H. Ding

发表

Complementary roles of SufA and IscA in the biogenesis of iron-sulfur clusters in Escherichia coli.

Juanjuan Yang, Jianxin Lu, Guoqiang Tan, 2008, The Biochemical journal.

Nucleotide Binding Activity of SecA Homodimer Is Conformationally Regulated by Temperature and Altered byprlD and azi Mutations*

V. Ramamurthy, H. Ding, I. Mukerji, 2000, The Journal of Biological Chemistry.

Characterization of iron binding in IscA, an ancient iron-sulphur cluster assembly protein.

R. Clark, H. Ding, 2004, The Biochemical journal.

Ubiquinone pair in the Qo site central to the primary energy conversion reactions of cytochrome bc1 complex.

P. Dutton, F. Daldal, D. Robertson, 1995, Biochemistry.

Escherichia coli FtnA acts as an iron buffer for re-assembly of iron–sulfur clusters in response to hydrogen peroxide stress

Gen-fu Wu, H. Ding, J. Bitoun, 2008, BioMetals.

Nitric oxide‐induced bacteriostasis and modification of iron‐sulphur proteins in Escherichia coli

Juanjuan Yang, H. Ding, B. Ren, 2008, Molecular microbiology.

Cytochrome bc1 complex [2Fe-2S] cluster and its interaction with ubiquinone and ubihydroquinone at the Qo site: a double-occupancy Qo site model.

P. Dutton, F. Daldal, D. Robertson, 1992, Biochemistry.

Identification of the N-terminal Peptide Binding Site of Glucose-regulated Protein 94*

H. Wolfson, S. Radford, D. Schneidman-Duhovny, 2004, Journal of Biological Chemistry.

In vivo evidence for the iron-binding activity of an iron-sulfur cluster assembly protein IscA in Escherichia coli.

Min Liu, Hao Huang, Jianxin Lu, 2010, The Biochemical journal.

IscA/SufA paralogues are required for the [4Fe-4S] cluster assembly in enzymes of multiple physiological pathways in Escherichia coli under aerobic growth conditions.

Hao Huang, Jianxin Lu, Guoqiang Tan, 2009, The Biochemical journal.

Redox signal transduction via iron-sulfur clusters in the SoxR transcription activator.

B. Demple, H. Ding, E. Hidalgo, 1997, Trends in biochemical sciences.

In vivo kinetics of a redox-regulated transcriptional switch

B. Demple, H. Ding, 1997 .

Harnessing toxic reactions to signal stress: reactions of nitric oxide with iron–sulfur centers and the informative case of SoxR protein

B. Demple, H. Ding, T. Reiter, 2007 .

Exploring the FMN binding site in the mitochondrial outer membrane protein mitoNEET.

H. Ding, Homyra Tasnim, A. P. Landry, 2020, Free radical biology & medicine.

Redox Control of Human Mitochondrial Outer Membrane Protein MitoNEET [2Fe-2S] Clusters by Biological Thiols and Hydrogen Peroxide*

H. Ding, A. P. Landry, 2014, The Journal of Biological Chemistry.

Nitric oxide reversibly binds the reduced [2Fe-2S] cluster in mitochondrial outer membrane protein mitoNEET and inhibits its electron transfer activity

H. Ding, Zishuo Cheng, Chelsey R. Fontenot, 2022, Frontiers in Molecular Biosciences.

Ferric uptake regulator (Fur) reversibly binds a [2Fe-2S] cluster to sense intracellular iron homeostasis in Escherichia coli

H. Ding, Homyra Tasnim, C. Popescu, 2020, The Journal of Biological Chemistry.

In vivo kinetics of a redox-regulated transcriptional switch.

B. Demple, H. Ding, 1997, Proceedings of the National Academy of Sciences of the United States of America.

Stimulation of Escherichia coli DNA damage inducible DNA helicase DinG by the single‐stranded DNA binding protein SSB

H. Ding, Zishuo Cheng, B. Ren, 2012, FEBS letters.

Iron-sulfur proteins are the major source of protein-bound dinitrosyl iron complexes formed in Escherichia coli cells under nitric oxide stress.

Hao Huang, H. Ding, A. P. Landry, 2011, Free radical biology & medicine.

Repair of Nitric Oxide-modified Ferredoxin [2Fe-2S] Cluster by Cysteine Desulfurase (IscS)*

Wenyu Yang, H. Ding, P. Rogers, 2002, The Journal of Biological Chemistry.

Electron transfer activity of the nanodisc-bound mitochondrial outer membrane protein mitoNEET.

H. Ding, Homyra Tasnim, 2022, Free radical biology & medicine.

Copper binding in IscA inhibits iron‐sulphur cluster assembly in Escherichia coli

Jianxin Lu, Guoqiang Tan, H. Ding, 2014, Molecular microbiology.

Reversible inactivation of E. coli endonuclease III via modification of its [4Fe-4S] cluster by nitric oxide.

A. Klungland, L. Eide, H. Ding, 2003, DNA repair.

Escherichia coli SoxR protein: sensor/transducer of oxidative stress and nitric oxide.

B. Demple, H. Ding, M. Jorgensen, 2002, Methods in enzymology.

Ferric uptake regulators (Fur) from Vibriocholerae and Helicobacterpylori bind a [2Fe–2S] cluster in response to elevation of intracellular free iron content

H. Ding, Chelsey R. Fontenot, 2022, BioMetals.

Deletion of the Proposed Iron Chaperones IscA/SufA Results in Accumulation of a Red Intermediate Cysteine Desulfurase IscS in Escherichia coli*

Robert H. White, Jianxin Lu, Guoqiang Tan, 2015, The Journal of Biological Chemistry.

Iron binding activity is essential for the function of IscA in iron-sulphur cluster biogenesis.

H. Ding, Zishuo Cheng, A. P. Landry, 2013, Dalton transactions.

Iron Homeostasis and Iron–Sulfur Cluster Assembly in Escherichia Coli

H. Ding, 2016 .

Thioredoxin Reductase System Mediates Iron Binding in IscA and Iron Delivery for the Iron-Sulfur Cluster Assembly in IscU*

Jianxin Lu, H. Ding, K. Harrison, 2005, Journal of Biological Chemistry.

Zinc Toxicity and Iron-Sulfur Cluster Biogenesis in Escherichia coli

Zhaoyang Huang, J. Lyu, Guoqiang Tan, 2019, Applied and Environmental Microbiology.

Anaerobic Copper Toxicity and Iron-Sulfur Cluster Biogenesis in Escherichia coli

J. Lyu, Guoqiang Tan, H. Ding, 2017, Applied and Environmental Microbiology.

Crystal structure of the ancient, Fe-S scaffold IscA reveals a novel protein fold.

M. Newcomer, P. Bilder, H. Ding, 2004, Biochemistry.

Reactivity of nitric oxide with the [4Fe-4S] cluster of dihydroxyacid dehydratase from Escherichia coli.

Juanjuan Yang, Guoqiang Tan, H. Ding, 2009, The Biochemical journal.

The Redox State of the [2Fe-2S] Clusters in SoxR Protein Regulates Its Activity as a Transcription Factor*

B. Demple, H. Ding, E. Hidalgo, 1996, The Journal of Biological Chemistry.

Redox Signal Transduction: Mutations Shifting [2Fe-2S] Centers of the SoxR Sensor-Regulator to the Oxidized Form

B. Demple, H. Ding, E. Hidalgo, 1997, Cell.

Redox Control of the DNA Damage-inducible Protein DinG Helicase Activity via Its Iron-Sulfur Cluster*

H. Ding, B. Ren, Xuewu Duan, 2009, Journal of Biological Chemistry.

The N-Terminal Domain of Human DNA Helicase Rtel1 Contains a Redox Active Iron-Sulfur Cluster

H. Ding, A. P. Landry, 2014, BioMed research international.

IscA Mediates Iron Delivery for Assembly of Iron-Sulfur Clusters in IscU under the Limited Accessible Free Iron Conditions*

R. Clark, H. Ding, Baojin Ding, 2004, Journal of Biological Chemistry.

Binding of Nitric Oxide in CDGSH-type [2Fe-2S] Clusters of the Human Mitochondrial Protein Miner2*

H. Ding, Zishuo Cheng, A. P. Landry, 2017, The Journal of Biological Chemistry.

Iron and zinc binding activity of Escherichia coli topoisomerase I homolog YrdD

Jianxin Lu, Guoqiang Tan, H. Ding, 2014, BioMetals.

Ion pair formation between basic residues at 144 of the Cyt b polypeptide and the ubiquinones at the Qo site of the Cyt bc1 complex.

P. Dutton, F. Daldal, H. Ding, 1995, Biochemistry.

Direct nitric oxide signal transduction via nitrosylation of iron-sulfur centers in the SoxR transcription activator.

B. Demple, H. Ding, 2000, Proceedings of the National Academy of Sciences of the United States of America.

The mitochondrial outer membrane protein mitoNEET is a redox enzyme catalyzing electron transfer from FMNH2 to oxygen or ubiquinone

H. Ding, A. P. Landry, Yiming Wang, 2017, The Journal of Biological Chemistry.

Flavin nucleotides act as electron shuttles mediating reduction of the [2Fe‐2S] clusters in mitochondrial outer membrane protein mitoNEET

Yong-Hwan Lee, H. Ding, Zishuo Cheng, 2017, Free radical biology & medicine.

Reduction of mitochondrial protein mitoNEET [2Fe-2S] clusters by human glutathione reductase.

H. Ding, Zishuo Cheng, A. P. Landry, 2015, Free radical biology & medicine.

Iron-binding activity of human iron-sulfur cluster assembly protein hIscA1.

Jianxin Lu, Guoqiang Tan, H. Ding, 2010, The Biochemical journal.

Distinct Iron Binding Property of Two Putative Iron Donors for the Iron-Sulfur Cluster Assembly

Juanjuan Yang, H. Ding, S. Yeung, 2007, Journal of Biological Chemistry.

Interplay of IscA and IscU in Biogenesis of Iron-Sulfur Clusters*

Juanjuan Yang, H. Ding, J. Bitoun, 2006, Journal of Biological Chemistry.

Mobilization of the iron centre in IscA for the iron-sulphur cluster assembly in IscU.

Edward S. Smith, H. Ding, Baojin Ding, 2005, The Biochemical journal.

Escherichia coli topoisomerase I is an iron and zinc binding protein

Jianxin Lu, Guoqiang Tan, H. Ding, 2011, BioMetals.

Hydroubiquinone-cytochrome c2 oxidoreductase from Rhodobacter capsulatus: definition of a minimal, functional isolated preparation.

C. Slaughter, P. Dutton, F. Daldal, 1993, Biochemistry.

Cysteine-to-alanine replacements in the Escherichia coli SoxR protein and the role of the [2Fe-2S] centers in transcriptional activation.

T. M. Bradley, B. Demple, H. Ding, 1997, Nucleic acids research.

Electron transfer kinetics of the mitochondrial outer membrane protein mitoNEET

J. Lyu, Guoqiang Tan, H. Ding, 2018, Free radical biology & medicine.

Light-induced release of nitric oxide from the nitric oxide-bound CDGSH-type [2Fe-2S] clusters in mitochondrial protein Miner2.

Jeonghoon Lee, H. Ding, Yiming Wang, 2019, Nitric oxide : biology and chemistry.

Competition of zinc ion for the [2Fe–2S] cluster binding site in the diabetes drug target protein mitoNEET

Jianxin Lu, Guoqiang Tan, H. Ding, 2012, BioMetals.

Ferric uptake regulator (Fur) binds a [2Fe-2S] cluster to regulate intracellular iron homeostasis in Escherichia coli

H. Ding, Chelsey R. Fontenot, 2023, The Journal of biological chemistry.

Oxygen is required for the L-cysteine-mediated decomposition of protein-bound dinitrosyl-iron complexes.

Juanjuan Yang, H. Ding, A. P. Landry, 2010, Free radical biology & medicine.

Inhibition of hemoglobin S polymerization in vitro by a novel 15-mer EF-helix beta73 histidine-containing peptide.

S. Surrey, K. Reddy, M. Rosenblatt, 2006, Biochemistry.

Glutathione-mediated destabilization in vitro of [2Fe-2S] centers in the SoxR regulatory protein.

B. Demple, H. Ding, 1996, Proceedings of the National Academy of Sciences of the United States of America.

Thiol-mediated disassembly and reassembly of [2Fe-2S] clusters in the redox-regulated transcription factor SoxR.

B Demple, B. Demple, H. Ding, 1998, Biochemistry.

l-Cysteine-mediated Destabilization of Dinitrosyl Iron Complexes in Proteins*

H. Ding, P. Rogers, 2001, The Journal of Biological Chemistry.

Tyrosine 147 of cytochrome b is required for efficient electron transfer at the ubihydroquinone oxidase site (Qo) of the cytochrome bc1 complex.

P. Dutton, F. Daldal, A. Saribaş, 1995, Biochemistry.

Iron–sulfur cluster assembly scaffold protein IscU is required for activation of ferric uptake regulator (Fur) in Escherichiacoli

H. Ding, Chelsey R. Fontenot, Aidan G Purcell, 2024, The Journal of biological chemistry.

The C-terminal domain of the ferric uptake regulator (Fur) binds a [2Fe–2S] cluster to sense the intracellular free iron content in Escherichia coli

H. Ding, Chelsey R. Fontenot, 2023, Biometals.