2, and A8 as potential molecular targets for Ni (II) ions
NE Wezynfeld, K Bossak, W Goch… - Chemical Research …, 2014 - ACS Publications
Nickel is harmful for humans, but molecular mechanisms of its toxicity are far from being fully
elucidated. One of such mechanisms may be associated with the Ni (II)-dependent peptide …
elucidated. One of such mechanisms may be associated with the Ni (II)-dependent peptide …
Inactivation of annexin II tetramer by S‐nitrosoglutathione
L Liu, E Enright, P Sun, SY Tsai, P Mehta… - European journal of …, 2002 - Wiley Online Library
We investigated the effect of nitric oxide (NO) donors on the activities of annexin II tetramer
(AIIt), a member of the Ca2+‐dependent phospholipid‐binding protein family. Incubation of …
(AIIt), a member of the Ca2+‐dependent phospholipid‐binding protein family. Incubation of …
Annexins: calcium binding proteins with unusual binding sites
A Rosengarth, H Luecke - Encyclopedia of Inorganic and …, 2011 - Wiley Online Library
Annexins comprise a multigene family of calcium‐and phospholipid‐binding proteins. They
are structurally divided into a conserved core domain and a flexible N‐terminal domain. The …
are structurally divided into a conserved core domain and a flexible N‐terminal domain. The …
[HTML][HTML] Annexin A2 heterotetramer: structure and function
A Bharadwaj, M Bydoun, R Holloway… - International journal of …, 2013 - mdpi.com
Annexin A2 is a pleiotropic calcium-and anionic phospholipid-binding protein that exists as
a monomer and as a heterotetrameric complex with the plasminogen receptor protein …
a monomer and as a heterotetrameric complex with the plasminogen receptor protein …
Peptide bond cleavage by Ni (II) ions within the nuclear localization signal sequence
Nickel is harmful to humans, being both carcinogenic and allergenic. However, the
mechanisms of this toxicity are still unresolved. We propose that Ni (II) ions disintegrate …
mechanisms of this toxicity are still unresolved. We propose that Ni (II) ions disintegrate …
N-and C-terminal halves of human annexin VI differ in ability to form low pH-induced ion channels
M Golczak, A Kirilenko, J Bandorowicz-Pikula… - Biochemical and …, 2001 - Elsevier
Human recombinant annexin VI (AnxVI) or its N-(AnxVIA) and C-terminal (AnxVIB) fragments
were expressed in E. coli. Their ability to form voltage-dependent ion channels in …
were expressed in E. coli. Their ability to form voltage-dependent ion channels in …
A comparison of the energetics of annexin I and annexin V
A Rosengarth, J Rösgen, HJ Hinz, V Gerke - Journal of molecular biology, 1999 - Elsevier
The annexins comprise a family of soluble Ca2+-and phospholipid-binding proteins.
Although highly similar in three-dimensional structure, different annexins are likely to exhibit …
Although highly similar in three-dimensional structure, different annexins are likely to exhibit …
[HTML][HTML] Regulation of annexin A2 by reversible glutathionylation
JF Caplan, NR Filipenko, SL Fitzpatrick… - Journal of Biological …, 2004 - ASBMB
The annexin A2-S100A10 heterotetramer (AIIt) is a multifunctional Ca 2+-dependent,
phospholipid-binding, and F-actin-binding phosphoprotein composed of two annexin A2 …
phospholipid-binding, and F-actin-binding phosphoprotein composed of two annexin A2 …
The penta-EF-hand domain of ALG-2 interacts with amino-terminal domains of both annexin VII and annexin XI in a Ca2+-dependent manner
The apoptosis-linked protein ALG-2 is a Ca2+-binding protein that belongs to the penta-EF-
hand (PEF) protein family. ALG-2 forms a homodimer, a heterodimer with another PEF …
hand (PEF) protein family. ALG-2 forms a homodimer, a heterodimer with another PEF …
Structural elucidation of the protein-and membrane-binding properties of the N-terminal tail domain of human annexin II
YH Hong, HS Won, HC Ahn, BJ Lee - Journal of biochemistry, 2003 - academic.oup.com
The conformational preferences and the solution structure of AnxIIN31, a peptide
corresponding to the full-length sequence (residues 1–31) of the human annexin II N …
corresponding to the full-length sequence (residues 1–31) of the human annexin II N …