Dawn M. Z. Schmidt - Concepedia

Concepedia

Author

Dawn M. Z. Schmidt

University of Illinois Urbana-Champaign

Also Known As

Dawn M. Schmidt, Dawn M. Z. Schmidt, Dawn M.Z. Schmidt

12

Publications

1.2K

Citations

9

H-Index

26

Concepts

All Affiliations

University of Illinois Urbana-Champaign Duke University University of Wisconsin–Madison University of Pennsylvania Center for Genomic Science

DM

About

Dawn M. Z. Schmidt is an author at University of Illinois Urbana-Champaign specializing in medicine, natural sciences, and biochemistry.

Top Concepts

#	Concept	H-Index	Publications	Citations
1	Medicine	4	4	588
2	Natural Sciences	3	3	150
3	Biochemistry	3	3	150
4	Chemical Biology	2	2	75
5	Chemistry	1	1	37

Dawn M. Z. Schmidt

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9

Publications

1.2K

Citations

9

H-Index

	Year	Citations
Histone H3 Lysine 4 Demethylation Is a Target of Nonselective Antidepressive Medications Min Gyu Lee, Christopher Wynder, Dawn M. Z. Schmidt, Chemistry & Biology Histone ModificationsChromatinNonselective Antidepressive MedicationsPsychiatryMedicine	2006	438
<i>trans</i>-2-Phenylcyclopropylamine Is a Mechanism-Based Inactivator of the Histone Demethylase LSD1 Dawn M. Z. Schmidt, Dewey G. McCafferty Biochemistry	2007	301
Evolutionary Potential of (β/α)<sub>8</sub>-Barrels: Functional Promiscuity Produced by Single Substitutions in the Enolase Superfamily Dawn M. Z. Schmidt, Emily C. Mundorff, Michael Dojka, Biochemistry	2003	171
Evolution of Enzymatic Activities in the Enolase Superfamily: Functional Assignment of Unknown Proteins in <i>Bacillus subtilis </i>and <i>Escherichia coli</i> as <scp>l</scp>-Ala-<scp>d</scp>/<scp>l</scp>-Glu Epimerases Dawn M. Z. Schmidt, Brian K. Hubbard, J.A. Gerlt Biochemistry	2001	84
Facile synthesis of substituted trans-2-arylcyclopropylamine inhibitors of the human histone demethylase LSD1 and monoamine oxidases A and B David M. Gooden, Dawn M. Z. Schmidt, Julie A. Pollock, Bioorganic & Medicinal Chemistry Letters Molecular PharmacologyMedicinal ChemistryBiochemistryMedicineFacile Synthesis	2008	75
Evolutionary Potential of (β/α)<sub>8</sub>-Barrels: In Vitro Enhancement of a “New” Reaction in the Enolase Superfamily Jacob E. Vick, Dawn M. Z. Schmidt, J.A. Gerlt Biochemistry	2005	50
Evolution of Enzymatic Activities in the Enolase Superfamily: Crystal Structures of the <scp>l</scp>-Ala-<scp>d</scp>/<scp>l</scp>-Glu Epimerases from <i>Escherichia coli</i> and <i>Bacillus subtilis</i><sup>,</sup> Andrew M. Gulick, Dawn M. Z. Schmidt, J.A. Gerlt, Biochemistry Bacillus SubtilisEnolase SuperfamilyBioorganic ChemistryEnzymatic ActivitiesBiochemistry	2001	38
Use of pH and Kinetic Isotope Effects To Establish Chemistry as Rate-Limiting in Oxidation of a Peptide Substrate by LSD1 Helena Gaweska, Michelle Henderson Pozzi, Dawn M. Z. Schmidt, Biochemistry Chemical AnalysisMolecular BiologyChemistryChemical BiologyRedox Biology	2009	37
Evolution of Enzymatic Activities in the Enolase Superfamily: Structure of a Substrate-Liganded Complex of the <scp>l</scp>-Ala-<scp>d</scp>/<scp>l</scp>-Glu Epimerase from <i>Bacillus subtilis</i><sup>,</sup> Vadim A. Klenchin, Dawn M. Z. Schmidt, J.A. Gerlt, Biochemistry	2004	36

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