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Nirmala Ramanujam

Researcher at Duke University

Publications -  198
Citations -  10422

Nirmala Ramanujam is an academic researcher from Duke University. The author has contributed to research in topics: Diffuse reflectance infrared fourier transform & Breast cancer. The author has an hindex of 51, co-authored 185 publications receiving 9914 citations. Previous affiliations of Nirmala Ramanujam include University of Texas at Austin & Durham University.

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In vivo multiphoton microscopy of NADH and FAD redox states, fluorescence lifetimes, and cellular morphology in precancerous epithelia

TL;DR: This study combines cellular redox ratio, NADH and FAD lifetime, and subcellular morphology imaging in three dimensions to identify intrinsic sources of metabolic and structural contrast in vivo at the earliest stages of cancer development.
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Fluorescence Spectroscopy of Neoplastic and Non-Neoplastic Tissues

TL;DR: A comprehensive review on steady-state and time-resolved, fluorescence measurements of neoplastic and non-neoplastic, biologic systems of varying degrees of complexity is provided.
Reference EntryDOI

Fluorescence Spectroscopy In Vivo

TL;DR: The goal of this report is to review the development and application of optical spectroscopy in the ultraviolet (UV) and visible (VIS) spectral regions, as a diagnostic tool in clinical applications, with a particular emphasis on steady-state, UV/VIS fluorescence spectroscopic for the detection of precancers and cancers, in vivo.
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Metabolic Mapping of MCF10A Human Breast Cells via Multiphoton Fluorescence Lifetime Imaging of the Coenzyme NADH

TL;DR: A novel method for deriving functional maps of intracellular reduction-oxidation ratio in vivo via measurement of the fluorescence lifetimes and the ratio of free and protein-bound NADH using two-photon fluorescence lifetime imaging (FLIM).
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In vivo multiphoton fluorescence lifetime imaging of protein-bound and free nicotinamide adenine dinucleotide in normal and precancerous epithelia

TL;DR: Results indicate that the decrease in protein-bound NADH lifetime with dysplasia is due to a shift from oxidative phosphorylation to glycolysis, consistent with the predictions of neoplastic metabolism.