W. Pratt

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p50 cdc37 Binds Directly to the Catalytic Domain of Raf as Well as to a Site on hsp90 That Is Topologically Adjacent to the Tetratricopeptide Repeat Binding Site*

B. Cochran, A. Silverstein, N. Grammatikakis, 1998, The Journal of Biological Chemistry.

A model for the cytoplasmic trafficking of signalling proteins involving the hsp90-binding immunophilins and p50cdc37.

M. Galigniana, A. Silverstein, W. Pratt, 1999, Cellular signalling.

Heat shock protein 90-dependent (geldanamycin-inhibited) movement of the glucocorticoid receptor through the cytoplasm to the nucleus requires intact cytoskeleton.

M. Welsh, J. Herrington, C. Carter-Su, 1998, Molecular endocrinology.

Evidence That the Peptidylprolyl Isomerase Domain of the hsp90-binding Immunophilin FKBP52 Is Involved in Both Dynein Interaction and Glucocorticoid Receptor Movement to the Nucleus*

M. Galigniana, W. Pratt, J. Renoir, 2001, The Journal of Biological Chemistry.

Steroid receptor interactions with heat shock protein and immunophilin chaperones.

W. Pratt, D. Toft, David O. Toft, 1997, Endocrine reviews.

HDAC6 regulates Hsp90 acetylation and chaperone-dependent activation of glucocorticoid receptor.

Minoru Yoshida, June-Tai Wu, C. Nicchitta, 2005, Molecular cell.

The hsp90-based Chaperone System: Involvement in Signal Transduction from a Variety of Hormone and Growth Factor Receptors

W. Pratt, 1998, Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine.

Nucleotide Binding States of hsp70 and hsp90 during Sequential Steps in the Process of Glucocorticoid Receptor·hsp90 Heterocomplex Assembly*

W. Pratt, K. C. Kanelakis, D. Shewach, 2002, The Journal of Biological Chemistry.

The Hsp Organizer Protein Hop Enhances the Rate of but Is Not Essential for Glucocorticoid Receptor Folding by the Multiprotein Hsp90-based Chaperone System*

A. Silverstein, W. Pratt, K. C. Kanelakis, 2000, The Journal of Biological Chemistry.

Studies with Purified Chaperones Advance the Understanding of the Mechanism of Glucocorticoid Receptor–hsp90 Heterocomplex Assembly

W. Pratt, K. D. Dittmar, 1998, Trends in Endocrinology & Metabolism.

Evidence that the 90-kDa phosphoprotein associated with the untransformed L-cell glucocorticoid receptor is a murine heat shock protein.

W. Pratt, E. R. Sánchez, D. Toft, 1985, The Journal of biological chemistry.

Direct evidence that the glucocorticoid receptor binds to hsp90 at or near the termination of receptor translation in vitro.

S. Watson, E. Bresnick, W. Pratt, 1989, The Journal of biological chemistry.

Evidence that the 90-kDa heat shock protein is necessary for the steroid binding conformation of the L cell glucocorticoid receptor.

E. Bresnick, W. Pratt, E. R. Sánchez, 1989, The Journal of biological chemistry.

Structural and functional reconstitution of the glucocorticoid receptor-hsp90 complex.

S. Meshinchi, W. Pratt, F. C. Dalman, 1990, The Journal of biological chemistry.

Control of steroid receptor function and cytoplasmic‐nuclear transport by heat shock proteins

W. Pratt, 1992, BioEssays : news and reviews in molecular, cellular and developmental biology.

Monovalent cation selectivity for ATP-dependent association of the glucocorticoid receptor with hsp70 and hsp90.

W. Pratt, L. Scherrer, K. Hutchison, 1992, The Journal of biological chemistry.

The protein-protein complex between pp60v-src and hsp90 is stabilized by molybdate, vanadate, tungstate, and an endogenous cytosolic metal.

R. Jove, W. Pratt, L. Stancato, 1992, The Journal of biological chemistry.

Reconstitution of the multiprotein complex of pp60src, hsp90, and p50 in a cell-free system.

R. Jove, W. Pratt, G. Perdew, 1992, The Journal of biological chemistry.

Raf exists in a native heterocomplex with hsp90 and p50 that can be reconstituted in a cell-free system.

R. Jove, W. Pratt, G. Perdew, 1993, The Journal of biological chemistry.

The hsp56 immunophilin component of steroid receptor heterocomplexes: Could this be the elusive nuclear localization signal-binding protein?

W. Pratt, L. Stancato, M. Czar, 1993, The Journal of Steroid Biochemistry and Molecular Biology.

All of the factors required for assembly of the glucocorticoid receptor into a functional heterocomplex with heat shock protein 90 are preassociated in a self-sufficient protein folding structure, a "foldosome".

W. Pratt, K. D. Dittmar, K. Hutchison, 1994, The Journal of biological chemistry.

Proof that hsp70 is required for assembly of the glucocorticoid receptor into a heterocomplex with hsp90.

W. Pratt, K. D. Dittmar, K. Hutchison, 1994, The Journal of biological chemistry.

The native v-Raf.hsp90.p50 heterocomplex contains a novel immunophilin of the FK506 binding class.

R. Jove, W. Pratt, L. Stancato, 1994, The Journal of biological chemistry.

The hsp56 immunophilin component of untransformed steroid receptor complexes is localized both to microtubules in the cytoplasm and to the same nonrandom regions within the nucleus as the steroid receptor.

M. Welsh, K. Leach, W. Pratt, 1994, Molecular endocrinology.

Characterization of the protein-protein interactions determining the heat shock protein (hsp90.hsp70.hsp56) heterocomplex.

K. Leach, W. Pratt, M. Deibel, 1994, The Journal of biological chemistry.

The 23-kDa Acidic Protein in Reticulocyte Lysate Is the Weakly Bound Component of the hsp Foldosome That Is Required for Assembly of the Glucocorticoid Receptor into a Functional Heterocomplex with hsp90 (*)

W. Pratt, J. Johnson, D. Toft, 1995, The Journal of Biological Chemistry.

The Cyclosporin A-binding Immunophilin CyP-40 and the FK506-binding Immunophilin hsp56 Bind to a Common Site on hsp90 and Exist in Independent Cytosolic Heterocomplexes with the Untransformed Glucocorticoid Receptor (*)

W. Pratt, R. Handschumacher, M. Deibel, 1995, The Journal of Biological Chemistry.

Evidence that the FK506-binding immunophilin heat shock protein 56 is required for trafficking of the glucocorticoid receptor from the cytoplasm to the nucleus.

M. Welsh, R. Lyons, W. Pratt, 1995, Molecular endocrinology.

Use of the Thiol-specific Derivatizing Agent N-Iodoacetyl-3-Iiodotyrosine to Demonstrate Conformational Differences between the Unbound and hsp90-bound Glucocorticoid Receptor Hormone Binding Domain (*)

B. Groner, A. Silverstein, W. Pratt, 1996, The Journal of Biological Chemistry.

A Model of Protein Targeting Mediated by Immunophilins and Other Proteins That Bind to hsp90 via Tetratricopeptide Repeat Domains*

W. Pratt, G. Perdew, K. Hutchison, 1996, The Journal of Biological Chemistry.

Animal and plant cell lysates share a conserved chaperone system that assembles the glucocorticoid receptor into a functional heterocomplex with hsp90.

W. Pratt, L. Stancato, K. Hutchison, 1996, Biochemistry.

The Tetratricopeptide Repeat Domain of Protein Phosphatase 5 Mediates Binding to Glucocorticoid Receptor Heterocomplexes and Acts as a Dominant Negative Mutant*

A. Silverstein, Michael Chinkers, W. Pratt, 1996, The Journal of Biological Chemistry.

Reconstitution of the Steroid Receptor·hsp90 Heterocomplex Assembly System of Rabbit Reticulocyte Lysate*

W. Pratt, K. D. Dittmar, K. Hutchison, 1996, The Journal of Biological Chemistry.

Binding of immunophilins to the 90 kDa heat shock protein (hsp90) via a tetratricopeptide repeat domain is a conserved protein interaction in plants.

W. Pratt, L. Stancato, J. Owens-grillo, 1996, Biochemistry.

Folding of the Glucocorticoid Receptor by the Heat Shock Protein (hsp) 90-based Chaperone Machinery

W. Pratt, L. Stancato, P. Krishna, 1997, The Journal of Biological Chemistry.

Protein Phosphatase 5 Is a Major Component of Glucocorticoid Receptor·hsp90 Complexes with Properties of an FK506-binding Immunophilin*

M. Galigniana, A. Silverstein, Michael Chinkers, 1997, The Journal of Biological Chemistry.

Folding of the Glucocorticoid Receptor by the Reconstituted hsp90-based Chaperone Machinery

W. Pratt, K. D. Dittmar, 1997, The Journal of Biological Chemistry.

The hsp90-binding Antibiotic Geldanamycin Decreases Raf Levels and Epidermal Growth Factor Signaling without Disrupting Formation of Signaling Complexes or Reducing the Specific Enzymatic Activity of Raf Kinase*

R. Jove, A. Silverstein, W. Pratt, 1997, The Journal of Biological Chemistry.

Geldanamycin, a heat shock protein 90-binding benzoquinone ansamycin, inhibits steroid-dependent translocation of the glucocorticoid receptor from the cytoplasm to the nucleus.

M. Galigniana, A. Silverstein, W. Pratt, 1997, Biochemistry.

Evidence for Glucocorticoid Receptor Transport on Microtubules by Dynein*

Jennifer M Harrell, M. Galigniana, W. Pratt, 2004, Journal of Biological Chemistry.

Wild-type EGFR is stabilized by direct interaction with HSP90 in cancer cells and tumors.

S. Jolly, A. Rehemtulla, C. Van Waes, 2012, Neoplasia.

Chaperoning of glucocorticoid receptors.

W. Pratt, M. Murphy, Y. Morishima, 2006, Handbook of experimental pharmacology.

The effect of glucocorticoids on protein and nucleic acid synthesis in mouse fibroblasts growing in vitro.

W. Pratt, L. Aronow, 1966, The Journal of biological chemistry.

Retrograde transport of the glucocorticoid receptor in neurites requires dynamic assembly of complexes with the protein chaperone hsp90 and is linked to the CHIP component of the machinery for proteasomal degradation.

Jennifer M Harrell, C. Patterson, M. Galigniana, 2004, Brain research. Molecular brain research.

Role of molecular chaperones in steroid receptor action.

M. Galigniana, W. Pratt, P. Murphy, 2004, Essays in biochemistry.

Cyclophilin-A Is Bound through Its Peptidylprolyl Isomerase Domain to the Cytoplasmic Dynein Motor Protein Complex*

M. Galigniana, W. Pratt, P. Gallay, 2004, Journal of Biological Chemistry.

Specific glucocorticoid-binding macromolecules from mouse fibroblasts growing in vitro. A possible steroid receptor for growth inhibition.

W. Pratt, J. Hackney, L. Aronow, 1970, Molecular pharmacology.

The active transport of cortisol by mouse fibroblasts growing in vitro.

W. Pratt, S. R. Gross, L. Arow, 1968, Proceedings of the Western Pharmacology Society.

THE OUTWARD TRANSPORT OF CORTISOL BY MAMMALIAN CELLS IN VITRO

W. Pratt, L. Aronow, S. R. Gross, 1970, The Journal of cell biology.

Relationship of the 90-kDa murine heat shock protein to the untransformed and transformed states of the L cell glucocorticoid receptor.

S. Meshinchi, W. Pratt, E. R. Sánchez, 1987, The Journal of biological chemistry.

[39] Glucocorticoid receptor thiols andsteroid-binding activity

W. Pratt, S. Simons, 1995 .

ATP-dependent activation of L cell glucocorticoid receptors to the steroid binding form.

W. Pratt, J. J. Sando, A. C. La Forest, 1979, The Journal of biological chemistry.

Proof that the endogenous, heat-stable glucocorticoid receptor-activating factor is thioredoxin.

A. Holmgren, J. Grippo, W. Pratt, 1985, The Journal of biological chemistry.

FUNDAMENTALS OF CHEMOTHERAPY

W. Pratt, 1974, The Ulster Medical Journal.

Targeting Proteostasis Through the Protein Quality Control Function of the Hsp90/Hsp70-based Chaperone Machinery for Treatment of Adult Onset Neurodegenerative Diseases

J. Gestwicki, W. Pratt, A. Lieberman, 2015 .

Heme-dependent activation of neuronal nitric oxide synthase by cytosol is due to an Hsp70-dependent, thioredoxin-mediated thiol-disulfide interchange in the heme/substrate binding cleft.

J. Gestwicki, W. Pratt, Yoshinari Miyata, 2011, Biochemistry.

The Role of hsp90 in Heme-dependent Activation of Apo-neuronal Nitric-oxide Synthase*

W. Pratt, P. Murphy, Y. Morishima, 2004, Journal of Biological Chemistry.

Immunofluorescence localization of the 90-kDa heat-shock protein to cytoskeleton.

M. Welsh, W. Pratt, M. Czar, 1996, European journal of cell biology.

Immunofluorescence colocalization of the 90-kDa heat-shock protein and microtubules in interphase and mitotic mammalian cells.

M. Welsh, E. Bresnick, W. Pratt, 1989, European journal of cell biology.

Regulation of Signaling Protein Function and Trafficking by the hsp90/hsp70-Based Chaperone Machinery 1

W. Pratt, D. Toft, 2003, Experimental biology and medicine.

Chaperone Activity and Dimerization Properties of Hsp90α and Hsp90β in Glucocorticoid Receptor Activation by the Multiprotein Hsp90/Hsp70-Dependent Chaperone Machinery

T. Lawrence, W. Pratt, M. Nyati, 2018, Molecular Pharmacology.

ATM is the primary kinase responsible for phosphorylation of Hsp90α after ionizing radiation

T. Lawrence, D. Ray, W. Pratt, 2016, Oncotarget.

CHIP deletion reveals functional redundancy of E3 ligases in promoting degradation of both signaling proteins and expanded glutamine proteins.

Zhigang Yu, W. Pratt, A. Lieberman, 2008, Human molecular genetics.

Regulation of the Dynamics of hsp90 Action on the Glucocorticoid Receptor by Acetylation/Deacetylation of the Chaperone*

T. Yao, W. Pratt, Jeffrey J. Kovacs, 2005, Journal of Biological Chemistry.

Ubiquitylation of Neuronal Nitric-oxide Synthase by CHIP, a Chaperone-dependent E3 Ligase*

C. Patterson, W. Pratt, Y. Morishima, 2004, Journal of Biological Chemistry.

The Hsp90 Cochaperone p23 Is the Limiting Component of the Multiprotein Hsp90/Hsp70-based Chaperone System in Vivo Where It Acts to Stabilize the Client Protein·Hsp90 Complex*

R. Sunahara, W. Pratt, K. C. Kanelakis, 2003, Journal of Biological Chemistry.

Visualization and Mechanism of Assembly of a Glucocorticoid Receptor·Hsp70 Complex That Is Primed for Subsequent Hsp90-dependent Opening of the Steroid Binding Cleft*

M. Galigniana, W. Pratt, P. Murphy, 2003, Journal of Biological Chemistry.

Binding of hsp90 to the Glucocorticoid Receptor Requires a Specific 7-Amino Acid Sequence at the Amino Terminus of the Hormone-binding Domain*

G. Giannoukos, W. Pratt, K. D. Dittmar, 1998, The Journal of Biological Chemistry.

hsp70 interacting protein Hip does not affect glucocorticoid receptor folding by the hsp90-based chaperone machinery except to oppose the effect of BAG-1.

John Calvin Reed, S. Takayama, M. Galigniana, 2000, Biochemistry.

Stoichiometry, Abundance, and Functional Significance of the hsp90/hsp70-based Multiprotein Chaperone Machinery in Reticulocyte Lysate*

M. Galigniana, W. Pratt, K. C. Kanelakis, 2001, The Journal of Biological Chemistry.

Stepwise Assembly of a Glucocorticoid Receptor·hsp90 Heterocomplex Resolves Two Sequential ATP-dependent Events Involving First hsp70 and Then hsp90 in Opening of the Steroid Binding Pocket*

W. Pratt, E. R. Sánchez, P. Murphy, 2000, The Journal of Biological Chemistry.

Hsp90-binding immunophilins in plants: the protein movers.

W. Pratt, P. Krishna, L. J. Olsen, 2001, Trends in plant science.

Different Regions of the Immunophilin FKBP52 Determine Its Association with the Glucocorticoid Receptor, hsp90, and Cytoplasmic Dynein*

M. Galigniana, A. Silverstein, W. Pratt, 1999, The Journal of Biological Chemistry.

All of the protein interactions that link steroid receptor.hsp90.immunophilin heterocomplexes to cytoplasmic dynein are common to plant and animal cells.

I. Kurek, M. Galigniana, W. Pratt, 2002, Biochemistry.

Evidence for iterative ratcheting of receptor-bound hsp70 between its ATP and ADP conformations during assembly of glucocorticoid receptor.hsp90 heterocomplexes.

W. Pratt, K. C. Kanelakis, P. Murphy, 2001, Biochemistry.

The Role of DnaJ-like Proteins in Glucocorticoid Receptor·hsp90 Heterocomplex Assembly by the Reconstituted hsp90·p60·hsp70 Foldosome Complex*

M. Galigniana, W. Pratt, K. D. Dittmar, 1998, The Journal of Biological Chemistry.

The Seven Amino Acids (547–553) of Rat Glucocorticoid Receptor Required for Steroid and Hsp90 Binding Contain a Functionally Independent LXXLL Motif That Is Critical for Steroid Binding*

G. Giannoukos, A. Silverstein, W. Pratt, 1999, The Journal of Biological Chemistry.

Binding of hsp90-associated immunophilins to cytoplasmic dynein: direct binding and in vivo evidence that the peptidylprolyl isomerase domain is a dynein interaction domain.

Mingjie Zhang, M. Galigniana, Michael Chinkers, 2002, Biochemistry.

Interaction of the glucocorticoid receptor with the Mr 90,000 heat shock protein: an evolving model of ligand-mediated receptor transformation and translocation.

M. Welsh, S. Meshinchi, E. Bresnick, 1989, Cancer research.

The molybdate-stabilized glucocorticoid binding complex of L-cells contains a 98-100 kdalton steroid binding phosphoprotein and a 90 kdalton nonsteroid-binding phosphoprotein that is part of the murine heat-shock complex.

W. Pratt, E. R. Sánchez, P. R. Housley, 1986, Journal of Steroid Biochemistry.

Demonstration that the 90-kilodalton heat shock protein is bound to the glucocorticoid receptor in its 9S nondeoxynucleic acid binding form.

S. Meshinchi, W. Pratt, E. R. Sánchez, 1987, Molecular endocrinology.

A model of glucocorticoid receptor unfolding and stabilization by a heat shock protein complex

W. Pratt, F. C. Dalman, L. Scherrer, 1992, The Journal of Steroid Biochemistry and Molecular Biology.

Glucocorticoid receptor activation and inactivation in cultured human lymphocytes.

K. Leach, W. Pratt, R. Wheeler, 1981, The Journal of biological chemistry.

Redox manipulation of DNA binding activity and BuGR epitope reactivity of the glucocorticoid receptor.

S. Meshinchi, E. Bresnick, W. Pratt, 1991, The Journal of biological chemistry.

Interaction of hsp90 with steroid receptors: organizing some diverse observations and presenting the newest concepts

W. Pratt, 1990, Molecular and Cellular Endocrinology.

Mutations at Positions 547–553 of Rat Glucocorticoid Receptors Reveal That hsp90 Binding Requires the Presence, but Not Defined Composition, of a Seven-amino Acid Sequence at the Amino Terminus of the Ligand Binding Domain*

S. Kaul, W. Pratt, P. Murphy, 2002, The Journal of Biological Chemistry.

Differential Responsivity of the Hypothalamic‐Pituitary‐Adrenal Axis to Glucocorticoid Negative‐Feedback and Corticotropin Releasing Hormone in Rats Undergoing Morphine Withdrawal: Possible Mechanisms Involved in Facilitated and Attenuated Stress Responses

H. Houshyar, M. Galigniana, W. Pratt, 2001, Journal of neuroendocrinology.

Effects of molybdate and endogenous inhibitors on steroid-receptor inactivation, transformation, and translocation.

W. Pratt, M. Dahmer, P. R. Housley, 1984, Annual review of physiology.

Regulation of Glucocorticoid Receptor Function through Assembly of a Receptor‐Heat Shock Protein Complex a

R. Jove, W. Pratt, L. Stancato, 1993, Annals of the New York Academy of Sciences.

Heat Shock Proteins and the Cytoplasmic-Nuclear Trafficking of Steroid Receptors

W. Pratt, L. Scherrer, 1994 .

Evidence that the hormone-binding domain of the mouse glucocorticoid receptor directly represses DNA binding activity in a major portion of receptors that are "misfolded" after removal of hsp90.

W. Pratt, K. Hutchison, M. Czar, 1992, Journal of Biological Chemistry.

Inactivation of glucocorticoid receptors in cell-free preparations of rat liver.

W. Pratt, W. Vogel, C. Nielsen, 1977, Cancer research.

Direct demonstration of glucocorticoid receptor phosphorylation by intact L-cells.

W. Pratt, P. R. Housley, 1983, The Journal of biological chemistry.

Regulation of glucocorticoid receptor ligand-binding activity by the hsp90/hsp70-based chaperone machinery.

W. Pratt, K. C. Kanelakis, 2003, Methods in enzymology.

Hormone-free mouse glucocorticoid receptors overexpressed in Chinese hamster ovary cells are localized to the nucleus and are associated with both hsp70 and hsp90.

J. Harmon, M. Welsh, W. Pratt, 1990, The Journal of biological chemistry.

Transformation of glucocorticoid and progesterone receptors to the DNA‐binding state

W. Pratt, 1987, Journal of cellular biochemistry.

Glucocorticoid receptor thiols and steroid-binding activity.

W. Pratt, S. Simons, 1995, Methods in enzymology.

Hydrogen peroxide stabilizes the steroid-binding state of rat liver glucocorticoid receptors by promoting disulfide bond formation.

R. Harrison, E. Bresnick, W. Pratt, 1988, Biochemistry.

Inhibition of Glucocorticoid Receptor Nucleocytoplasmic Shuttling by Okadaic Acid Requires Intact Cytoskeleton*

D. DeFranco, M. Galigniana, W. Pratt, 1999, The Journal of Biological Chemistry.

Molybdate inhibition of glucocorticoid receptor inactivation and transformation.

K. Leach, W. Pratt, M. Dahmer, 1979, The Journal of biological chemistry.

Steroid receptor folding by heat-shock proteins and composition of the receptor heterocomplex

W. Pratt, L. Scherrer, K. Hutchison, 1992, Trends in Endocrinology & Metabolism.

Glucocorticoid receptor inactivation under cell-free conditions.

W. Pratt, J. J. Sando, W. Vogel, 1977, The Journal of biological chemistry.

Endosymbionts as a source of cytoplasmic satellite deoxyribonucleic acid.

W. Pratt, L. Aronow, S. R. Gross, 1968, Journal of molecular biology.

FK506 binding to the 56-kilodalton immunophilin (Hsp56) in the glucocorticoid receptor heterocomplex has no effect on receptor folding or function.

K. Leach, W. Pratt, E. R. Sánchez, 1993, Biochemistry.

Glucocorticoid receptor phosphorylation, transformation, and DNA binding.

R. Harrison, W. Pratt, E. R. Sánchez, 1987, The Journal of biological chemistry.

Evidence that the FK506-binding immunophilin heat shock protein 56 is required for trafficking of the glucocorticoid receptor from the cytoplasm to the nucleus.

M. Welsh, R. Lyons, W. Pratt, 1995, Molecular endocrinology.

Localization of phosphorylation sites with respect to the functional domains of the mouse L cell glucocorticoid receptor.

W. Pratt, E. R. Sánchez, F. C. Dalman, 1988, The Journal of biological chemistry.

Evidence that dephosphorylation inactivates glucocorticoid receptors.

W. Pratt, J. J. Sando, C. Nielsen, 1977, Proceedings of the National Academy of Sciences of the United States of America.

Molybdate permits resolution of untransformed glucocorticoid receptors from the transformed state.

W. Pratt, M. Dahmer, M. Quasney, 1981, The Journal of biological chemistry.

Localization of the 90-kDa heat shock protein-binding site within the hormone-binding domain of the glucocorticoid receptor by peptide competition.

H. Akil, W. Pratt, L. Taylor, 1991, The Journal of biological chemistry.

The relationship between glucocorticoid receptor binding to Hsp90 and receptor function.

S. Meshinchi, W. Pratt, F. C. Dalman, 1990, Nihon Naibunpi Gakkai zasshi.

Evidence for a phospholipid requirement in the specific binding of glucocorticoids to receptors of fibroblasts and thymic lymphocytes.

H. F. Schulte, W. Pratt, J. J. Sando, 1976, The Journal of biological chemistry.

Demonstration by confocal microscopy that unliganded overexpressed glucocorticoid receptors are distributed in a nonrandom manner throughout all planes of the nucleus.

V. Martins, W. Pratt, G. Ringold, 1991, Molecular endocrinology.

In contrast to the glucocorticoid receptor, the thyroid hormone receptor is translated in the DNA binding state and is not associated with hsp90.

W. Pratt, G. Perdew, R. Koenig, 1990, The Journal of biological chemistry.

Cisplatin Induces Bmi1 and Enhances the Stem Cell Fraction in Head and Neck Cancer

A. Chinnaiyan, D. Beer, Guoan Chen, 2015 .

Inhibition of Glucocorticoid Receptor Conversion to the DNA-Binding State and Inhibition of Subunit Dissociation

S. Meshinchi, E. Bresnick, W. Pratt, 1987 .

Energy-dependent conversion of transformed cytosolic glucocorticoid receptors from soluble to particulate-bound form.

W. Pratt, L. Scherrer, 1992, Biochemistry.

Nutritional status of orthopedic patients with surgical complications.

W. Pratt, J. Veitch, R. McRoberts, 1981, Clinical orthopaedics and related research.

The mechanism of glucocorticoid effects in fibroblasts.

W. Pratt, William B. Pratt, 1978, The Journal of investigative dermatology.

Localization of the ∼12 kDa Mr discrepancy in gel migration of the mouse glucocorticoid receptor to the major phosphorylated cyanogen bromide fragment in the transactivating domain

B. Groner, W. Pratt, K. Hutchison, 1993, The Journal of Steroid Biochemistry and Molecular Biology.

Direct stoichiometric evidence that the untransformed Mr 300,000, 9S, glucocorticoid receptor is a core unit derived from a larger heteromeric complex.

E. Bresnick, W. Pratt, F. C. Dalman, 1990, Biochemistry.

Speculations on the Role of the 90 kDa Heat Shock Protein in Glucocorticoid Receptor Transport and Function

M. Welsh, S. Meshinchi, E. Bresnick, 1989 .

The heat-stable cytosolic factor that promotes glucocorticoid receptor binding to DNA is neither thioredoxin nor ribonuclease.

A. Holmgren, J. Grippo, W. Pratt, 1987, Journal of steroid biochemistry.

Association of the transformed glucocorticoid receptor with a cytoskeletal protein complex

W. Pratt, L. Scherrer, 1992, The Journal of Steroid Biochemistry and Molecular Biology.

Elimination and reconstitution of the requirement for hormone in promoting temperature-dependent transformation of cytosolic glucocorticoid receptors to the DNA-binding state.

S. Meshinchi, W. Pratt, E. R. Sánchez, 1990, The Journal of biological chemistry.

A heat shock protein complex isolated from rabbit reticulocyte lysate can reconstitute a functional glucocorticoid receptor-Hsp90 complex.

W. Pratt, E. R. Sánchez, S. Randall, 1992, Biochemistry.

The Anticancer Drugs

W. Pratt, William B. Pratt, 1979 .

Chemotherapy of infection

W. Pratt, 1977 .

Fungemia secondary to gastrointestinal Mucor indicus infection.

W. Pratt, T. Solano, C. Aboltins, 2006, Clinical infectious diseases : an official publication of the Infectious Diseases Society of America.

Lack of effects of copper gluconate supplementation.

W. Pratt, J. Omdahl, J. Sorenson, 1985, The American journal of clinical nutrition.

CHAPTER 12 – Inactivation, Activation, and Stabilization of Glucocorticoid Receptors

J. Grippo, W. Pratt, M. Dahmer, 1984 .

EFFECTS OF MOLYBDATE AND ENDOGENOUS INHIBITORS ON

W. Pratt, M. Dahmer, P. R. Housley, 1984 .

Inactivation of glucocorticoid-binding capacity by protein phosphatases in the presence of molybdate and complete reactivation of dithiothreitol.

W. Pratt, M. Dahmer, P. R. Housley, 1982, The Journal of biological chemistry.

Reactivation of thymocyte glucocorticoid receptors in a cell-free system.

W. Pratt, J. J. Sando, C. Nielsen, 1977, The Journal of biological chemistry.

The kinetics of glucocorticoid binding to the soluble specific binding protein of mouse fibroblasts.

W. Pratt, J. Kaine, D. Pratt, 1975, The Journal of biological chemistry.

Phosphorylation of the glucocorticoid receptor

J. Grippo, W. Pratt, M. Dahmer, 1984 .

Phosphorylation of L-cell glucocorticoid receptors in immune complexes: evidence that the receptor is not a protein kinase.

W. Pratt, E. R. Sánchez, 1986, Biochemistry.

Targeting Hsp90/Hsp70-based protein quality control for treatment of adult onset neurodegenerative diseases.

J. Gestwicki, W. Pratt, A. Lieberman, 2015, Annual review of pharmacology and toxicology.

Activation of thymocyte glucocorticoid receptors to the steroid binding form. The roles of reduction agents, ATP, and heat-stable factors.

W. Pratt, J. J. Sando, N. Hammond, 1979, The Journal of biological chemistry.

hsp90 Is Required for Heme Binding and Activation of Apo-Neuronal Nitric-oxide Synthase

W. Pratt, A. Bender, K. C. Kanelakis, 2002, The Journal of Biological Chemistry.

The role of the hsp90-based chaperone system in signal transduction by nuclear receptors and receptors signaling via MAP kinase.

W. Pratt, 1997, Annual review of pharmacology and toxicology.

The Hsp90-Based Protein Trafficking System and Linkage to Protein Quality Control

W. Pratt, A. Lieberman, Y. Morishima, 2012 .

Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement.

D. DeFranco, M. Galigniana, W. Pratt, 2004, Cellular signalling.

The 56-59-kilodalton protein identified in untransformed steroid receptor complexes is a unique protein that exists in cytosol in a complex with both the 70- and 90-kilodalton heat shock proteins.

W. Pratt, E. R. Sánchez, W. Henzel, 1990, Biochemistry.

Evidence that the 90-kilodalton heat shock protein is associated with tubulin-containing complexes in L cell cytosol and in intact PtK cells.

M. Welsh, E. Bresnick, W. Pratt, 1988, Molecular endocrinology.

Evidence that the hormone binding domain of steroid receptors confers hormonal control on chimeric proteins by determining their hormone-regulated binding to heat-shock protein 90.

K. Yamamoto, J. Harmon, W. Pratt, 1993, Biochemistry.

Evidence for a Mechanism of Repression of Heat Shock Factor 1 Transcriptional Activity by a Multichaperone Complex*

W. Pratt, D. Toft, R. Voellmy, 2001, The Journal of Biological Chemistry.

Destabilization of the Epidermal Growth Factor Receptor (EGFR) by a Peptide That Inhibits EGFR Binding to Heat Shock Protein 90 and Receptor Dimerization*♦

A. Rehemtulla, T. Lawrence, D. Ray, 2013, The Journal of Biological Chemistry.

Regulation of the Polyglutamine Androgen Receptor by the Hsp90/Hsp70-Based Chaperone Machinery

W. Pratt, A. Lieberman, 2011 .

Inhibition of Hsp70 by Methylene Blue Affects Signaling Protein Function and Ubiquitination and Modulates Polyglutamine Protein Degradation*

Jason E Gestwicki, J. Gestwicki, W. Pratt, 2010, The Journal of Biological Chemistry.

Proposal for a role of the Hsp90/Hsp70-based chaperone machinery in making triage decisions when proteins undergo oxidative and toxic damage

W. Pratt, Y. Morishima, Hwei-Ming Peng, 2010, Experimental biology and medicine.

Pharmacologic and genetic inhibition of hsp90-dependent trafficking reduces aggregation and promotes degradation of the expanded glutamine androgen receptor without stress protein induction.

W. Pratt, A. Lieberman, Monzy Thomas, 2006, Human molecular genetics.

The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor.

W. Pratt, 1993, The Journal of biological chemistry.

Hsp90-binding Immunophilins Link p53 to Dynein During p53 Transport to the Nucleus*

M. Ljungman, M. Galigniana, W. Pratt, 2004, Journal of Biological Chemistry.

Differential Effects of the hsp70-binding Protein BAG-1 on Glucocorticoid Receptor Folding by the hsp90-based Chaperone Machinery*

John Calvin Reed, S. Takayama, M. Galigniana, 1999, The Journal of Biological Chemistry.

The Hsp90 Chaperone Machinery Regulates Signaling by Modulating Ligand Binding Clefts*

W. Pratt, Y. Morishima, Y. Osawa, 2008, Journal of Biological Chemistry.

Chaperone functions of the heat shock proteins associated with steroid receptors.

M. Welsh, W. Pratt, M. J. Welsh, 1994, Seminars in cell biology.

Specific binding of glucocorticoids in vitro in the soluble fraction of mouse fibroblasts.

W. Pratt, D. Ishii, 1972, Biochemistry.

Steady-state level of the specific glucocorticoid binding component in mouse fibroblasts.

W. Pratt, D. Ishii, L. Aronow, 1972, Biochemistry.

Characterization and partial purification of the specific glucocorticoid-binding component from mouse fibroblasts.

W. Pratt, J. Hackney, 1971, Biochemistry.

Molecular chaperoning of steroid hormone receptors.

W. Pratt, D. Toft, U. Gehring, 1996, EXS.

Targeting Hsp70 facilitated protein quality control for treatment of polyglutamine diseases

W. Pratt, A. Lieberman, Amanda K. Davis, 2019, Cellular and Molecular Life Sciences.

Efficacy of an EGFR-specific peptide against EGFR-dependent cancer cell lines and tumor xenografts.

A. Rehemtulla, T. Lawrence, D. Ray, 2014, Neoplasia.

Low-Dose Hsp90 Inhibitor Selectively Radiosensitizes HNSCC and Pancreatic Xenografts

Dafydd G. Thomas, M. Schipper, T. Lawrence, 2020, Clinical Cancer Research.

The Hsp90 Chaperone Machinery Acts at Protein Folding Clefts to Regulate Both Signaling Protein Function and Protein Quality Control

W. Pratt, Y. Morishima, Y. Osawa, 2007 .

A region in the steroid binding domain determines formation of the non-DNA-binding, 9 S glucocorticoid receptor complex.

R. Evans, E. Baulieu, V. Giguère, 1988, The Journal of biological chemistry.

A model in which heat shock protein 90 targets protein-folding clefts: Rationale for a new approach to neuroprotective treatment of protein folding diseases

J. Gestwicki, W. Pratt, A. Lieberman, 2014, Experimental biology and medicine.

neuroprotective treatment of protein folding diseases A model in which heat shock protein 90 targets protein-folding clefts : Rationale for a new approach to

J. Gestwicki, W. Pratt, A. Lieberman, 2014 .

Modulation of Heme/Substrate Binding Cleft of Neuronal Nitric-oxide Synthase (nNOS) Regulates Binding of Hsp90 and Hsp70 Proteins and nNOS Ubiquitination*

W. Pratt, Y. Morishima, Hwei-Ming Peng, 2011, The Journal of Biological Chemistry.

C331A Mutant of Neuronal Nitric-oxide Synthase Is Labilized for Hsp70/CHIP (C Terminus of HSC70-interacting Protein)-dependent Ubiquitination*

W. Pratt, Y. Morishima, Hwei-Ming Peng, 2010, The Journal of Biological Chemistry.

Dynamic cycling with Hsp90 stabilizes neuronal nitric oxide synthase through calmodulin-dependent inhibition of ubiquitination.

W. Pratt, Y. Morishima, Hwei-Ming Peng, 2009, Biochemistry.

Pifithrin-α Inhibits p53 Signaling after Interaction of the Tumor Suppressor Protein with hsp90 and Its Nuclear Translocation*

M. Ljungman, M. Galigniana, W. Pratt, 2004, Journal of Biological Chemistry.

Differential effects of the reversible thiol-reactive agents arsenite and methyl methanethiosulfonate on steroid binding by the glucocorticoid receptor.

W. Pratt, L. Stancato, K. Hutchison, 1993, Biochemistry.

Hepatic glucocorticoid receptors and the H–2 locus

R. Erickson, W. Pratt, MARTIN S. BUTLEY, 1978, Nature.

Regulation of cytochrome P450 2E1 by heat shock protein 90-dependent stabilization and CHIP-dependent proteasomal degradation.

R. Sunahara, W. Pratt, P. Hollenberg, 2005, Biochemistry.

Preassociation of STAT1 with STAT2 and STAT3 in Separate Signalling Complexes Prior to Cytokine Stimulation (*)

M. David, C. Carter-Su, W. Pratt, 1996, The Journal of Biological Chemistry.

Activation of Hsp70 reduces neurotoxicity by promoting polyglutamine protein degradation

Catherine A. Collins, T. Komiyama, J. Gestwicki, 2012, Nature chemical biology.

Spondylolysis and associated spondylolisthesis in Eskimo and Athabascan populations.

S. S. Tower, W. Pratt, 1990, Clinical orthopaedics and related research.

Laboratory testing of bolts and screws in cancellous bone.

W. Pratt, S. Yazdani, 1989, Orthopaedic review.

Evidence that the endogenous heat-stable glucocorticoid receptor-activating factor is thioredoxin.

J. Grippo, W. Pratt, M. Dahmer, 1983, The Journal of biological chemistry.

Murine glucocorticoid receptors and the H-2 locus--a reappraisal.

J. Grippo, R. Erickson, W. Pratt, 1984, Journal of steroid biochemistry.

The Antimicrobial Drugs

W. Pratt, F. Fekety, William B. Pratt, 1986 .

Nucleic acid synthesis in intact nuclei isolated from mouse fibroblasts. Characterization of the system and effects of glucocorticoids.

B. Kemper, W. Pratt, L. Aronow, 1969, Molecular pharmacology.

Untreated acetabular dysplasia of the hip in the Navajo. A 34 year case series followup.

W. Pratt, R. Schwend, J. Fultz, 1999, Clinical orthopaedics and related research.

Treatment of back pain with copper supplementation

W. Pratt, J. Omdahl, J. Sorenson, 1985 .

Untreated Congenital Hip Dysplasia

W. Pratt, R. Freiberger, 2006 .

Untreated congenital hip dysplasia in the Navajo.

W. Pratt, R. Freiberger, W. D. Arnold, 1982, Clinical orthopaedics and related research.

The endogenous heat-stable glucocorticoid receptor stabilizing factor and the H-2 locus.

R. Erickson, K. Leach, W. Pratt, 1982, Journal of steroid biochemistry.

Hallucinogens and Drosophila: linking serotonin receptor activation to behavior

J. Ronesi, W. Pratt, C. Nichols, 2002, Neuroscience.

Evidence that the conserved region in the steroid binding domain of the glucocorticoid receptor is required for both optimal binding of hsp90 and protection from proteolytic cleavage. A two-site model for hsp90 binding to the steroid binding domain.

W. Pratt, G. Ringold, M. Danielsen, 1990, The Journal of biological chemistry.

Retinoic acid receptor belongs to a subclass of nuclear receptors that do not form "docking" complexes with hsp90.

P. Chambon, J. Grippo, W. Pratt, 1991, Biochemistry.

The role of sulfhydryl groups in permitting transformation and DNA binding of the glucocorticoid receptor.

S. Meshinchi, A. Holmgren, J. Grippo, 1987, The Journal of biological chemistry.

The Functional Relevance of the Heteromeric Structure of Corticosteroid Receptors a

H. Akil, S. Watson, W. Pratt, 1994, Annals of the New York Academy of Sciences.

The molybdate-stabilized L-cell glucocorticoid receptor isolated by affinity chromatography or with a monoclonal antibody is associated with a 90-92-kDa nonsteroid-binding phosphoprotein.

M. Beato, W. Pratt, E. R. Sánchez, 1985, The Journal of biological chemistry.

Targeting Hsp70 facilitated protein quality control for treatment of polyglutamine diseases

W. Pratt, A. Lieberman, Amanda K. Davis, 2019, Cellular and Molecular Life Sciences.

Independent Functions of hsp90 in Neurotransmitter Release and in the Continuous Synaptic Cycling of AMPA Receptors

Michael Chinkers, W. Pratt, J. Esteban, 2004, The Journal of Neuroscience.

Neuronal Nitric-oxide Synthase Is Regulated by the hsp90-based Chaperone System in Vivo *

A. Silverstein, W. Pratt, A. Bender, 1999, The Journal of Biological Chemistry.

Dynamic cycling with a unique Hsp90/Hsp70-dependent chaperone machinery and GAPDH is needed for heme insertion and activation of neuronal NO synthase

W. Pratt, Y. Morishima, Y. Osawa, 2022, The Journal of biological chemistry.

Purification of the endogenous glucocorticoid receptor stabilizing factor.

S. Meshinchi, W. Pratt, L. Stancato, 1991, Biochemistry.

Glucocorticoid receptor stabilization: relative effects of molybdate ion on inactivation by alkaline phosphatase and phospholipase A2.

K. Leach, W. Pratt, M. Dahmer, 1983, Journal of steroid biochemistry.

Androgen Receptor Acetylation Site Mutations Cause Trafficking Defects, Misfolding, and Aggregation Similar to Expanded Glutamine Tracts*

Abhishek Aphale, Jennifer M Harrell, W. Pratt, 2004, Journal of Biological Chemistry.

A Conserved Proline in the hsp90 Binding Region of the Glucocorticoid Receptor Is Required for hsp90 Heterocomplex Stabilization and Receptor Signaling*

H. Akil, W. Pratt, F. C. Dalman, 1998, The Journal of Biological Chemistry.

Relationship between glucocorticoid receptor steroid-binding capacity and association of the Mr 90,000 heat shock protein with the unliganded receptor.

E. Bresnick, W. Pratt, E. R. Sánchez, 1988, Journal of steroid biochemistry.

Effect of glucocorticoids on hexose uptake by mouse fibroblasts in vitro.

W. Pratt, L. Aronow, J. Gray, 1971, Biochemistry.

Characteristics of an endogenous glucocorticoid receptor stabilizing factor.

J. Grippo, K. Leach, W. Pratt, 1982, Journal of Biological Chemistry.

Evidence that removal of an endogenous metal that stabilizes the untransformed glucocorticoid receptor in cytosol allows ligand-independent receptor transformation.

S. Meshinchi, W. Pratt, 1989, Journal of steroid biochemistry.

Effects of glucocorticoids on nucleic acid synthesis in mouse lymphoma cells growing in vitro and on nuclei isolated from these cells.

B. Kemper, W. Pratt, L. Aronow, 1970, Biochemical pharmacology.

DNA-binding and non-DNA-binding forms of the transformed glucocorticoid receptor

W. Pratt, G. Matić, M. Czar, 1992, The Journal of Steroid Biochemistry and Molecular Biology.

Ability of various members of the hsp70 family of chaperones to promote assembly of the glucocorticoid receptor into a functional heterocomplex with hsp90

W. Pratt, L. Stancato, K. D. Dittmar, 1996, The Journal of Steroid Biochemistry and Molecular Biology.

Chaperone Activity and Dimerization Properties of Hsp90α and Hsp90β in Glucocorticoid Receptor Activation by the Multiprotein Hsp90/Hsp70-Dependent Chaperone Machinery

T. Lawrence, W. Pratt, M. Nyati, 2018, Molecular Pharmacology.

Small-Colony Variants of Staphylococcus aureus

W. Pratt, T. Solano, C. Aboltins, 2010 .

CHIP deletion reveals functional redundancy of E3 ligases in promoting degradation of both signaling proteins and expanded glutamine proteins.

Zhigang Yu, W. Pratt, A. Lieberman, 2008, Human molecular genetics.

Glucocorticoid receptor structure and the initial events in signal transduction.

W. Pratt, 1990, Progress in clinical and biological research.

ArticleHDAC 6 Regulates Hsp 90 Acetylation and Chaperone-Dependent Activation of Glucocorticoid Receptor

C. Nicchitta, Xuan Zhao, T. Yao, 2005 .