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Denis L. Rousseau

Researcher at Albert Einstein College of Medicine

Publications -  232
Citations -  11435

Denis L. Rousseau is an academic researcher from Albert Einstein College of Medicine. The author has contributed to research in topics: Heme & Cytochrome c oxidase. The author has an hindex of 58, co-authored 232 publications receiving 11044 citations. Previous affiliations of Denis L. Rousseau include University of Illinois at Urbana–Champaign & Yeshiva University.

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Journal ArticleDOI

Normal mode determination in crystals

Denis L. Rousseau, +2 more
- 01 Jan 1981 - 
TL;DR: In this article, a series of tables are presented to facilitate rapid determination of the selection rules for vibrational transitions for nuclear site group analysis, where the number of infrared and Raman active modes of each symmetry may be obtained without detailed analysis of the symmetry elements in the crystallographic unit cell or the construction of tables.
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First-Order Raman Effect in Wurtzite-Type Crystals

C. A. Arguello, +2 more
- 15 May 1969 - 
TL;DR: In this article, the effects of the competition between the long-range electrostatic forces and the short-range forces due to anisotropy in the interatomic force constants on the vibrational spectrum has been included.
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Submillisecond protein folding kinetics studied by ultrarapid mixing

Chi-Kin Chan, +6 more
- 04 Mar 1997 - 
TL;DR: An ultrarapid-mixing continuous-flow method has been developed to study submillisecond folding of chemically denatured proteins and raises several fundamental issues concerning the dynamics of collapse and barrier crossings in protein folding.
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A cooperative oxygen-binding hemoglobin from Mycobacterium tuberculosis

Manon Couture, +6 more
- 28 Sep 1999 - 
TL;DR: The results suggest that, physiologically, the primary role of HbN may be to protect the bacilli against reactive nitrogen species produced by the host macrophage.
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Neuronal Nitric Oxide Synthase Self-inactivates by Forming a Ferrous-Nitrosyl Complex during Aerobic Catalysis

Husam M. Abu-Soud, +5 more
- 29 Sep 1995 - 
TL;DR: It is concluded that a majority of neuronal NOS is converted quickly to a catalytically inactive ferrous-nitrosyl complex during NO synthesis independent of the external NO concentration, which indicates that NO binding to the NOS heme may be a fundamental feature of catalysis and functions to down-regulate NO synthesis by neurons.