B. Mitra

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Metal-binding characteristics of the amino-terminal domain of ZntA: binding of lead is different compared to cadmium and zinc.

Jun-bo Liu, A. Stemmler, J. Fatima, 2005, Biochemistry.

From bortezomib to other inhibitors of the proteasome and beyond.

Sara Schmitt, Q Ping Dou, Q. Dou, 2013, Current pharmaceutical design.

Arginine 165/arginine 277 pair in (S)-mandelate dehydrogenase from Pseudomonas putida: role in catalysis and substrate binding.

B. Mitra, Yang Xu, A. Dewanti, 2002, Biochemistry.

Pb(II)-translocating P-type ATPases*

C. Rensing, B. Mitra, Y. Sun, 1998, The Journal of Biological Chemistry.

Insertional inactivation of dsbA produces sensitivity to cadmium and zinc in Escherichia coli

C. Rensing, B. Mitra, B. Rosen, 1997, Journal of bacteriology.

Involvement of ALAD‐20S Proteasome Complexes in Ubiquitination and Acetylation of Proteasomal α2 Subunits

Q. Dou, C. Neslund-Dudas, B. Mitra, 2016, Journal of cellular biochemistry.

Escherichia coli Soft Metal Ion-translocating ATPases*

B. Mitra, D. Gatti, B. Rosen, 2000, The Journal of Biological Chemistry.

Zinc, Cadmium, and Lead Resistance and Homeostasis

C. Rensing, B. Mitra, 2007 .

Case‐only gene–environment interaction between ALAD tagSNPs and occupational lead exposure in prostate cancer

A. Levin, N. Nock, Q. Dou, 2014, The Prostate.

The ATP Hydrolytic Activity of Purified ZntA, a Pb(II)/Cd(II)/Zn(II)-translocating ATPase from Escherichia coli *

C. Rensing, B. Mitra, B. Rosen, 2000, The Journal of Biological Chemistry.

Prostate Tissue Metal Levels and Prostate Cancer Recurrence in Smokers

C. Rogers, Q. Dou, C. Neslund-Dudas, 2014, Biological Trace Element Research.

Association between cadmium and androgen receptor protein expression differs in prostate tumors of African American and European American men.

A. Levin, C. Cordon-Cardo, C. Rogers, 2018, Journal of trace elements in medicine and biology : organ of the Society for Minerals and Trace Elements.

Association of Metals and Proteasome Activity in Erythrocytes of Prostate Cancer Patients and Controls

Di Chen, Q. Dou, C. Neslund-Dudas, 2012, Biological Trace Element Research.

A Zn(II)-translocating P-type ATPase from Proteus mirabilis.

C. Rensing, B. Mitra, B. Rosen, 1998, Biochemistry and cell biology = Biochimie et biologie cellulaire.

Characterization of three-subunit chloroplast coupling factor.

G. Hammes, B. Mitra, 1988, Biochemistry.

Membrane-protein structural mapping of chloroplast coupling factor in asolectin vesicles.

G. Hammes, B. Mitra, 1990, Biochemistry.

Antimonite is accumulated by the glycerol facilitator GlpF in Escherichia coli

C. Rensing, B. Mitra, B. Rosen, 1997, Journal of bacteriology.

High Resolution Structures of an Oxidized and Reduced Flavoprotein

F. S. Mathews, B. Mitra, N. Sukumar, 2004, Journal of Biological Chemistry.

CopA: An Escherichia coli Cu(I)-translocating P-type ATPase.

C. Rensing, B. Mitra, B. Rosen, 2000, Proceedings of the National Academy of Sciences of the United States of America.

Mechanism of the reaction catalyzed by mandelate racemase: structure and mechanistic properties of the D270N mutant.

G L Kenyon, G A Petsko, G. Petsko, 1995, Biochemistry.

The zntA gene of Escherichia coli encodes a Zn(II)-translocating P-type ATPase.

C. Rensing, B. Mitra, B. Rosen, 1997, Proceedings of the National Academy of Sciences of the United States of America.

Discovering proteasomal deubiquitinating enzyme inhibitors for cancer therapy: lessons from rational design, nature and old drug reposition.

Q. Dou, Jinbao Liu, C. Neslund-Dudas, 2018, Future medicinal chemistry.

Conserved aspartic acid 714 in transmembrane segment 8 of the ZntA subgroup of P1B-type ATPases is a metal-binding residue.

Jun-bo Liu, B. Mitra, Z. Hou, 2006, Biochemistry.

Metal-binding affinity of the transmembrane site in ZntA: implications for metal selectivity.

Jun-bo Liu, A. Stemmler, B. Mitra, 2006, Biochemistry.

Conservative and nonconservative mutations of the transmembrane CPC motif in ZntA: effect on metal selectivity and activity.

Jun-bo Liu, A. Stemmler, B. Mitra, 2007, Biochemistry.

The cysteine-rich amino-terminal domain of ZntA, a Pb(II)/Zn(II)/Cd(II)-translocating ATPase from Escherichia coli, is not essential for its function.

B. Mitra, R. Sharma, 2001, Biochemistry.

The Zinc and Iron Binuclear Transport Center of ZupT, a ZIP Transporter from Escherichia coli.

B. Mitra, Fei Ni, C. Roberts, 2021, Biochemistry.

Structures of the G81A mutant form of the active chimera of (S)-mandelate dehydrogenase and its complex with two of its substrates.

A. Merli, B. Mitra, G. Rossi, 2009, Acta crystallographica. Section D, Biological crystallography.

Association of Metals and Proteasome Activity in Erythrocytes of Prostate Cancer Patients and Controls

Di Chen, Q. Dou, C. Neslund-Dudas, 2012, Biological Trace Element Research.

Mechanism of the reaction catalyzed by mandelate racemase: importance of electrophilic catalysis by glutamic acid 317.

G. Petsko, J. Clifton, G. L. Kenyon, 1995, Biochemistry.

Gene–environment interactions between JAZF1 and occupational and household lead exposure in prostate cancer among African American men

T. Rebbeck, A. Levin, N. Nock, 2014, Cancer Causes & Control.

Kinetic analysis of metal binding to the amino-terminal domain of ZntA by monitoring metal-thiolate charge-transfer complexes.

Jun-bo Liu, B. Mitra, S. Dutta, 2005, Biochemistry.

(S)-Mandelate dehydrogenase from Pseudomonas putida: mutations of the catalytic base histidine-274 and chemical rescue of activity.

B. Mitra, I. Lehoux, 1999, Biochemistry.

A highly active, soluble mutant of the membrane-associated (S)-mandelate dehydrogenase from Pseudomonas putida.

B. Mitra, Y. Xu, 1999, Biochemistry.

(S)-Mandelate dehydrogenase from Pseudomonas putida: mechanistic studies with alternate substrates and pH and kinetic isotope effects.

B. Mitra, I. Lehoux, 1999, Biochemistry.

Structure of the monotopic membrane protein (S)-mandelate dehydrogenase at 2.2 Å resolution.

B. Mitra, N. Sukumar, P. Kandavelu, 2018, Biochimie.

Role of glycine 81 in (S)-mandelate dehydrogenase from Pseudomonas putida in substrate specificity and oxidase activity.

B. Mitra, Yang Xu, A. Dewanti, 2004, Biochemistry.

A transient intermediate in the reaction catalyzed by (S)-mandelate dehydrogenase from Pseudomonas putida.

B. Mitra, A. Dewanti, 2003, Biochemistry.

Structure of an active soluble mutant of the membrane-associated (S)-mandelate dehydrogenase.

B. Mitra, N. Sukumar, D. Gatti, 2001, Biochemistry.

High Resolution Structures of an Oxidized and Reduced Flavoprotein THE WATER SWITCH IN A SOLUBLE FORM OF (S)-MANDELATE DEHYDROGENASE*

B. Mitra, N. Sukumar, A. Dewanti, 2004 .

The Metal Specificity and Selectivity of ZntA from Escherichia coli Using the Acylphosphate Intermediate*

B. Mitra, Z. Hou, 2003, Journal of Biological Chemistry.

Functional Analysis of Chimeric Proteins of the Wilson Cu(I)-ATPase (ATP7B) and ZntA, a Pb(II)/Zn(II)/Cd(II)-ATPase fromEscherichia coli *

B. Mitra, Zhanqun Hou, B. Sarkar, 2001, The Journal of Biological Chemistry.