J. Petrash

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alpha-Crystallin chaperone-like activity and membrane binding in age-related cataracts.

B. Cobb, J. Petrash, Brian A. Cobb, 2002, Biochemistry.

Temperature-dependent Chaperone Activity and Structural Properties of Human αA- and αB-crystallins*

W. Surewicz, K. Das, J. Petrash, 2000, The Journal of Biological Chemistry.

Kinetic and spectroscopic evidence for active site inhibition of human aldose reductase.

T. Nakano, J. Petrash, 1996, Biochemistry.

Probing the active site of human aldose reductase. Site-directed mutagenesis of Asp-43, Tyr-48, Lys-77, and His-110.

F. Quiocho, D. Borhani, J. Petrash, 1993, The Journal of biological chemistry.

Substrate specificity and catalytic efficiency of aldo-keto reductases with phospholipid aldehydes.

A. Bhatnagar, S. Baba, O. Barski, 2007, The Biochemical journal.

Structure-Function Studies of FR-1

S. Srivastava, A. Bhatnagar, S. Srivastava, 1999 .

Regulation of aldose reductase by aldehydes and nitric oxide.

S. Srivastava, A. Bhatnagar, S. Srivastava, 1999, Advances in experimental medicine and biology.

1.7 A structure of FR-1, a fibroblast growth factor-induced member of the aldo-keto reductase family, complexed with coenzyme and inhibitor.

F. Quiocho, T. Nakano, J. Petrash, 1995, Biochemistry.

Cloning, Expression, and Chaperone-like Activity of Human αA-Crystallin*

U. Andley, T. Griest, J. Petrash, 1996, The Journal of Biological Chemistry.

Interactions between small heat shock protein alpha-crystallin and galectin-related interfiber protein (GRIFIN) in the ocular lens.

J. Petrash, Cheng-Da Hsu, K. Barton, 2009, Biochemistry.

Aldose Reductase Protects Against Early Atherosclerotic Lesion Formation in Apolipoprotein E–Null Mice

A. Bhatnagar, B. Dawn, O. Barski, 2009, Circulation research.

Insight into the secondary structure of non-native proteins bound to a molecular chaperone alpha-crystallin. An isotope-edited infrared spectroscopic study.

L. Choo-Smith, W. Surewicz, K. Das, 1999, The Journal of biological chemistry.

Conformational Properties of Substrate Proteins Bound to a Molecular Chaperone -Crystallin (*)

W. Surewicz, K. Das, J. Petrash, 1996, The Journal of Biological Chemistry.

Aldose Reductase Catalysis and Crystallography: Insights From Recent Advances in Enzyme Structure and Function

F. Quiocho, David K Wilson, J. Petrash, 1994, Diabetes.

cDNA Clones encoding bovine γ-crystallins

R. E. Hay, J. Petrash, R. Church, 1987 .

Functional studies of aldo-keto reductases in Saccharomyces cerevisiae.

T. Griest, J. Petrash, T. Harter, 2007, Biochimica et biophysica acta.

Nucleotide sequence of a bovine lens αA-crystallin cDNA

R. E. Hay, J. Petrash, 1987 .

Specifically Targeted Modification of Human Aldose Reductase by Physiological Disulfides*

F. Quiocho, M. Dal Monte, A. Del Corso, 1996, The Journal of Biological Chemistry.

Purification, crystallization and preliminary crystallographic analysis of porcine aldose reductase.

K. Moore, L. DeLucas, O. El-Kabbani, 1991, Journal of molecular biology.

Oxidative modification of aldose reductase induced by copper ion. Factors and conditions affecting the process.

G. Rastelli, L. Costantino, D. Garland, 1998, Biochemistry.

Purification and properties of human liver aldehyde reductases.

S. Srivastava, J. Petrash, 1982, Biochimica et biophysica acta.

cDNA clones encoding bovine gamma-crystallins.

R. E. Hay, J. Petrash, R. Church, 1987, Biochemical and biophysical research communications.

Structural and kinetic modifications of aldose reductase by S-nitrosothiols.

K. Ramana, S. Srivastava, A. Bhatnagar, 2001, The Biochemical journal.

A novel mutation (F71L) in alphaA-crystallin with defective chaperone-like function associated with age-related cataract.

M. Vidyavathi, T. Padma, J. Petrash, 2009, Biochimica et biophysica acta.

Modification of aldose reductase by S-nitrosoglutathione.

S. Srivastava, A. Bhatnagar, S. Srivastava, 1997, Biochemistry.

Effects of osmotic stress and hyperglycemia on aldose reductase gene expression in human renal proximal tubule cells.

D. Sens, J. Bylander, J. Petrash, 1992, Biochemical and Biophysical Research Communications - BBRC.

Alteration of substrate selectivity through mutation of two arginine residues in the binding site of amadoriase II from Aspergillus sp.

V. Monnier, Shu G. Chen, J. Petrash, 2002, Biochemistry.

Insight into the Secondary Structure of Non-native Proteins Bound to a Molecular Chaperone α-Crystallin

L. Choo-Smith, W. Surewicz, K. Das, 1999, Journal of Biological Chemistry.

Characterization of α-Crystallin-Plasma Membrane Binding*

B. Cobb, J. Petrash, 2000, The Journal of Biological Chemistry.

Structural studies of aldo-keto reductase inhibition.

F. Quiocho, T. Nakano, J. Petrash, 1997, Advances in experimental medicine and biology.

Binding of 1-benzopyran-4-one derivatives to aldose reductase: a free energy perturbation study.

A. Ferrari, G. Rastelli, L. Costantino, 2002, Bioorganic & medicinal chemistry.

Kinetic characteristics of ZENECA ZD5522, a potent inhibitor of human and bovine lens aldose reductase.

W. Ward, R. Howe, F. Carey, 1995, Biochemical pharmacology.

Refined 1.8 A structure of human aldose reductase complexed with the potent inhibitor zopolrestat.

F A Quiocho, F. Quiocho, D K Wilson, 1993, Proceedings of the National Academy of Sciences of the United States of America.

The crystal structure of the aldose reductase.NADPH binary complex.

D. Borhani, J. Petrash, T. Harter, 1992, The Journal of biological chemistry.

All in the family: aldose reductase and closely related aldo-keto reductases

J. Petrash, 2004, Cellular and Molecular Life Sciences CMLS.

Structural and kinetic determinants of aldehyde reduction by aldose reductase.

S. Watowich, S. Srivastava, A. Bhatnagar, 1999, Biochemistry.

Detection of Herpes Simplex Virus Type 1 Latency—Associated Transcripts in Corneal Cells of Inbred Mice by In Situ Hybridization

R. D. Stulting, S. Abghari, J. Petrash, 1992, Cornea.

Characterization of alpha-crystallin-plasma membrane binding.

B. Cobb, J. Petrash, 2000, The Journal of biological chemistry.

Cloning, expression, and chaperone-like activity of human alphaA-crystallin.

U. Andley, T. Griest, J. Petrash, 1996, The Journal of biological chemistry.

Expression of Recombinant Bovine γB-, γC- and γD-Crystallins and Correlation with Native Proteins

R. E. Hay, U. Andley, J. Petrash, 1994 .

Susceptibility of aldehyde and aldose reductases of human tissues to aldose reductase inhibitors.

Samir K. Srivastava, S. Srivastava, N. Ansari, 1982, Current eye research.

A potential role for aldose reductase in steroid metabolism.

J. Petrash, G. L. Murdock, T. Harter, 1997, Advances in experimental medicine and biology.

Functional genomic studies of aldo-keto reductases.

M. Young, T. Griest, B. S. Murthy, 2001, Chemico-biological interactions.

Oxidative Modification of Aldose Reductase Induced by Copper Ion

G. Rastelli, A. Scaloni, L. Costantino, 2002, The Journal of Biological Chemistry.

Mouse Models of the Cornea and Lens: Understanding Ocular Disease

V. Vasiliou, S. Marchitti, J. Petrash, 2008 .

Inhibition of aldose reductase by dietary antioxidant curcumin: Mechanism of inhibition, specificity and significance

P. Suryanarayana, S. Gunda, P. Muthenna, 2009, FEBS letters.

Assignment of the mouse alpha A-crystallin structural gene to chromosome 17.

J. Piatigorsky, P. Lalley, J. Petrash, 1985, Current eye research.

Structural and functional changes in the alpha A-crystallin R116C mutant in hereditary cataracts.

B. Cobb, J. Petrash, 2000, Biochemistry.

Structure of a glutathione conjugate bound to the active site of aldose reductase

S. Watowich, K. Ramana, S. Srivastava, 2006, Proteins.

Temperature-dependent chaperone activity and structural properties of human alphaA- and alphaB-crystallins.

W. Surewicz, K. Das, J. Petrash, 2000, The Journal of biological chemistry.

Disruption of aldo-keto reductase genes leads to elevated markers of oxidative stress and inositol auxotrophy in Saccharomyces cerevisiae.

J Mark Petrash, Qing Chang, J. Petrash, 2008, Biochimica et biophysica acta.

Mechanisms Involved in the Protection of UV-induced Protein Inactivation by the Corneal Crystallin ALDH3A1*

V. Vasiliou, J. Carpenter, Tia Estey, 2007, Journal of Biological Chemistry.

Characterization of the glutathione binding site of aldose reductase.

S. Watowich, G. Balendiran, K. Ramana, 2001, Chemico-biological interactions.

Kinetic and Structural Characterization of the Glutathione-binding Site of Aldose Reductase*

S. Watowich, G. Balendiran, K. Ramana, 2000, The Journal of Biological Chemistry.

Structure-function studies of FR-1. A growth factor-inducible aldo-keto reductase.

A. Bhatnagar, J. Petrash, T. Harter, 1999, Advances in experimental medicine and biology.

Resolving isoforms of aldose reductase by preparative isoelectric focusing in the Rotofor

L. DeLucas, J. Petrash, N. Egen, 1991, Electrophoresis.

Erythrocyte aldose reductase activity and sorbitol levels in diabetic retinopathy

K. Viswanath, N. Balakrishna, R. Ayyagari, 2008, Molecular vision.

Formation of sorbitol 6-phosphate by bovine and human lens aldose reductase, sorbitol dehydrogenase and sorbitol kinase.

S. Srivastava, N. Ansari, J. Brown, 1982, Biochimica et biophysica acta.

Interrelationships among human aldo-keto reductases: immunochemical, kinetic and structural properties.

S. Srivastava, R. W. Gracy, N. Ansari, 1985, Biochimica et biophysica acta.

Applications of molecular biological techniques to the understanding of visual system disorders.

J. Petrash, 1992, American journal of ophthalmology.

7-Hydroxy-2-substituted-4-H-1-benzopyran-4-one derivatives as aldose reductase inhibitors: a SAR study.

G. Rastelli, L. Costantino, A. Del Corso, 2001, European journal of medicinal chemistry.

Comment on: the Stokes-Einstein equation and the physiological effects of vitreous surgery.

Y. Shui, D. Beebe, J. Petrash, 2007, Acta ophthalmologica Scandinavica.

Regional assignment of the mouse alpha A2-crystallin gene (Crya-1) to chromosome 17A3----B by in situ hybridization.

P. Lalley, J. Petrash, R. Church, 1990, Cytogenetics and Cell Genetics.

Aldo-keto reductases as modulators of stress response.

J. Petrash, T. Harter, Q. Chang, 2003, Chemico-biological interactions.

Mechanism of inhibition of aldose reductase by menadione (vitamin K3).

S. Srivastava, A. Bhatnagar, S. Liu, 1992, Molecular pharmacology.

The stratified syncytium of the vertebrate lens

Alan Shiels, S. Bassnett, Yanrong Shi, 2009, Journal of Cell Science.

Importance of eye lens α‐crystallin heteropolymer with 3:1 αA to αB ratio: Stability, aggregation, and modifications

M. J. Swamy, G. B. Reddy, J. M. Petrash, 2010, IUBMB life.

Aldose reductase deficiency in mice prevents azoxymethane-induced colonic preneoplastic aberrant crypt foci formation.

K. Ramana, S. Srivastava, R. Tammali, 2009, Carcinogenesis.

Involvement of cysteine residues in catalysis and inhibition of human aldose reductase. Site-directed mutagenesis of Cys-80, -298, and -303.

C. S. Devine, S. Srivastava, A. Bhatnagar, 1992, The Journal of biological chemistry.

Expression of recombinant bovine gamma B-, gamma C- and gamma D-crystallins and correlation with native proteins.

R. E. Hay, U. Andley, J. Petrash, 1994, Experimental Eye Research.

Aldo-keto reductases and toxicant metabolism

T. Penning, J. Petrash, T. Penning, 2003 .

Active site modification of aldose reductase by nitric oxide donors.

A. Bhatnagar, J. Petrash, A. Chandra, 1997, Biochimica et biophysica acta.

A transgenic mouse model for human autosomal dominant cataract.

S. Kymes, J. Petrash, Cheng-Da Hsu, 2006, Investigative ophthalmology & visual science.

Kinetic studies of FR-1, a growth factor-inducible aldo-keto reductase.

A. Bhatnagar, J. Petrash, T. Harter, 1998, Biochemistry.

Factors influencing α -crystallin association with phospholipid vesicles

B. Cobb, J. Petrash, 2002 .