Hasan (pronounce /hʌˈsɑːn/ as huh-SAHN) is an innovative Computational / Molecular Biologist with 5+ years of experience generating and handling Biological Big Data. I have designed pipelines for streamlined analysis of NGS data assisted by bioinformatics and machine learning algorithms that have analyzed Terabytes of data.
NGS Data Hasan knows how to analyze:
| PhD in Molecular and Developmental Biology | University of Cincinnati Oct 2023 |
| MS in Genetic Engineering and Biotechnology | University of Dhaka Sep 2017 |
| BS in Genetic Engineering and Biotechnology | University of Dhaka Feb 2016 |
| Time | Position | PI/Supervisor | Institution |
|---|---|---|---|
| 2025- | Bioinformatics Research | Beisi Xu / | St. Jude Children’s Research Hospital, |
| Scientist | Wojciech Rosikiewicz | Memphis, TN | |
| 2024-2025 | Bioinformatics Data | Yan Xu | Cincinnati Children’s Hospital Medical Center, |
| Scientist | Cincinnati, OH | ||
| 2023-2024 | Research Fellow | Takanori Takebe | CCHMC, Cincinnati, OH |
| 2018-2023 | Graduate Research Assistant | Takanori Takebe | CCHMC, Cincinnati, OH |
| 2016-2023 | Graduate Research Assistant | M. Aftab Uddin | University of Dhaka, Dhaka, Bangladesh |
| 2014-2016 | Undergraduate Research | Miraj Kobad | University of Dhaka, Dhaka, Bangladesh |
| Assistant | Chowdhury |
For a full list (GEO|SRA|Browser|Code) see below , or Google Scholar , or Pubmed
Abstract This study investigates bioelectric stimulation’s role in tissue regeneration by enhancing the piezoelectric properties of tissue‐engineered grafts using annealed poly(vinylidene fluoride‐trifluoroethylene) (PVDF‐TrFE) scaffolds. Annealing at temperatures of 80, 100, 120, and 140 °C is assessed for its impact on material properties and physiological utility. Analytical techniques such as Differential Scanning Calorimetry (DSC), Fourier‐Transform Infrared Spectroscopy (FTIR), and X‐ray Diffraction (XRD) reveal increased crystallinity with higher annealing temperatures, peaking in β‐phase content and crystallinity at 140 °C. Scanning Electron Microscopy (SEM) shows that 140 °C annealed scaffolds have enhanced lamellar structures, increased porosity, and maximum piezoelectric response. Mechanical tests indicate that 140 °C annealing improved elastic modulus, tensile strength, and substrate stiffness, aligning these properties with physiological soft tissues. In vitro assessments in Schwann cells demonstrate favorable responses, with increased cell proliferation, contraction, and extracellular matrix attachment. Additionally, genes linked to extracellular matrix production, vascularization, and calcium signaling are upregulated. The foreign body response in C57BL/6 mice, evaluated through Hematoxylin and Eosin (H&E) and Picrosirius Red staining, shows no differences between scaffold groups, supporting the potential for future functional evaluation of the annealed group in tissue repair.
Abstract Tumor suppressor cylindromatosis protein (CYLD) regulates NF-κB and JNK signaling pathways by cleaving K63-linked poly-ubiquitin chain from its substrate molecules and thus preventing the progression of tumorigenesis and metastasis of the cancer cells. Mutations in CYLD can cause aberrant structure and abnormal functionality leading to tumor formation. In this study, we utilized several computational tools such as PANTHER, PROVEAN, PredictSNP, PolyPhen-2, PhD-SNP, PON-P2, and SIFT to find out deleterious nsSNPs. We also highlighted the damaging impact of those deleterious nsSNPs on the structure and function of the CYLD utilizing ConSurf, I-Mutant, SDM, Phyre2, HOPE, Swiss-PdbViewer, and Mutation 3D. We shortlisted 18 high-risk nsSNPs from a total of 446 nsSNPs recorded in the NCBI database. Based on the conservation profile, stability status, and structural impact analysis, we finalized 13 nsSNPs. Molecular docking analysis and molecular dynamic simulation concluded the study with the findings of two significant nsSNPs (R830K, H827R) which have a remarkable impact on binding affinity, RMSD, RMSF, radius of gyration, and hydrogen bond formation during CYLD-ubiquitin interaction. The principal component analysis compared native and two mutants R830K and H827R of CYLD that signify structural and energy profile fluctuations during molecular dynamic (MD) simulation. Finally, the protein–protein interaction network showed CYLD interacts with 20 proteins involved in several biological pathways that mutations can impair. Considering all these in silico analyses, our study recommended conducting large-scale association studies of nsSNPs of CYLD with cancer as well as designing precise medications against diseases associated with these polymorphisms.