Nature Search

The substrate-binding site in Cu nitrite reductase and its similarity to Zn carbonic anhydrase

Richard W. Strange
Fraser E. Dodd
S. Samar Hasnain
Research01 Apr 1995
Nature Structural Biology

Volume: 2, P: 287-292
Stereochemistry of iron in deoxyhaemoglobin

M. F. Perutz
S. Samar Hasnain
J. E. Hahn
Research11 Feb 1982
Nature

Volume: 295, P: 535-538
Vanadium K-edge X-ray absorption spectrum of the VFe protein of the vanadium nitrogenase of Azotobacter chroococcum

Judith M. Arber
Barry R. Dobson
Barry E. Smith
Research22 Jan 1987
Nature

Volume: 325, P: 372-374
Ligand binding and aggregation of pathogenic SOD1

Mutations of the SOD1gene are implicated in neurodegenerative diseases such as amyotrophic lateral sclerosis. Wright and colleagues find that SOD1 aggregation in cells is arrested by compounds that bind at the core of SOD1 aggregates, rather than at the dimer interface site.

Gareth S.A. Wright
Svetlana V. Antonyuk
S Samar Hasnain
ResearchOpen Access23 Apr 2013
Nature Communications

Volume: 4, P: 1-10
Global, regional and national burden of dietary iron deficiency from 1990 to 2021: a Global Burden of Disease study

Systematic analysis from the Global Burden of Disease study reported that, despite global improvements from 1990 to 2021, dietary iron deficiency-associated disease burden remains high in women, children and residents in low socio-demographic index countries.

Sooji Lee
Yejun Son
Nicholas. J. Kassebaum
Research22 Apr 2025
Nature Medicine

Volume: 31, P: 1809-1829
The cysteine-reactive small molecule ebselen facilitates effective SOD1 maturation

Mutations in superoxide dismutase-1 (SOD1) cause amyotrophic lateral sclerosis (ALS). Here the authors present the SOD1 crystal structure bound to the small cysteine-reactive molecule ebselen and show that ebselen is a chaperone for SOD1.

Michael J. Capper
Gareth S. A. Wright
S. Samar Hasnain
ResearchOpen Access27 Apr 2018
Nature Communications

Volume: 9, P: 1-9
A 2.2 Å cryoEM structure of a quinol-dependent NO Reductase shows close similarity to respiratory oxidases

Quinol-dependent nitric oxide reductases, unique to bacteria, are considered members of respiratory heme copper oxidases. A 2.2 Å cryoEM structure of qNOR is reported shedding light on key aspects of enzyme mechanism including quinol binding and pathways for electron, substrate, and proton transport.

Alex J. Flynn
Svetlana V. Antonyuk
S. Samar Hasnain
ResearchOpen Access09 Jun 2023
Nature Communications

Volume: 14, P: 1-12
Inhibition mechanism of SARS-CoV-2 main protease by ebselen and its derivatives

Ebselen is an organoselenium drug that inhibits the SARS-CoV-2 main protease (M^pro). Here, the authors co-crystallised M^pro with ebselen and an ebselen derivative and observed an enzyme bound organoselenium covalent adduct in the crystal structures, which was also confirmed by mass spectrometry analysis.

Kangsa Amporndanai
Xiaoli Meng
S. Samar Hasnain
ResearchOpen Access24 May 2021
Nature Communications

Volume: 12, P: 1-7
Impact of residues remote from the catalytic centre on enzyme catalysis of copper nitrite reductase

Residues within the catalytic site of enzymes are important for activity, but whether more distant residues are also sensitive to mutation is unclear. Here, Leferink et al.show that mutation of residues in copper nitrate reductase that are 12Å away from the active site perturb enzyme function.

Nicole G. H. Leferink
Svetlana V. Antonyuk
S. Samar Hasnain
ResearchOpen Access15 Jul 2014
Nature Communications

Volume: 5, P: 1-8
Structures of protein–protein complexes involved in electron transfer

Structures of a newly characterized three-domain haem-c-Cu nitrite reductase are reported at 1.01 Å resolution, indicating how electron transfer may occur in protein–protein complexes.

Svetlana V. Antonyuk
Cong Han
S. Samar Hasnain
Research27 Mar 2013
Nature

Volume: 496, P: 123-126
Macromolecular structures probed by combining single-shot free-electron laser diffraction with synchrotron coherent X-ray imaging

Macromolecular complexes hold promise for future generations of drug delivery carriers, but probing their structures with high resolution is challenging. Here, the authors combine X-ray free-electron laser and synchrotron approaches to reveal the core-shell structure of RNA interference microsponges.

Marcus Gallagher-Jones
Yoshitaka Bessho
Changyong Song
Research02 May 2014
Nature Communications

Volume: 5, P: 1-9
Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS

Jennifer Stine Elam
Alexander B Taylor
P John Hart
Research19 May 2003
Nature Structural & Molecular Biology

Volume: 10, P: 461-467
A faulty interaction between SOD1 and hCCS in neurodegenerative disease

Gareth S. A. Wright
Svetlana V. Antonyuk
S. Samar Hasnain
ResearchOpen Access10 Jun 2016
Scientific Reports

Volume: 6, P: 1-9
Ebselen analogues delay disease onset and its course in fALS by on-target SOD-1 engagement

Seiji Watanabe
Kangsa Amporndanai
S. Samar Hasnain
ResearchOpen Access27 May 2024
Scientific Reports

Volume: 14, P: 1-18
Ebselen as template for stabilization of A4V mutant dimer for motor neuron disease therapy

Chantadul et al. uses x-ray crystallography and differential scanning fluorescence-based assay to show that ebselen and its analogues increase thermostability of both WT and A4V mutant SOD1 when second free cysteine is removed using a point mutation. Hence, ebselen can be used as a template for structure based drug development of ALS therapeutics.

Varunya Chantadul
Gareth S. A. Wright
S. Samar Hasnain
ResearchOpen Access05 Mar 2020
Communications Biology

Volume: 3, P: 1-10
Modulation of LAT1 (SLC7A5) transporter activity and stability by membrane cholesterol

David Dickens
George N. Chiduza
S. Samar Hasnain
ResearchOpen Access08 Mar 2017
Scientific Reports

Volume: 7, P: 1-13
Characterization of the quinol-dependent nitric oxide reductase from the pathogen Neisseria meningitidis, an electrogenic enzyme

Nathalie Gonska
David Young
Pia Ädelroth
ResearchOpen Access26 Feb 2018
Scientific Reports

Volume: 8, P: 1-13
New paradigms for understanding and step changes in treating active and chronic, persistent apicomplexan infections

Martin McPhillie
Ying Zhou
Rima McLeod
ResearchOpen Access14 Jul 2016
Scientific Reports

Volume: 6, P: 1-23
Author Correction: New paradigms for understanding and step changes in treating active and chronic, persistent apicomplexan infections

Martin McPhillie
Ying Zhou
Rima McLeod
Amendments and CorrectionsOpen Access23 Mar 2020
Scientific Reports

Volume: 10, P: 1-2

Search

The substrate-binding site in Cu nitrite reductase and its similarity to Zn carbonic anhydrase

Stereochemistry of iron in deoxyhaemoglobin

Vanadium K-edge X-ray absorption spectrum of the VFe protein of the vanadium nitrogenase of Azotobacter chroococcum

Ligand binding and aggregation of pathogenic SOD1

Global, regional and national burden of dietary iron deficiency from 1990 to 2021: a Global Burden of Disease study

The cysteine-reactive small molecule ebselen facilitates effective SOD1 maturation

A 2.2 Å cryoEM structure of a quinol-dependent NO Reductase shows close similarity to respiratory oxidases

Inhibition mechanism of SARS-CoV-2 main protease by ebselen and its derivatives

Impact of residues remote from the catalytic centre on enzyme catalysis of copper nitrite reductase

Structures of protein–protein complexes involved in electron transfer

Macromolecular structures probed by combining single-shot free-electron laser diffraction with synchrotron coherent X-ray imaging

Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS

A faulty interaction between SOD1 and hCCS in neurodegenerative disease

Ebselen analogues delay disease onset and its course in fALS by on-target SOD-1 engagement

Ebselen as template for stabilization of A4V mutant dimer for motor neuron disease therapy

Modulation of LAT1 (SLC7A5) transporter activity and stability by membrane cholesterol

Characterization of the quinol-dependent nitric oxide reductase from the pathogen Neisseria meningitidis, an electrogenic enzyme

New paradigms for understanding and step changes in treating active and chronic, persistent apicomplexan infections

Author Correction: New paradigms for understanding and step changes in treating active and chronic, persistent apicomplexan infections

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