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 …

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 …

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 …

[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 …

Peptide bond cleavage by Ni (II) ions within the nuclear localization signal sequence

T Frączyk, A Bonna, E Stefaniak… - Chemistry & …, 2020 - Wiley Online Library
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 …

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 …

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 …

[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 …

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

H Satoh, Y Nakano, H Shibata, M Maki - Biochimica et Biophysica Acta …, 2002 - Elsevier
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 …

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 …