J. Udgaonkar

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Structural effects of multiple pathogenic mutations suggest a model for the initiation of misfolding of the prion protein.

Jogender Singh, J. Udgaonkar, 2015, Angewandte Chemie.

Rational stabilization of helix 2 of the prion protein prevents its misfolding and oligomerization.

Jogender Singh, J. Udgaonkar, H. Kumar, 2014, Journal of the American Chemical Society.

Discrepancies between the NMR and X-ray structures of uncomplexed barstar: analysis suggests that packing densities of protein structures determined by NMR are unreliable.

R. Varadarajan, J. Udgaonkar, G. Ratnaparkhi, 1998, Biochemistry.

Characterization of intra-molecular distances and site-specific dynamics in chemically unfolded barstar: evidence for denaturant-dependent non-random structure.

J. Udgaonkar, A. Saxena, G. Krishnamoorthy, 2006, Journal of molecular biology.

The slow folding reaction of barstar: the core tryptophan region attains tight packing before substantial secondary and tertiary structure formation and final compaction of the polypeptide chain.

J. Udgaonkar, G. Krishnamoorthy, K. Sridevi, 2000, Journal of molecular biology.

Dynamics of the core tryptophan during the formation of a productive molten globule intermediate of barstar.

J. Udgaonkar, G. Krishnamoorthy, B. R. Rami, 2003, Biochemistry.

Fluorescence anisotropy uncovers changes in protein packing with inclusion growth in a cellular model of polyglutamine aggregation.

J. Udgaonkar, V. Bhardwaj, M. Panicker, 2014, Biochemistry.

Mass spectrometry studies of protein folding

J. Udgaonkar, A. H. Wani, Ajazul H Wani, 2012 .

Synthesis, photochemistry, and biological activity of a caged photolabile acetylcholine receptor ligand.

W. Denk, W. Webb, J. Udgaonkar, 1989, Biochemistry.

Chemical kinetic measurements of transmembrane processes using rapid reaction techniques: acetylcholine receptor.

W. Olbricht, J. Udgaonkar, G. P. Hess, 1987, Annual review of biophysics and biophysical chemistry.

How cooperative are protein folding and unfolding transitions?

P. Malhotra, J. Udgaonkar, 2016, Protein science : a publication of the Protein Society.

Heterologous expression, purification and characterization of heterodimeric monellin.

J. Udgaonkar, Nilesh Aghera, 2011, Protein expression and purification.

Acetylcholine receptor: evidence for a voltage-dependent regulatory site for acetylcholine. Chemical kinetic measurements in membrane vesicles using a voltage clamp.

J. Udgaonkar, K. Takeyasu, G. P. Hess, 1983, Biochemistry.

Four-state folding of a SH3 domain: salt-induced modulation of the stabilities of the intermediates and native state.

J. Udgaonkar, Amrita Dasgupta, 2012, Biochemistry.

NMR identification and characterization of the flexible regions in the 160 kDa molten globule-like aggregate of barstar at low pH.

J. Udgaonkar, J. Juneja, R. Hosur, 2002, Biochemistry.

Native State Hydrogen Exchange-Mass Spectrometry Methods to Probe Protein Folding and Unfolding.

P. Malhotra, J. Udgaonkar, 2021, Methods in molecular biology.

A thermodynamic coupling mechanism can explain the GroEL-mediated acceleration of the folding of barstar.

J. Udgaonkar, N. Bhutani, 2000, Journal of molecular biology.

Stepwise Assembly of β-Sheet Structure during the Folding of an SH3 Domain Revealed by a Pulsed Hydrogen Exchange Mass Spectrometry Study.

J. Udgaonkar, Nilesh Aghera, 2017, Biochemistry.

Salt-Mediated Oligomerization of the Mouse Prion Protein Monitored by Real-Time NMR.

J. Udgaonkar, Ishita Sengupta, R. Das, 2017, Journal of molecular biology.

Observation of Continuous Contraction and a Metastable Misfolded State during the Collapse and Folding of a Small Protein.

J. Udgaonkar, D. Dhar, G. Krishnamoorthy, 2019, Journal of molecular biology.

Evolutionarily conserved proline residues impede the misfolding of the mouse prion protein by destabilizing an aggregation-competent partially unfolded form.

J. Udgaonkar, S. Pal, 2022, Journal of molecular biology.

How do proteins fold

J. Udgaonkar, U. Nath, 1997 .

Stopped‐flow NMR measurement of hydrogen exchange rates in reduced horse cytochrome c under strongly destabilizing conditions

J. Udgaonkar, A. Bhuyan, Jayant B. Udgaonkar, 1998, Proteins.

Nature of the early folding intermediate of ribonuclease A.

R. L. Baldwin, J. Udgaonkar, 1995, Biochemistry.

Characterization of the heterogeneity and specificity of interpolypeptide interactions in amyloid protofibrils by measurement of site-specific fluorescence anisotropy decay kinetics.

J. Udgaonkar, G. Krishnamoorthy, A. Jha, 2009, Journal of molecular biology.

The folding mechanism of barstar: evidence for multiple pathways and multiple intermediates.

J. Udgaonkar, M. Shastry, M.C.R. Shastry, 1995, Journal of molecular biology.

Acetylcholine receptor kinetics: Chemical kinetics

J. Udgaonkar, G. P. Hess, 2005, The Journal of Membrane Biology.

Folding and binding.

S. Marqusee, J. Udgaonkar, 2013, Current Opinion in Structural Biology.

Guanidine hydrochloride-induced reversible unfolding of sheep liver serine hydroxymethyltransferase

J. Udgaonkar, B. Venkatesha, H. Savithri, 1999, Journal of Biosciences.

Identification of intermediate species in protein-folding by quantitative analysis of amplitudes in time-domain fluorescence spectroscopy

J. Udgaonkar, A. Saxena, G. Krishnamoorthy, 2007 .

Equilibrium unfolding studies of barstar: evidence for an alternative conformation which resembles a molten globule.

J. Udgaonkar, R. Khurana, 1994, Biochemistry.

Chemical kinetic measurements of a mammalian acetylcholine receptor by a fast-reaction technique.

J. Udgaonkar, G. P. Hess, Jayantb . Udgaonkar, 1987, Proceedings of the National Academy of Sciences of the United States of America.

Reduced fluorescence lifetime heterogeneity of 5-fluorotryptophan in comparison to tryptophan in proteins: implication for resonance energy transfer experiments.

J. Udgaonkar, G. Krishnamoorthy, Saswata S. Sarkar, 2011, The journal of physical chemistry. B.

Binding-induced folding under unfolding conditions: Switching between induced fit and conformational selection mechanisms

J. Udgaonkar, Sreemantee Sen, 2019, The Journal of Biological Chemistry.

pH dependence of the stability of barstar to chemical and thermal denaturation

J. Udgaonkar, R. Khurana, U. Nath, 1995, Protein science : a publication of the Protein Society.

The Lys 280 → Gln mutation mimicking disease‐linked acetylation of Lys 280 in tau extends the structural core of fibrils and modulates their catalytic properties

J. Udgaonkar, H. Kumar, 2021, Protein science : a publication of the Protein Society.

Mechanistic approaches to understand the prion-like propagation of aggregates of the human tau protein.

J. Udgaonkar, H. Kumar, 2019, Biochimica et biophysica acta. Proteins and proteomics.

Regulatory properties of acetylcholine receptor: evidence for two different inhibitory sites, one for acetylcholine and the other for a noncompetitive inhibitor of receptor function (procaine).

J. Udgaonkar, A. Delcour, K. Takeyasu, 1984, Biochemistry.

Acetylcholine receptor: evidence for a regulatory binding site in investigations of suberyldicholine-induced transmembrane ion flux in Electrophorus electricus membrane vesicles.

J. Udgaonkar, E. Pasquale, K. Takeyasu, 1983, Biochemistry.

Isosteric regulation of the acetylcholine receptor

J. Udgaonkar, G. P. Hess, 1987 .

Mechanistic studies unravel the complexity inherent in tau aggregation leading to Alzheimer's disease and the tauopathies.

J. Udgaonkar, G. Ramachandran, 2013, Biochemistry.

Understanding the Kinetic Roles of the Inducer Heparin and of Rod-like Protofibrils during Amyloid Fibril Formation by Tau Protein*

J. Udgaonkar, G. Ramachandran, 2011, The Journal of Biological Chemistry.

Elongation of Fibrils Formed by a Tau Fragment is Inhibited by a Transient Dimeric Intermediate.

J. Udgaonkar, H. Kumar, 2022, The journal of physical chemistry. B.

Prion protein aggregation

J. Udgaonkar, Shweta Jain, 2011 .

SecB-mediated protein export need not occur via kinetic partitioning.

R. Varadarajan, J. Udgaonkar, Beena Krishnan, 2009, Journal of molecular biology.

SecB binds only to a late native-like intermediate in the folding pathway of barstar and not to the unfolded state.

V. G. Panse, R. Varadarajan, J. Udgaonkar, 1998, Biochemistry.

Amino‐acid composition after loop deletion drives domain swapping

J. Udgaonkar, S. Gosavi, R. Das, 2017, Protein science : a publication of the Protein Society.

Effect of signal peptide on the stability and folding kinetics of maltose binding protein.

R. Varadarajan, J. Udgaonkar, K. Beena, 2004, Biochemistry.

Thermodynamic characterization of the unfolding of the prion protein.

J. Udgaonkar, R. Moulick, 2014, Biophysical journal.

Salt-induced modulation of the pathway of amyloid fibril formation by the mouse prion protein.

J. Udgaonkar, Shweta Jain, 2010, Biochemistry.

Mechanisms of amyloid fibril formation by proteins

J. Udgaonkar, Santosh Kumar, 2010 .

Structurally distinct amyloid protofibrils form on separate pathways of aggregation of a small protein.

J. Udgaonkar, Santosh Kumar, 2009, Biochemistry.

Conformational conversion may precede or follow aggregate elongation on alternative pathways of amyloid protofibril formation.

J. Udgaonkar, Santosh Kumar, 2009, Journal of molecular biology.

StructurallyDistinctAmyloidProtofibrilsFormonSeparatePathwaysofAggregationofa Small Protein

J. Udgaonkar, Santosh Kumar, 2009 .

GroEL channels the folding of thioredoxin along one kinetic route.

J. Udgaonkar, N. Bhutani, 2001, Journal of molecular biology.

Heterogeneity in Protein Folding and Unfolding Reactions.

J. Udgaonkar, Sandhya Bhatia, 2022, Chemical reviews.

NMR evidence for an early framework intermediate on the folding pathway of ribonuclease A

Robert L. Baldwin, R. L. Baldwin, J. Udgaonkar, 1988, Nature.

Characterization of deamidation of barstar using electrospray ionization quadrupole time‐of‐flight mass spectrometry, which stabilizes an equilibrium unfolding intermediate

J. Udgaonkar, S. Jha, P. D. Deepalakshmi, 2012, Protein science : a publication of the Protein Society.

Structural mechanisms of oligomer and amyloid fibril formation by the prion protein.

J. Udgaonkar, Ishita Sengupta, 2018, Chemical communications.

Unraveling the Molecular Mechanism of pH-Induced Misfolding and Oligomerization of the Prion Protein.

Jogender Singh, J. Udgaonkar, 2016, Journal of molecular biology.

Development of the structural core and of conformational heterogeneity during the conversion of oligomers of the mouse prion protein to worm-like amyloid fibrils.

Jogender Singh, J. Udgaonkar, A. T. Sabareesan, 2012, Journal of molecular biology.

Identification and Structural Characterization of the Precursor Conformation of the Prion Protein which Directly Initiates Misfolding and Oligomerization.

J. Udgaonkar, R. Moulick, 2017, Journal of molecular biology.

Partially Unfolded Forms of the Prion Protein Populated under Misfolding-promoting Conditions

J. Udgaonkar, R. Das, R. Moulick, 2015, The Journal of Biological Chemistry.

Evidence for stepwise formation of amyloid fibrils by the mouse prion protein.

J. Udgaonkar, Shweta Jain, 2008, Journal of molecular biology.

Molecular Mechanism of the Misfolding and Oligomerization of the Prion Protein: Current Understanding and Its Implications.

Jogender Singh, J. Udgaonkar, 2015, Biochemistry.

Mechanism of aggregation and membrane interactions of mammalian prion protein.

J. Udgaonkar, M. Mathew, Sabareesan Ambadi Thody, 2018, Biochimica et biophysica acta. Biomembranes.

Backbone dynamics of barstar: A 15N NMR relaxation study

J. Udgaonkar, A. Bhuyan, S. Sahu, 2000, Proteins.

Backbone dynamics of free barnase and its complex with barstar determined by 15N NMR relaxation study

J. Udgaonkar, A. Bhuyan, S. Sahu, 2000, Journal of biomolecular NMR.

α-Synuclein aggregation intermediates form fibril polymorphs with distinct prion-like properties

J. Udgaonkar, H. Kumar, N. N. Jha, 2020, bioRxiv.

Monitoring site-specific conformational changes in real-time reveals a misfolding mechanism of the prion protein

J. Udgaonkar, Ishita Sengupta, 2019, eLife.

Modulation of the extent of structural heterogeneity in α-synuclein fibrils by the small molecule thioflavin T

Jogender Singh, J. Udgaonkar, H. Kumar, 2017, The Journal of Biological Chemistry.

Thioflavin T modulates fibrillar heterogeneity

Jogender Singh, J. Udgaonkar, H. Kumar, 2017 .

Microsecond dynamics during the binding-induced folding of an intrinsically disordered protein.

J. Udgaonkar, H. Kumar, H. Kumar, 2021, Journal of molecular biology.

Defining the pathway of worm-like amyloid fibril formation by the mouse prion protein by delineation of the productive and unproductive oligomerization reactions.

J. Udgaonkar, Shweta Jain, 2011, Biochemistry.

A five-residue motif for the design of domain swapping in proteins

J. Udgaonkar, S. Gosavi, N. M. Mascarenhas, 2019, Nature Communications.

Reversible unfolding of sheep liver tetrameric serine hydroxymethyltransferase.

J. Udgaonkar, B. Venkatesha, H. Savithri, 1998, Biochimica et biophysica acta.

Effect of salt on the urea-unfolded form of barstar probed by m value measurements.

J. Udgaonkar, Lovy Pradeep, 2004, Biochemistry.

A buried ionizable residue destabilizes the native state and the transition state in the folding of monellin.

J. Udgaonkar, Nilesh Aghera, I. Dasgupta, 2012, Biochemistry.

Equilibrium unfolding studies of monellin: the double-chain variant appears to be more stable than the single-chain variant.

J. Udgaonkar, Nilesh Aghera, N. Earanna, 2011, Biochemistry.

Free energy barriers in protein folding and unfolding reactions

J. Udgaonkar, S. Jha, 2010 .

Direct evidence for a dry molten globule intermediate during the unfolding of a small protein

J. Udgaonkar, S. Jha, 2009, Proceedings of the National Academy of Sciences.

Folding of horse cytochrome c in the reduced state.

J. Udgaonkar, A. Bhuyan, 2001, Journal of molecular biology.

Protein dynamics control proton transfer from bulk solvent to protein interior: A case study with a green fluorescent protein

J. Udgaonkar, A. Saxena, G. Krishnamoorthy, 2005, Protein science : a publication of the Protein Society.

Kinetics of proton transfer in a green fluorescent protein: A laser-induced pH jump study

J. Udgaonkar, G. Krishnamoorthy, R. Mallik, 2003 .

Molecular crowding causes narrowing of population heterogeneity and restricts internal dynamics in a protein

J. Udgaonkar, G. Krishnamoorthy, Samsuzzoha Mondal, 2015 .

The Osmolyte TMAO Modulates Protein Folding Cooperativity by Altering Global Protein Stability.

J. Udgaonkar, Prashant N. Jethva, 2018, Biochemistry.

Modulation of the Extent of Cooperative Structural Change During Protein Folding by Chemical Denaturant.

J. Udgaonkar, Prashant N. Jethva, 2017, The journal of physical chemistry. B.

Native state dynamics drive the unfolding of the SH3 domain of PI3 kinase at high denaturant concentration

J. Udgaonkar, Ajazul H Wani, 2009, Proceedings of the National Academy of Sciences.

Critical evaluation of the two-state model describing the equilibrium unfolding of the PI3K SH3 domain by time-resolved fluorescence resonance energy transfer.

J. Udgaonkar, G. Krishnamoorthy, Megha Kishore, 2013, Biochemistry.

Continuous dissolution of structure during the unfolding of a small protein

J. Udgaonkar, D. Dhar, G. Krishnamoorthy, 2009, Proceedings of the National Academy of Sciences.

Structure is lost incrementally during the unfolding of barstar

G. Krishnamoorthy, J. Udgaonkar, G. Krishnamoorthy, 2001, Nature Structural Biology.

Motional dynamics of a buried tryptophan reveals the presence of partially structured forms during denaturation of barstar.

J. Udgaonkar, G. Krishnamoorthy, R. Swaminathan, 1996, Biochemistry.

Mechanistic and Structural Origins of the Asymmetric Barrier to Prion-like Cross-Seeding between Tau-3R and Tau-4R.

J. Udgaonkar, H. Kumar, 2018, Journal of molecular biology.

Amyloid fibril formation by the chain B subunit of monellin occurs by a nucleation-dependent polymerization mechanism.

J. Udgaonkar, A. T. Sabareesan, 2014, Biochemistry.

Evidence for the existence of a secondary pathway for fibril growth during the aggregation of tau.

J. Udgaonkar, G. Ramachandran, 2012, Journal of molecular biology.

Fluoroalcohol-induced modulation of the pathway of amyloid protofibril formation by barstar.

J. Udgaonkar, A. Sekhar, 2011, Biochemistry.

Barrierless evolution of structure during the submillisecond refolding reaction of a small protein

J. Udgaonkar, K. K. Sinha, 2008, Proceedings of the National Academy of Sciences.

Early folding intermediate of ribonuclease A.

R. L. Baldwin, J. Udgaonkar, R L Baldwin, 1990, Proceedings of the National Academy of Sciences of the United States of America.

GroEL can unfold late intermediates populated on the folding pathways of monellin.

J. Udgaonkar, Ashish K Patra, 2009, Journal of molecular biology.

Characterization of the formation of amyloid protofibrils from barstar by mapping residue-specific fluorescence dynamics.

J. Udgaonkar, G. Krishnamoorthy, S. Mukhopadhyay, 2006, Journal of molecular biology.

Revealing a concealed intermediate that forms after the rate-limiting step of refolding of the SH3 domain of PI3 kinase.

J. Udgaonkar, Ajazul H Wani, 2009, Journal of molecular biology.

Rise of the Helix from a Collapsed Globule during the Folding of Monellin.

J. Udgaonkar, R. R. Goluguri, 2015, Biochemistry.

Multistage unfolding of an SH3 domain: an initial urea-filled dry molten globule precedes a wet molten globule with non-native structure.

J. Udgaonkar, Amrita Dasgupta, Payel Das, 2014, The journal of physical chemistry. B.

Polypeptide chain collapse and protein folding.

Jayant B Udgaonkar, J. Udgaonkar, 2013, Archives of biochemistry and biophysics.

Transient non-native burial of a Trp residue occurs initially during the unfolding of a SH3 domain.

J. Udgaonkar, Amrita Dasgupta, 2012, Biochemistry.

Evidence for initial non-specific polypeptide chain collapse during the refolding of the SH3 domain of PI3 kinase.

J. Udgaonkar, Amrita Dasgupta, 2010, Journal of molecular biology.

Early events in protein folding

J. Udgaonkar, K. K. Sinha, 2009 .

Native and nonnative conformational preferences in the urea‐unfolded state of barstar

J. Udgaonkar, J. Juneja, R. Hosur, 2004, Protein science : a publication of the Protein Society.

Folding subdomains of thioredoxin characterized by native‐state hydrogen exchange

J. Udgaonkar, N. Bhutani, 2003, Protein science : a publication of the Protein Society.

Thermodynamics of denaturation of barstar: evidence for cold denaturation and evaluation of the interaction with guanidine hydrochloride.

J. Udgaonkar, V. R. Agashe, 1995, Biochemistry.

Multiple routes and structural heterogeneity in protein folding.

Jayant B Udgaonkar, J. Udgaonkar, 2008, Annual review of biophysics.

Resonance Raman spectroscopic measurements delineate the structural changes that occur during tau fibril formation.

Jayant B Udgaonkar, J. Udgaonkar, Gayathri Ramachandran, 2014, Biochemistry.

Exploration of the correlation between solvation dynamics and internal dynamics of a protein.

J. Udgaonkar, G. Krishnamoorthy, T. Tahara, 2011, Biochemistry.

Chemical Denaturants Smoothen Ruggedness on the Free Energy Landscape of Protein Folding.

P. Malhotra, J. Udgaonkar, Prashant N. Jethva, 2017, Biochemistry.

Secondary Structural Change Can Occur Diffusely and Not Modularly during Protein Folding and Unfolding Reactions.

P. Malhotra, J. Udgaonkar, 2016, Journal of the American Chemical Society.

Tuning Cooperativity on the Free Energy Landscape of Protein Folding.

P. Malhotra, J. Udgaonkar, 2015, Biochemistry.

Protein Folding, Unfolding, and Aggregation Processes Revealed by Rapid Sampling of Time-Domain Fluorescence

J. Udgaonkar, A. Saxena, G. Krishnamoorthy, 2011 .

High-energy intermediates in protein unfolding characterized by thiol labeling under nativelike conditions.

P. Malhotra, J. Udgaonkar, 2014, Biochemistry.

Destabilization of polar interactions in the prion protein triggers misfolding and oligomerization

J. Udgaonkar, R. Das, Suhas H Bhate, 2021, Protein science : a publication of the Protein Society.

Initial hydrophobic collapse in the folding of barstar

J. Udgaonkar, V. R. Agashe, M. Shastry, 1995, Nature.

Molten Globule-like Conformation of Barstar: A Study by Fluorescence Dynamics

J. Udgaonkar, G. Krishnamoorthy, R. Swaminathan, 1994 .

pH-jump-induced folding and unfolding studies of barstar: evidence for multiple folding and unfolding pathways.

J. Udgaonkar, B. R. Rami, 2001, Biochemistry.

Protein Dynamics and Protein Folding Dynamics Revealed by Time-Resolved Fluorescence

Guruswamy Krishnamoorthy, J. Udgaonkar, A. Saxena, 2005 .

Resolving Site-Specific Heterogeneity of the Unfolded State under Folding Conditions.

J. Udgaonkar, G. Krishnamoorthy, Sandhya Bhatia, 2021, The journal of physical chemistry letters.

Solvent-induced tuning of internal structure in a protein amyloid protofibril.

J. Udgaonkar, G. Krishnamoorthy, S. Narayan, 2012, Biophysical journal.

Diffusional barrier in the unfolding of a small protein.

J. Udgaonkar, Lovy Pradeep, 2007, Journal of molecular biology.

Thermodynamics of the complex protein unfolding reaction of barstar.

J. Udgaonkar, F. Schmid, V. R. Agashe, 1997, Biochemistry.

Folding of tryptophan mutants of barstar: evidence for an initial hydrophobic collapse on the folding pathway.

J. Udgaonkar, U. Nath, 1997, Biochemistry.

Initial loss of secondary structure in the unfolding of barstar

J. Udgaonkar, V. R. Agashe, U. Nath, 1996, Nature Structural Biology.

Crystallization and molecular packing analysis of barstar crystals.

J. Udgaonkar, D. Salunke, V. Gupta, 1994, Journal of Molecular Biology.

Quantitative analysis of the kinetics of denaturation and renaturation of barstar in the folding transition zone

J. Udgaonkar, V. R. Agashe, M. Shastry, 1994, Protein science : a publication of the Protein Society.

Pathogenic Mutations within the Disordered Palindromic Region of the Prion Protein Induce Structure Therein and Accelerate the Formation of Misfolded Oligomers.

J. Udgaonkar, A. T. Sabareesan, 2016, Journal of molecular biology.

Unfolding of a small protein proceeds via dry and wet globules and a solvated transition state.

Guruswamy Krishnamoorthy, Jayant B Udgaonkar, J. Udgaonkar, 2013, Biophysical journal.

The utilization of competing unfolding pathways of monellin is dictated by enthalpic barriers.

J. Udgaonkar, Nilesh Aghera, 2013, Biochemistry.

Differential salt-induced stabilization of structure in the initial folding intermediate ensemble of barstar.

J. Udgaonkar, Lovy Pradeep, 2002, Journal of molecular biology.

Multiple intermediates and transition states during protein unfolding

J. Udgaonkar, Jayant B. Udgaonkar, Faisal N. Zaidi, 1997, Nature Structural Biology.

Four-state folding of a SH3 domain: salt-induced modulation of the stabilities of the intermediates and native state.

J. Udgaonkar, Amrita Dasgupta, 2012, Biochemistry.

Difference in fibril core stability between two tau four-repeat domain proteins: a hydrogen-deuterium exchange coupled to mass spectrometry study.

J. Udgaonkar, G. Ramachandran, 2013, Biochemistry.

Osmolytes Induce Structure in an Early Intermediate on the Folding Pathway of Barstar*

J. Udgaonkar, Lovy Pradeep, 2004, Journal of Biological Chemistry.

Identification of multiple folding pathways of monellin using pulsed thiol labeling and mass spectrometry.

P. Malhotra, J. Udgaonkar, Amrita Dasgupta, 2011, Biochemistry.

Measurements of cysteine reactivity during protein unfolding suggest the presence of competing pathways.

J. Udgaonkar, S. Ramachandran, B. R. Rami, 2000, Journal of molecular biology.

Acetylcholine receptor: characterization of the voltage-dependent regulatory (inhibitory) site for acetylcholine in membrane vesicles from Torpedo californica electroplax.

J. Udgaonkar, K. Takeyasu, G. P. Hess, 1986, Biochemistry.

Dissection of conformational conversion events during prion amyloid fibril formation using hydrogen exchange and mass spectrometry.

Jogender Singh, J. Udgaonkar, 2013, Journal of molecular biology.

Kinetic studies of the folding of heterodimeric monellin: evidence for switching between alternative parallel pathways.

J. Udgaonkar, Nilesh Aghera, 2012, Journal of molecular biology.

Mechanism of formation of a productive molten globule form of barstar.

J. Udgaonkar, B. R. Rami, 2002, Biochemistry.

Two structural subdomains of barstar detected by rapid mixing NMR measurement of amide hydrogen exchange

J. Udgaonkar, A. Bhuyan, J B Udgaonkar, 1998, Proteins.

Stabilization of barstar by chemical modification of the buried cysteines.

J. Udgaonkar, S. Ramachandran, 1996, Biochemistry.

Microsecond Rearrangements of Hydrophobic Clusters in an Initially Collapsed Globule Prime Structure Formation during the Folding of a Small Protein.

J. Udgaonkar, R. R. Goluguri, 2016, Journal of molecular biology.

Characterization of the folding and unfolding reactions of single-chain monellin: evidence for multiple intermediates and competing pathways.

J. Udgaonkar, Ashish K Patra, 2007, Biochemistry.

Dissecting the non-specific and specific components of the initial folding reaction of barstar by multi-site FRET measurements.

J. Udgaonkar, K. K. Sinha, 2007, Journal of molecular biology.

Increasing stability reduces conformational heterogeneity in a protein folding intermediate ensemble.

Jayant B Udgaonkar, J. Udgaonkar, G. Krishnamoorthy, 2004, Journal of molecular biology.

Mechanism of formation of amyloid protofibrils of barstar from soluble oligomers: evidence for multiple steps and lateral association coupled to conformational conversion.

J. Udgaonkar, Subhendu K. Mohanty, Santosh Kumar, 2007, Journal of molecular biology.

Ruggedness in the Free Energy Landscape Dictates Misfolding of the Prion Protein.

J. Udgaonkar, R. Moulick, R. R. Goluguri, 2019, Journal of molecular biology.

Microsecond sub-domain motions and the folding and misfolding of the mouse prion protein

J. Udgaonkar, Sreemantee Sen, R. R. Goluguri, 2019, eLife.

Dependence of the size of the initially collapsed form during the refolding of barstar on denaturant concentration: evidence for a continuous transition.

J. Udgaonkar, K. K. Sinha, 2005, Journal of molecular biology.

A Dry Transition State More Compact Than the Native State Is Stabilized by Non-Native Interactions during the Unfolding of a Small Protein.

J. Udgaonkar, Sreemantee Sen, R. R. Goluguri, 2017, Biochemistry.

Expression and purification of single cysteine-containing mutant variants of the mouse prion protein by oxidative refolding.

J. Udgaonkar, Ishita Sengupta, 2017, Protein expression and purification.

Exploring the Cooperativity of the Fast Folding Reaction of a Small Protein Using Pulsed Thiol Labeling and Mass Spectrometry*

J. Udgaonkar, S. Jha, 2007, Journal of Biological Chemistry.

Unfolding rates of barstar determined in native and low denaturant conditions indicate the presence of intermediates.

J. Udgaonkar, K. Sridevi, 2002, Biochemistry.

Monitoring site-specific conformational changes in real-time reveals a misfolding mechanism of the prion protein

J. Udgaonkar, Ishita Sengupta, 2019, eLife.

The G126V Mutation in the Mouse Prion Protein Hinders Nucleation-Dependent Fibril Formation by Slowing Initial Fibril Growth and by Increasing the Critical Concentration.

J. Udgaonkar, A. T. Sabareesan, Ambadi Thody Sabareesan, 2017, Biochemistry.

The Pathogenic Mutation T182A Converts the Prion Protein into a Molten Globule-like Conformation Whose Misfolding to Oligomers but Not to Fibrils Is Drastically Accelerated.

Jogender Singh, J. Udgaonkar, 2016, Biochemistry.

A five-residue motif for the design of domain swapping in proteins

J. Udgaonkar, S. Gosavi, N. M. Mascarenhas, 2019, Nature Communications.

A designed domain swapped dimer

J. Udgaonkar, S. Gosavi, N. M. Mascarenhas, 2019 .

Differentiating between the sequence of structural events on alternative pathways of folding of a heterodimeric protein

J. Udgaonkar, Rupam Bhattacharjee, 2022, Protein science : a publication of the Protein Society.

Intricate packing in the hydrophobic core of barstar through a CH-π interaction

J. Udgaonkar, Sayantan Mondal, Mrinalini Puranik, 2014 .

HX-ESI-MS and optical studies of the unfolding of thioredoxin indicate stabilization of a partially unfolded, aggregation-competent intermediate at low pH.

J. Udgaonkar, Ajazul Hamid Wani, 2006, Biochemistry.

Observation of multistate kinetics during the slow folding and unfolding of barstar.

J. Udgaonkar, A. Bhuyan, 1999, Biochemistry.

Mechanism of aggregation and membrane interactions of mammalian prion protein.

J. Udgaonkar, M. Mathew, Sabareesan Ambadi Thody, 2018, Biochimica et biophysica acta. Biomembranes.

Fluoroalcohol-induced modulation of the pathway of amyloid protofibril formation by barstar.

J. Udgaonkar, A. Sekhar, 2011, Biochemistry.

Structural mechanisms of oligomer and amyloid fibril formation by the prion protein.

J. Udgaonkar, Ishita Sengupta, 2018, Chemical communications.

α-Synuclein aggregation intermediates form fibril polymorphs with distinct prion-like properties.

J. Udgaonkar, H. Kumar, N. N. Jha, 2022, Journal of molecular biology.

Salt-induced modulation of the pathway of amyloid fibril formation by the mouse prion protein.

J. Udgaonkar, Shweta Jain, 2010, Biochemistry.

Ruggedness in the Free Energy Landscape Dictates Misfolding of the Prion Protein.

J. Udgaonkar, R. Moulick, R. R. Goluguri, 2019, Journal of molecular biology.

Evidence for stepwise formation of amyloid fibrils by the mouse prion protein.

J. Udgaonkar, Shweta Jain, 2008, Journal of molecular biology.

Critical evaluation of the two-state model describing the equilibrium unfolding of the PI3K SH3 domain by time-resolved fluorescence resonance energy transfer.

J. Udgaonkar, Megha Kishore, Govindarajan Krishnamoorthy, 2013, Biochemistry.

Replacement of the Native cis Prolines by Alanine Simplifies the Complex Folding Mechanism of a Small Globular Protein by Eliminating both Fast and Slow phases of Folding.

J. Udgaonkar, Anushka Kaushik, 2023, Biophysical Journal.

Multiple kinetic intermediates accumulate during the unfolding of horse cytochrome c in the oxidized state.

J. Udgaonkar, A. Bhuyan, 1998, Biochemistry.

Protein folding: from theory to practice.

Govardhan Reddy, Edward P O'Brien, S. Marqusee, 2013, Current opinion in structural biology.

Equilibrium unfolding studies of monellin: the double-chain variant appears to be more stable than the single-chain variant.

J. Udgaonkar, Nilesh Aghera, N. Earanna, 2011, Biochemistry.

Dissection of conformational conversion events during prion amyloid fibril formation using hydrogen exchange and mass spectrometry.

Jogender Singh, J. Udgaonkar, 2013, Journal of molecular biology.

Resolving Site-Speci ﬁ c Heterogeneity of the Unfolded State under Folding Conditions

J. Udgaonkar, Sandhya Bhatia, Guruswamy Krishnamoorthy, 2022 .

Site-specific time-resolved FRET reveals local variations in the unfolding mechanism in an apparently two-state protein unfolding transition.

J. Udgaonkar, G. Krishnamoorthy, Sandhya Bhatia, 2018, Physical chemistry chemical physics : PCCP.

Acetylcholine receptor: channel-opening kinetics evaluated by rapid chemical kinetic and single-channel current measurements.

J. Udgaonkar, George P. Hess, 1987, Biophysical journal.

HDX-MS reveals concealed conformations of ISWI during different stages of nucleosome sliding

J. Udgaonkar, S. Amin, J. Bhat, 2023, bioRxiv.