Dr. Mateen A. Khan obtained his PhD degree in the field of Biotechnology from the Aligarh Muslim University, India, and later completed a postdoctoral fellowship in the Department of Biochemistry and Chemistry, Hunter College of the City University of New York, and School of Medicine, Stanford University, California, USA. Dr. Khan has published over 30 peer review journal articles, book and book chapter, and has been invited/attended over 30 national and international conferences. Dr. Khan is an active and productive member of the scientific community, serving as a reviewer for multiple scholarly journals including Biochimica et Biophysica Acta-BBA, PLOS ONE, Journal of plant Pathology, Current Chemical Biology, Journal of Biochemistry and Modern Application, and the International Journal of Biochemistry, Biophysics & Molecular Biology. He is the recipient of Faculty Award for Research Excellent 2022, Teaching Award 2022, and Outstanding Research Award 2019 by the Alfaisal University. He has been identified as one of the best young scientists at the City University of New York by Gene Centre foundation and his name has been published by News Review. Dr. Khan's research achievements have been identified by the faculty of 1000 biology scientist. He has supervised or mentored over 20 undergraduate and graduate students and has served on over 20 committees.

Dr. Khan research interests are directed toward understanding the mechanism of gene regulation of iron metabolism and how it impacts on disease process. Alzheimer disease is a neurodegenerative process that is the leading cause of death worldwide for people over the age of 65. Overexpression of Alzheimer amyloid precursor protein (APP) has been linked to Alzheimer’s disease (AD). The fact that stem-loop structure of APP IRE mRNA has been linked to high level of iron and iron regulatory protein (IRP1) makes this an important model system for iron disorders research and is a potential therapeutic target. Protein aggregation and misfolding is directly associated with the neurodegenerative diseases. IRE-mRNA signaling pathway has been implicated in the modulation of amyloid, which is important to neurodegeneration in Alzheimer’s disease. Therefore, the identification of small molecular APP mRNA chemical inhibitors to reduce amyloid protein aggregation can have therapeutic significance to Alzheimer’s disease. IRE RNA inhibitors can decrease ferritin and transferrin receptor expression to alleviate the excess iron accumulation in AD brains cells. Furthermore, therapeutic IRE RNA inhibitors that down regulate APP protein translation and inhibit protein aggregation can promote neuronal survival. IRPs are key controllers of iron homeostasis and post-transcriptionally regulate expression of the major iron regulated genes. Despite considerable research efforts including identification of APP IRE mRNAs binding domain, binding proteins, and the specific mechanism through which IREs recruitment the IRP, initiation factors and ribosome, quantitative binding and structural studies are still unknown. The lack of these data is an important problem because the binding stability and highly ordered structure of APP/IRE complex plays a crucial role to find the start codon AUG for translation initiation. Therefore, it will be significant to determine the extent to which the IRP form complex with APP IRE, and the stability of the complex will be an important control point for the overall rate of protein synthesis. Lack of this knowledge makes it impossible to discriminate among proposed cellular regulatory mechanism between repressor IRP protein binding to IRE RNA in the gene regulation. Our major focus over the past several years has been involved the underlying mechanism based translational research of the iron mis-regulation and Alzheimer’s disease by dissecting the signaling pathway which plays critical role in aggregation, misfolding of amyloid protein in brain as observed in neurodegenerative diseases like Alzheimer’s and Parkinson’s. These studies will provide the understanding of the mechanism of amyloid aggregation and provide new targets for therapeutic intervention in Alzheimer’s disease.

PUBLICATIONS

1. Khan MA, Mohammad T, Malik A, Hassan MI, and Domashevskiy AV (2023) Iron response elements (IREs)-mRNA of Alzheimer’s amyloid precursor protein binding to iron regulatory protein (IRP1):  a combined molecular docking and spectroscopic approach. Scientific Reports, 13: 5073.  doi: 10.1038/s41598-023-32073-x.
2. Khan MA, Malik A, and Domashevskiy AV (2023) Translational control of the Alzheimer’s amyloid precursor protein mRNA by iron regulatory protein (IRP1). International Journal of Molecular Sciences (Submitted).
3. Khan MA, Yamak S. and Miyoshi H (2023) Poly(A)-binding protein promotes VPg-dependent translation of potyvirus through enhanced binding of phosphorylated eIFiso4Fp and eIFiso4Fp-eIF4F. (PLOS ONE). 
4. Khan, MA, (2022) Ferritin iron responsive elements (IREs) mRNA interacts with eIF4G and activates in vitro translation. Frontiers in Biosciences-Elite 14(3):17. https://doi.org/10.31083/j.fbe1403017.
5. Khan MA and Domashevskiy AV (2021) Iron enhances the binding rates and protein synthesis of iron responsive elements (IREs) mRNA with translation initiation factor eIF4F. PLOS One, 16(4): e0250374, 1-20.
6. Khan MA, Akif M, Kumar, P., and Miyoshi H (2021) Phosphorylation of eukaryotic initiation factor eIFiso4E enhances the binding rates to VPg of turnip mosaic virus. PLOS One, 16(11) e0259688. https://doi.org/10.1371/journal.pone.0259688.
7. Khan MA, Malik A, Domashevskiy AV, San A and Khan JM (2020) Interaction of ferritin iron responsive element (IRE) mRNA with translation initiation factor eIF4F. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 243, 118776. https://doi.org/10.1016/j.saa.2020.118776.
8. Khan JM, Malik A, Khan MA, Sharma P and Sen P (2020) Pre-micellar concentrations of sodium dodecyl-benzene sulphonate induce amyloid like fibril formation in myoglobin at pH 4.5. Journal of Colloids and Surfaces A: Physicochemical and Engineering Aspects. 586, 124240.
9. Khan MA (2020) Analysis of ion and pH effects on iron response element (IRE) mRNA iron regulatory protein (IRP1) interactions. Current Chemical Biology. Volume 14, No. 2. doi: 10.2174/2212796814999200604121937.
10. Khan MA and Goss DJ (2019) Poly(A) binding protein enhances the binding affinity of potyvirus VPg to eukaryotic initiation factor eIF4F and activates in vitro translation. Int J Biol Macromol. Jan; 121: 947-955, doi: 10.1016/j.ijbiomac.2018.10.135.
11. Khan MA (2019) Phosphorylation of translation initiation factor eIfiso4E promotes translation through enhanced binding of potyvirus VPg. The Journal of Biochemistry (Oxford Press). Feb 1; 165(2): 167-176. doi: 10.1093/jb/mvy091.
12. Khan MA and Goss DJ (2018) Kinetic analyses of phosphorylated and non-phosphorylated eIFiso4E binding to mRNA cap analogues. Int. J. Biol Macromol. 106, 387-395.
13. Khan MA, Walden WE, Theil EC and Goss DJ (2017) Thermodynamic and kinetic analyses of iron response element (IRE)-mRNA binding to iron regulatory protein, IRP1. Scientific Report, 7(1): 8532. Doi: 10.1038/s41598-017-09093-5.
14. Khan MA (2016) Iron balancing mechanism: iron regulatory element (IRE)-messenger RNA metal sensing. BAOJ Biotechnology, Review Article, 2(3) 1-11.
15. Khan MA, Ma J, Walden WE, Merrick WC, Theil EC and Goss DJ (2014). Rapid Kinetics of Iron Responsive Element (IRE) RNA/Iron Regulatory Protein1 and IRE-RNA/eIF4F Complexes Respond Differently to Metal Ions. Nucleic Acid Research, 42(10) 6567-6577.
16. Ma J, Haldar S, Khan MA, Sharma S, Merrick WC, Theil EC and Goss DJ (2012). Fe2+ binds iron responsive element-RNA, selectively changing protein-binding affinities and regulating mRNA repression and activation. Proceedings of the National Academy of Sciences (PNAS) USA 109(22) 8417-8422.
17. Khan MA and Goss DJ (2012) Poly(A)-binding protein increases the binding affinity and kinetic rates of viral protein linked to genome (VPg) interaction with translation initiation factors eIFiso4F and eIFiso4F-4B complex. Biochemistry 51(7), 1388-95.
18. Ecevit O, Khan MA and Goss DJ (2010) Kinetic analysis of B/HLH/Z transcription factors c-Myc/Max/Mad with cognate DNA. Biochemistry 49(12): 2627-35.
19. Yumak H, Khan MA and Goss DJ (2010). Poly(A)-tail affects Equilibrium and Thermodynamic Behavior of Tobacco Etch Virus mRNA with Translation Initiation factors eIF4F.eIF4B and PABP. Gene Regulatory Mechanisms-BBA 1799(9), 653-658.
20. Khan MA, Walden WE, Goss DJ and Theil EC (2009) Direct Fe²⁺ Sensing by Iron Responsive Messenger RNA•Repressor Complexes Weakens Binding. J. Biol. Chem. 284(44), 30122-30128.
21. Khan MA, Yumak H and Goss DJ (2009). Kinetic Mechanism for the Binding of eIF4F and tobacco etch virus Internal Ribosome Entry Site RNA: Effects of eIF4B and Poly A Binding Protein. J. Biol. Chem. 284(51), 35461-70.
22. Baldwin A., Khan MA, Tumer NE, Goss DJ and Friedland DE (2009) Characterization of pokeweed antiviral protein binding to mRNA cap analogs: competition with nucleotides and enhancement by translation initiation factor iso4G. Gene Regulatory Mechanisms-BBA, 1789, 109-116.
23. Khan MA, Miyoshi H, Gallie DR and Goss DJ (2008) Potyvirus genome-linked protein, VPg, directly affects wheat germ in vitro translation: Interactions with translation initiation factors eIF4F and eIFiso4F. J. Biol. Chem, 283(3), 1340-1349.
24. Khan MA, Yumak H, Gallie DR and Goss DJ (2008). Effects of poly(A)-binding protein on the interactions of translation initiation factor eIF4F and eIF4F-4B with internal ribosome entry site (IRES) of tobacco etch virus RNA. Gene Regulatory Mechanisms-BBA, 1779, 622-627.
25. Khan MA, Miyoshi H, Ray S, Natsuaki T, Suehiro N and Goss DJ (2006) Interaction of Genome-linked Protein (VPg) of Turnip Mosaic Virus (TuMV) with Translation Initiation Factors eIFiso4E and eIFiso4F. J. Biol. Chem. 281 (38), 28002-28010.
26. Ray S, Yumak H, Domashevskiy A, Khan MA, Gallie DR and Goss DJ (2006). Tobacco etch virus mRNA preferentially binds eukaryotic initiation factor (eIF)4G rather than (eIF)iso4G. J. Biol. Chem. 281 (47), 35826-35834.
27. Khan MA and Goss DJ (2005) Translation Initiation factor (eIF) 4B affects the Rates of binding of the mRNA m⁷G cap analogue to eIFiso4F and eIFiso4F.PABP.  Biochemistry 44, 4510-4516.
28. Khan MA and Goss DJ (2004) Phosphorylation States of Translational Initiation factors (eIFs) affect mRNA Cap-Binding.  Biochemistry 43, 9092-9097.
29. Khan MA, Mustafa J and Musarrat J (2003) Mechanism of DNA strand breakage induced by photosensitized tetracycline-Cu (II) complex. Mutation Research, 525(1)109-119.
30.  Khan MA and Musarrat J (2003) Interactions of tetracyclines and its derivatives with DNA in vitro in presence of metal ions. Int. J. Biol. Macromol, 33 (1-3) 49-56.
31. Tayyab S, Khan NJ, Khan MA and Kumar Y (2003) Behavior of various mammalian albumins towards bilirubin binding and photochemical properties of different bilirubin-albumin complexes. Int. J. Biol. Macromol, 31, 187-193.
32. Khan MA, Muzammil S and Musarrat J (2002) Differential binding of tetracyclines with serum albumin and induced structural alterations in drug bound protein. Int. J. Biol. Macromol, 30(5), 243.
33. Khan MA and Musarrat J (2002) Tetracycline-Cu (II) photo-induced fragmentation of serum albumin. Comp. Biochem. Physiol.C Toxicol Pharmacol. 131 (4) 439-446.
34. Khan MA, Kumar Y and Tayyab S (2002) Bilirubin binding properties of pigeon serum albumin and its comparison with human serum albumin. Int. J. Biol. Macromol, 30: 171-178.
35. Jaiswal R, Khan MA and Musarrat J (2002) Photosensitized paraquat-induced structural alteratins and free radical mediated fragmentation of serum albumin. J. Photochem. Photobiol. 67(3), 163-170.
36. Khan MA, Muzammil S and Musarrat J (1998) “Interaction of photosensitized tetracycline with serum albumin” Biochem.  Mol.  Biol. Int., 46, 943-9