| Year |
Citation |
Score |
| 2023 |
Bhatia S, Udgaonkar JB. Understanding the heterogeneity intrinsic to protein folding. Current Opinion in Structural Biology. 84: 102738. PMID 38041993 DOI: 10.1016/j.sbi.2023.102738 |
0.781 |
|
| 2023 |
Pal S, Udgaonkar JB. Mutations of evolutionarily conserved aromatic residues suggest that misfolding of the mouse prion protein may commence in multiple ways. Journal of Neurochemistry. PMID 37941487 DOI: 10.1111/jnc.16007 |
0.336 |
|
| 2022 |
Bhattacharjee R, Udgaonkar JB. Differentiating between the sequence of structural events on alternative pathways of folding of a heterodimeric protein. Protein Science : a Publication of the Protein Society. 31: e4513. PMID 36382901 DOI: 10.1002/pro.4513 |
0.364 |
|
| 2022 |
Pal S, Udgaonkar JB. Evolutionarily Conserved Proline Residues Impede the Misfolding of the Mouse Prion Protein by Destabilizing an Aggregation-competent Partially Unfolded Form. Journal of Molecular Biology. 434: 167854. PMID 36228749 DOI: 10.1016/j.jmb.2022.167854 |
0.367 |
|
| 2022 |
Bhatia S, Udgaonkar JB. Heterogeneity in Protein Folding and Unfolding Reactions. Chemical Reviews. PMID 35275612 DOI: 10.1021/acs.chemrev.1c00704 |
0.804 |
|
| 2022 |
Malhotra P, Udgaonkar JB. Native State Hydrogen Exchange-Mass Spectrometry Methods to Probe Protein Folding and Unfolding. Methods in Molecular Biology (Clifton, N.J.). 2376: 143-159. PMID 34845608 DOI: 10.1007/978-1-0716-1716-8_8 |
0.315 |
|
| 2021 |
Bhattacharjee R, Udgaonkar JB. Structural Characterization of the Cooperativity of Unfolding of a Heterodimeric Protein using Hydrogen Exchange-Mass Spectrometry. Journal of Molecular Biology. 433: 167268. PMID 34563547 DOI: 10.1016/j.jmb.2021.167268 |
0.356 |
|
| 2021 |
Sen S, Kumar H, Udgaonkar JB. Microsecond dynamics during the binding-induced folding of an intrinsically disordered protein. Journal of Molecular Biology. 167254. PMID 34537237 DOI: 10.1016/j.jmb.2021.167254 |
0.319 |
|
| 2021 |
Bhatia S, Krishnamoorthy G, Udgaonkar JB. Resolving Site-Specific Heterogeneity of the Unfolded State under Folding Conditions. The Journal of Physical Chemistry Letters. 3295-3302. PMID 33764778 DOI: 10.1021/acs.jpclett.1c00098 |
0.791 |
|
| 2021 |
Bhatia S, Krishnamoorthy G, Udgaonkar JB. Mapping Distinct Sequences of Structure Formation Differentiating Multiple Folding Pathways of a Small Protein. Journal of the American Chemical Society. PMID 33430589 DOI: 10.1021/jacs.0c11097 |
0.782 |
|
| 2019 |
Bhatia S, Krishnamoorthy G, Dhar D, Udgaonkar JB. Observation of Continuous Contraction and a Metastable Misfolded State during the Collapse and Folding of a Small Protein. Journal of Molecular Biology. PMID 31330152 DOI: 10.1016/j.jmb.2019.07.024 |
0.796 |
|
| 2019 |
Sengupta I, Udgaonkar J. Monitoring site-specific conformational changes in real-time reveals a misfolding mechanism of the prion protein. Elife. 8. PMID 31232689 DOI: 10.7554/Elife.44698 |
0.604 |
|
| 2019 |
Goluguri RR, Sen S, Udgaonkar J. Microsecond sub-domain motions and the folding and misfolding of the mouse prion protein. Elife. 8. PMID 31025940 DOI: 10.7554/Elife.44766 |
0.491 |
|
| 2019 |
Moulick R, Goluguri RR, Udgaonkar JB. Ruggedness in the Free Energy Landscape Dictates Misfolding of the Prion Protein. Journal of Molecular Biology. PMID 30611749 DOI: 10.1016/j.jmb.2018.12.009 |
0.308 |
|
| 2019 |
Goluguri RR, Sen S, Udgaonkar J. Author response: Microsecond sub-domain motions and the folding and misfolding of the mouse prion protein Elife. DOI: 10.7554/Elife.44766.032 |
0.318 |
|
| 2019 |
Sengupta I, Udgaonkar J. Author response: Monitoring site-specific conformational changes in real-time reveals a misfolding mechanism of the prion protein Elife. DOI: 10.7554/Elife.44698.030 |
0.387 |
|
| 2018 |
Jethva PN, Udgaonkar JB. The osmolyte TMAO modulates protein folding cooperativity by altering global protein stability. Biochemistry. PMID 30199620 DOI: 10.1021/acs.biochem.8b00698 |
0.395 |
|
| 2018 |
Sengupta I, Udgaonkar JB. Structural mechanisms of oligomer and amyloid fibril formation by the prion protein. Chemical Communications (Cambridge, England). PMID 29789820 DOI: 10.1039/c8cc03053g |
0.574 |
|
| 2017 |
Bhatia S, Krishnamoorthy G, Udgaonkar JB. Site-specific time-resolved FRET reveals local variations in the unfolding mechanism in an apparently two-state protein unfolding transition. Physical Chemistry Chemical Physics : Pccp. PMID 29085950 DOI: 10.1039/c7cp06214a |
0.78 |
|
| 2017 |
Jethva PN, Udgaonkar JB. Modulation of the Extent of Cooperative Structural Change During Protein Folding by Chemical Denaturant. The Journal of Physical Chemistry. B. PMID 28771359 DOI: 10.1021/acs.jpcb.7b04473 |
0.366 |
|
| 2017 |
Sengupta I, Udgaonkar JB. Expression and purification of single cysteine-containing mutant variants of the mouse prion protein by oxidative refolding. Protein Expression and Purification. PMID 28736314 DOI: 10.1016/j.pep.2017.07.014 |
0.594 |
|
| 2017 |
Malhotra P, Jethva PN, Udgaonkar JB. Chemical denaturants smoothen ruggedness on the free energy landscape of protein folding. Biochemistry. PMID 28714672 DOI: 10.1021/acs.biochem.7b00367 |
0.323 |
|
| 2017 |
Sen S, Goluguri RR, Udgaonkar JB. A dry transition state more compact than the native state is stabilized by non-native interactions during the unfolding of a small protein. Biochemistry. PMID 28682056 DOI: 10.1021/acs.biochem.7b00388 |
0.361 |
|
| 2017 |
Sengupta I, Bhate SH, Das R, Udgaonkar JB. Salt-mediated oligomerization of the mouse prion protein monitored by real time NMR. Journal of Molecular Biology. PMID 28502793 DOI: 10.1016/j.jmb.2017.05.006 |
0.624 |
|
| 2017 |
Moulick R, Udgaonkar JB. Identification and structural characterization of the precursor conformation of the prion protein which directly initiates misfolding and oligomerization. Journal of Molecular Biology. PMID 28147229 DOI: 10.1016/j.jmb.2017.01.019 |
0.351 |
|
| 2016 |
Malhotra P, Udgaonkar JB. How cooperative are protein folding and unfolding transitions? Protein Science : a Publication of the Protein Society. PMID 27522064 DOI: 10.1002/pro.3015 |
0.378 |
|
| 2016 |
Goluguri RR, Udgaonkar JB. Microsecond rearrangements of hydrophobic clusters in an initially collapsed globule prime structure formation during the folding of a small protein. Journal of Molecular Biology. PMID 27370109 DOI: 10.1016/j.jmb.2016.06.015 |
0.359 |
|
| 2016 |
Malhotra P, Udgaonkar JB. Secondary structural change can occur diffusely and not modularly during protein folding and unfolding reactions. Journal of the American Chemical Society. PMID 27093885 DOI: 10.1021/jacs.6b03356 |
0.376 |
|
| 2016 |
Mondal S, Kallianpur MV, Udgaonkar JB, Krishnamoorthy G. Molecular crowding causes narrowing of population heterogeneityand restricts internal dynamics in a protein Methods and Applications in Fluorescence. 4. DOI: 10.1088/2050-6120/4/1/014003 |
0.394 |
|
| 2015 |
Singh J, Udgaonkar JB. 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. Biochemistry. PMID 26713717 DOI: 10.1021/acs.biochem.5b01266 |
0.312 |
|
| 2015 |
Moulick R, Das R, Udgaonkar JB. Partially Unfolded Forms of the Prion Protein Populated under Misfolding-promoting Conditions: CHARACTERIZATION BY HYDROGEN EXCHANGE MASS SPECTROMETRY AND NMR. The Journal of Biological Chemistry. 290: 25227-40. PMID 26306043 DOI: 10.1074/jbc.M115.677575 |
0.338 |
|
| 2015 |
Goluguri RR, Udgaonkar JB. Rise of the Helix from a Collapsed Globule during the Folding of Monellin. Biochemistry. 54: 5356-65. PMID 26258844 DOI: 10.1021/acs.biochem.5b00730 |
0.364 |
|
| 2015 |
Malhotra P, Udgaonkar JB. Tuning Cooperativity on the Free Energy Landscape of Protein Folding. Biochemistry. 54: 3431-41. PMID 25984766 DOI: 10.1021/acs.biochem.5b00247 |
0.407 |
|
| 2015 |
Singh J, Udgaonkar JB. Structural Effects of Multiple Pathogenic Mutations Suggest a Model for the Initiation of Misfolding of the Prion Protein. Angewandte Chemie (International Ed. in English). 54: 7529-33. PMID 25959220 DOI: 10.1002/anie.201501011 |
0.333 |
|
| 2015 |
Krishnamoorthy G, Yadav A, Udgaonkar J. Barrierless Transition Identified during Folding of Barstar by using Time-Resolved FRET from 5-Flurotryptophan Biophysical Journal. 108: 50a. DOI: 10.1016/J.Bpj.2014.11.308 |
0.462 |
|
| 2014 |
Malhotra P, Udgaonkar JB. High-energy intermediates in protein unfolding characterized by thiol labeling under nativelike conditions. Biochemistry. 53: 3608-20. PMID 24832528 DOI: 10.1021/bi401493t |
0.373 |
|
| 2014 |
Bhardwaj V, Panicker MM, Udgaonkar JB. Fluorescence anisotropy uncovers changes in protein packing with inclusion growth in a cellular model of polyglutamine aggregation. Biochemistry. 53: 3621-36. PMID 24819723 DOI: 10.1021/Bi500383H |
0.304 |
|
| 2014 |
Dasgupta A, Udgaonkar JB, Das P. Multistage unfolding of an SH3 domain: an initial urea-filled dry molten globule precedes a wet molten globule with non-native structure. The Journal of Physical Chemistry. B. 118: 6380-92. PMID 24661021 DOI: 10.1021/Jp410019F |
0.314 |
|
| 2014 |
Moulick R, Udgaonkar JB. Thermodynamic characterization of the unfolding of the prion protein. Biophysical Journal. 106: 410-20. PMID 24461016 DOI: 10.1016/j.bpj.2013.11.4491 |
0.351 |
|
| 2013 |
Kishore M, Krishnamoorthy G, Udgaonkar JB. Critical evaluation of the two-state model describing the equilibrium unfolding of the PI3K SH3 domain by time-resolved fluorescence resonance energy transfer. Biochemistry. 52: 9482-96. PMID 24325755 DOI: 10.1021/Bi401337K |
0.601 |
|
| 2013 |
Sarkar SS, Udgaonkar JB, Krishnamoorthy G. Unfolding of a small protein proceeds via dry and wet globules and a solvated transition state. Biophysical Journal. 105: 2392-402. PMID 24268151 DOI: 10.1016/j.bpj.2013.09.048 |
0.581 |
|
| 2013 |
Aghera N, Udgaonkar JB. The utilization of competing unfolding pathways of monellin is dictated by enthalpic barriers. Biochemistry. 52: 5770-9. PMID 23901851 DOI: 10.1021/bi400688w |
0.313 |
|
| 2013 |
Singh J, Udgaonkar JB. Dissection of conformational conversion events during prion amyloid fibril formation using hydrogen exchange and mass spectrometry. Journal of Molecular Biology. 425: 3510-21. PMID 23811055 DOI: 10.1016/j.jmb.2013.06.009 |
0.321 |
|
| 2013 |
Udgaonkar J, Marqusee S. Folding and binding. Current Opinion in Structural Biology. 23: 1-3. PMID 23374590 DOI: 10.1016/J.Sbi.2013.01.002 |
0.65 |
|
| 2013 |
Udgaonkar JB. Polypeptide chain collapse and protein folding. Archives of Biochemistry and Biophysics. 531: 24-33. PMID 23085151 DOI: 10.1016/j.abb.2012.10.003 |
0.31 |
|
| 2012 |
Aghera N, Dasgupta I, Udgaonkar JB. A buried ionizable residue destabilizes the native state and the transition state in the folding of monellin. Biochemistry. 51: 9058-66. PMID 23088428 DOI: 10.1021/bi3008017 |
0.368 |
|
| 2012 |
Dasgupta A, Udgaonkar JB. Transient non-native burial of a Trp residue occurs initially during the unfolding of a SH3 domain. Biochemistry. 51: 8226-34. PMID 22998628 DOI: 10.1021/bi3008627 |
0.34 |
|
| 2012 |
Jha A, Narayan S, Udgaonkar JB, Krishnamoorthy G. Solvent-induced tuning of internal structure in a protein amyloid protofibril. Biophysical Journal. 103: 797-806. PMID 22947941 DOI: 10.1016/j.bpj.2012.07.021 |
0.568 |
|
| 2012 |
Aghera N, Udgaonkar JB. Kinetic studies of the folding of heterodimeric monellin: evidence for switching between alternative parallel pathways. Journal of Molecular Biology. 420: 235-50. PMID 22542529 DOI: 10.1016/j.jmb.2012.04.019 |
0.393 |
|
| 2011 |
Sarkar SS, Udgaonkar JB, Krishnamoorthy G. Reduced fluorescence lifetime heterogeneity of 5-fluorotryptophan in comparison to tryptophan in proteins: implication for resonance energy transfer experiments. The Journal of Physical Chemistry. B. 115: 7479-86. PMID 21574591 DOI: 10.1021/Jp2016984 |
0.56 |
|
| 2011 |
Jha SK, Dasgupta A, Malhotra P, Udgaonkar JB. Identification of multiple folding pathways of monellin using pulsed thiol labeling and mass spectrometry. Biochemistry. 50: 3062-74. PMID 21355628 DOI: 10.1021/bi1006332 |
0.322 |
|
| 2011 |
Aghera N, Earanna N, Udgaonkar JB. Equilibrium unfolding studies of monellin: the double-chain variant appears to be more stable than the single-chain variant. Biochemistry. 50: 2434-44. PMID 21351752 DOI: 10.1021/bi101955f |
0.373 |
|
| 2011 |
Jha A, Ishii K, Udgaonkar JB, Tahara T, Krishnamoorthy G. Exploration of the correlation between solvation dynamics and internal dynamics of a protein. Biochemistry. 50: 397-408. PMID 21141874 DOI: 10.1021/Bi101440C |
0.519 |
|
| 2010 |
Dasgupta A, Udgaonkar JB. Evidence for initial non-specific polypeptide chain collapse during the refolding of the SH3 domain of PI3 kinase. Journal of Molecular Biology. 403: 430-45. PMID 20837026 DOI: 10.1016/j.jmb.2010.08.046 |
0.353 |
|
| 2009 |
Wani AH, Udgaonkar JB. Native state dynamics drive the unfolding of the SH3 domain of PI3 kinase at high denaturant concentration. Proceedings of the National Academy of Sciences of the United States of America. 106: 20711-6. PMID 19920173 DOI: 10.1073/pnas.0908617106 |
0.307 |
|
| 2009 |
Jha A, Udgaonkar JB, Krishnamoorthy G. Characterization of the heterogeneity and specificity of interpolypeptide interactions in amyloid protofibrils by measurement of site-specific fluorescence anisotropy decay kinetics. Journal of Molecular Biology. 393: 735-52. PMID 19716830 DOI: 10.1016/j.jmb.2009.08.053 |
0.58 |
|
| 2009 |
Jha SK, Udgaonkar JB. Direct evidence for a dry molten globule intermediate during the unfolding of a small protein. Proceedings of the National Academy of Sciences of the United States of America. 106: 12289-94. PMID 19617531 DOI: 10.1073/pnas.0905744106 |
0.423 |
|
| 2009 |
Jha SK, Dhar D, Krishnamoorthy G, Udgaonkar JB. Continuous dissolution of structure during the unfolding of a small protein. Proceedings of the National Academy of Sciences of the United States of America. 106: 11113-8. PMID 19553216 DOI: 10.1073/pnas.0812564106 |
0.59 |
|
| 2009 |
Patra AK, Udgaonkar JB. GroEL can unfold late intermediates populated on the folding pathways of monellin. Journal of Molecular Biology. 389: 759-75. PMID 19393665 DOI: 10.1016/j.jmb.2009.04.039 |
0.33 |
|
| 2009 |
Wani AH, Udgaonkar JB. Revealing a concealed intermediate that forms after the rate-limiting step of refolding of the SH3 domain of PI3 kinase. Journal of Molecular Biology. 387: 348-62. PMID 19356591 DOI: 10.1016/j.jmb.2009.01.060 |
0.386 |
|
| 2009 |
Kumar S, Udgaonkar JB. Conformational conversion may precede or follow aggregate elongation on alternative pathways of amyloid protofibril formation. Journal of Molecular Biology. 385: 1266-76. PMID 19063899 DOI: 10.1016/j.jmb.2008.11.033 |
0.341 |
|
| 2009 |
Krishnan B, Kulothungan SR, Patra AK, Udgaonkar JB, Varadarajan R. SecB-mediated protein export need not occur via kinetic partitioning. Journal of Molecular Biology. 385: 1243-56. PMID 19028503 DOI: 10.1016/J.Jmb.2008.10.094 |
0.354 |
|
| 2008 |
Udgaonkar JB. Multiple routes and structural heterogeneity in protein folding. Annual Review of Biophysics. 37: 489-510. PMID 18573092 DOI: 10.1146/annurev.biophys.37.032807.125920 |
0.358 |
|
| 2008 |
Sinha KK, Udgaonkar JB. Barrierless evolution of structure during the submillisecond refolding reaction of a small protein. Proceedings of the National Academy of Sciences of the United States of America. 105: 7998-8003. PMID 18523007 DOI: 10.1073/pnas.0803193105 |
0.357 |
|
| 2007 |
Jha SK, Udgaonkar JB. Exploring the cooperativity of the fast folding reaction of a small protein using pulsed thiol labeling and mass spectrometry. The Journal of Biological Chemistry. 282: 37479-91. PMID 17959598 DOI: 10.1074/jbc.M706714200 |
0.387 |
|
| 2007 |
Patra AK, Udgaonkar JB. Characterization of the folding and unfolding reactions of single-chain monellin: evidence for multiple intermediates and competing pathways. Biochemistry. 46: 11727-43. PMID 17902706 DOI: 10.1021/bi701142a |
0.387 |
|
| 2007 |
Sinha KK, Udgaonkar JB. Dissecting the non-specific and specific components of the initial folding reaction of barstar by multi-site FRET measurements. Journal of Molecular Biology. 370: 385-405. PMID 17512542 DOI: 10.1016/j.jmb.2007.04.061 |
0.385 |
|
| 2007 |
Kumar S, Mohanty SK, Udgaonkar JB. Mechanism of formation of amyloid protofibrils of barstar from soluble oligomers: evidence for multiple steps and lateral association coupled to conformational conversion. Journal of Molecular Biology. 367: 1186-204. PMID 17292913 DOI: 10.1016/j.jmb.2007.01.039 |
0.321 |
|
| 2007 |
Pradeep L, Udgaonkar JB. Diffusional barrier in the unfolding of a small protein. Journal of Molecular Biology. 366: 1016-28. PMID 17188296 DOI: 10.1016/j.jmb.2006.11.064 |
0.343 |
|
| 2006 |
Saxena AM, Udgaonkar JB, Krishnamoorthy G. Characterization of intra-molecular distances and site-specific dynamics in chemically unfolded barstar: evidence for denaturant-dependent non-random structure. Journal of Molecular Biology. 359: 174-89. PMID 16603185 DOI: 10.1016/j.jmb.2006.03.013 |
0.59 |
|
| 2006 |
Mukhopadhyay S, Nayak PK, Udgaonkar JB, Krishnamoorthy G. Characterization of the formation of amyloid protofibrils from barstar by mapping residue-specific fluorescence dynamics. Journal of Molecular Biology. 358: 935-42. PMID 16546212 DOI: 10.1016/J.Jmb.2006.02.006 |
0.551 |
|
| 2005 |
Sinha KK, Udgaonkar JB. Dependence of the size of the initially collapsed form during the refolding of barstar on denaturant concentration: evidence for a continuous transition. Journal of Molecular Biology. 353: 704-18. PMID 16188274 DOI: 10.1016/j.jmb.2005.08.056 |
0.394 |
|
| 2005 |
Saxena AM, Udgaonkar JB, Krishnamoorthy G. Protein dynamics control proton transfer from bulk solvent to protein interior: a case study with a green fluorescent protein. Protein Science : a Publication of the Protein Society. 14: 1787-99. PMID 15937281 DOI: 10.1110/ps.051391205 |
0.522 |
|
| 2004 |
Bhavesh NS, Juneja J, Udgaonkar JB, Hosur RV. Native and nonnative conformational preferences in the urea-unfolded state of barstar. Protein Science : a Publication of the Protein Society. 13: 3085-91. PMID 15537753 DOI: 10.1110/ps.04805204 |
0.326 |
|
| 2004 |
Pradeep L, Udgaonkar JB. Osmolytes induce structure in an early intermediate on the folding pathway of barstar. The Journal of Biological Chemistry. 279: 40303-13. PMID 15258135 DOI: 10.1074/jbc.M406323200 |
0.351 |
|
| 2004 |
Beena K, Udgaonkar JB, Varadarajan R. Effect of signal peptide on the stability and folding kinetics of maltose binding protein. Biochemistry. 43: 3608-19. PMID 15035631 DOI: 10.1021/Bi0360509 |
0.306 |
|
| 2004 |
Sridevi K, Lakshmikanth GS, Krishnamoorthy G, Udgaonkar JB. Increasing stability reduces conformational heterogeneity in a protein folding intermediate ensemble. Journal of Molecular Biology. 337: 699-711. PMID 15019788 DOI: 10.1016/j.jmb.2003.12.083 |
0.544 |
|
| 2003 |
Rami BR, Krishnamoorthy G, Udgaonkar JB. Dynamics of the core tryptophan during the formation of a productive molten globule intermediate of barstar. Biochemistry. 42: 7986-8000. PMID 12834351 DOI: 10.1021/Bi030006B |
0.553 |
|
| 2003 |
Sridevi K, Udgaonkar JB. Surface expansion is independent of and occurs faster than core solvation during the unfolding of barstar. Biochemistry. 42: 1551-63. PMID 12578368 DOI: 10.1021/bi0268697 |
0.312 |
|
| 2003 |
Juneja J, Udgaonkar JB. NMR studies of protein folding Current Science. 84: 157-172. |
0.318 |
|
| 2002 |
Juneja J, Udgaonkar JB. Characterization of the unfolding of ribonuclease a by a pulsed hydrogen exchange study: evidence for competing pathways for unfolding. Biochemistry. 41: 2641-54. PMID 11851411 DOI: 10.1021/bi011480p |
0.33 |
|
| 2002 |
Rami BR, Udgaonkar JB. Mechanism of formation of a productive molten globule form of barstar. Biochemistry. 41: 1710-6. PMID 11827514 DOI: 10.1021/bi0120300 |
0.325 |
|
| 2002 |
Sridevi K, Udgaonkar JB. Unfolding rates of barstar determined in native and low denaturant conditions indicate the presence of intermediates. Biochemistry. 41: 1568-78. PMID 11814350 DOI: 10.1021/bi011494v |
0.324 |
|
| 2001 |
Bhutani N, Udgaonkar JB. GroEL channels the folding of thioredoxin along one kinetic route. Journal of Molecular Biology. 314: 1167-79. PMID 11743732 DOI: 10.1006/jmbi.2000.5193 |
0.392 |
|
| 2001 |
Rami BR, Udgaonkar JB. pH-jump-induced folding and unfolding studies of barstar: evidence for multiple folding and unfolding pathways. Biochemistry. 40: 15267-79. PMID 11735409 DOI: 10.1021/bi011701r |
0.314 |
|
| 2001 |
Bhuyan AK, Udgaonkar JB. Folding of horse cytochrome c in the reduced state. Journal of Molecular Biology. 312: 1135-60. PMID 11580255 DOI: 10.1006/jmbi.2001.4993 |
0.377 |
|
| 2001 |
Lakshmikanth GS, Sridevi K, Krishnamoorthy G, Udgaonkar JB. Structure is lost incrementally during the unfolding of barstar. Nature Structural Biology. 8: 799-804. PMID 11524685 DOI: 10.1038/nsb0901-799 |
0.608 |
|
| 2001 |
Ganesh C, Zaidi FN, Udgaonkar JB, Varadarajan R. Reversible formation of on-pathway macroscopic aggregates during the folding of maltose binding protein. Protein Science : a Publication of the Protein Society. 10: 1635-44. PMID 11468360 DOI: 10.1110/Ps.8101 |
0.353 |
|
| 2000 |
Sridevi K, Juneja J, Bhuyan AK, Krishnamoorthy G, Udgaonkar JB. 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. Journal of Molecular Biology. 302: 479-95. PMID 10970747 DOI: 10.1006/jmbi.2000.4060 |
0.601 |
|
| 2000 |
Bhutani N, Udgaonkar JB. A thermodynamic coupling mechanism can explain the GroEL-mediated acceleration of the folding of barstar. Journal of Molecular Biology. 297: 1037-44. PMID 10764571 DOI: 10.1006/jmbi.2000.3648 |
0.374 |
|
| 2000 |
Ramachandran S, Rami BR, Udgaonkar JB. Measurements of cysteine reactivity during protein unfolding suggest the presence of competing pathways. Journal of Molecular Biology. 297: 733-45. PMID 10731424 DOI: 10.1006/jmbi.2000.3605 |
0.347 |
|
| 1999 |
Bhuyan AK, Udgaonkar JB. Observation of multistate kinetics during the slow folding and unfolding of barstar. Biochemistry. 38: 9158-68. PMID 10413490 DOI: 10.1021/bi990285w |
0.379 |
|
| 1998 |
Panse VG, Udgaonkar JB, Varadarajan R. SecB binds only to a late native-like intermediate in the folding pathway of barstar and not to the unfolded state. Biochemistry. 37: 14477-83. PMID 9772175 DOI: 10.1021/Bi980777T |
0.344 |
|
| 1998 |
Bhuyan AK, Udgaonkar JB. Two structural subdomains of barstar detected by rapid mixing NMR measurement of amide hydrogen exchange. Proteins. 30: 295-308. PMID 9517545 DOI: 10.1002/(SICI)1097-0134(19980215)30:3<295::AID-PROT9>3.0.CO;2-J |
0.312 |
|
| 1997 |
Zaidi FN, Nath U, Udgaonkar JB. Multiple intermediates and transition states during protein unfolding. Nature Structural Biology. 4: 1016-24. PMID 9406552 |
0.395 |
|
| 1997 |
Agashe VR, Schmid FX, Udgaonkar JB. Thermodynamics of the complex protein unfolding reaction of barstar. Biochemistry. 36: 12288-95. PMID 9315868 DOI: 10.1021/Bi971062D |
0.544 |
|
| 1997 |
Nath U, Udgaonkar JB. Folding of tryptophan mutants of barstar: evidence for an initial hydrophobic collapse on the folding pathway. Biochemistry. 36: 8602-10. PMID 9214306 DOI: 10.1021/bi970426z |
0.385 |
|
| 1997 |
Nath U, Udgaonkar JB. How do proteins fold? Current Science. 72: 180-191. |
0.312 |
|
| 1996 |
Swaminathan R, Nath U, Udgaonkar JB, Periasamy N, Krishnamoorthy G. Motional dynamics of a buried tryptophan reveals the presence of partially structured forms during denaturation of barstar. Biochemistry. 35: 9150-7. PMID 8703920 DOI: 10.1021/Bi9603478 |
0.725 |
|
| 1995 |
Nath U, Udgaonkar JB. Perturbation of a tertiary hydrogen bond in barstar by mutagenesis of the sole His residue to Gln leads to accumulation of at least one equilibrium folding intermediate. Biochemistry. 34: 1702-13. PMID 7849030 |
0.329 |
|
| 1995 |
Udgaonkar JB, Baldwin RL. Nature of the early folding intermediate of ribonuclease A. Biochemistry. 34: 4088-96. PMID 7696273 DOI: 10.1021/Bi00012A027 |
0.442 |
|
| 1995 |
Agashe VR, Shastry MC, Udgaonkar JB. Initial hydrophobic collapse in the folding of barstar. Nature. 377: 754-7. PMID 7477269 DOI: 10.1038/377754a0 |
0.368 |
|
| 1994 |
Khurana R, Udgaonkar JB. Equilibrium unfolding studies of barstar: Evidence for an alternative conformation which resembles a molten globule Biochemistry. 33: 106-115. PMID 8286327 |
0.355 |
|
| 1993 |
Udgaonkar JB. Folding in an unfolded protein Current Science. 64: 452-454. |
0.329 |
|
| 1990 |
Udgaonkar JB, Baldwin RL. Early folding intermediate of ribonuclease A. Proceedings of the National Academy of Sciences of the United States of America. 87: 8197-201. PMID 2236032 DOI: 10.1073/Pnas.87.21.8197 |
0.474 |
|
| 1989 |
Milburn T, Matsubara N, Billington AP, Udgaonkar JB, Walker JW, Carpenter BK, Webb WW, Marque J, Denk W, McCray JA. Synthesis, photochemistry, and biological activity of a caged photolabile acetylcholine receptor ligand. Biochemistry. 28: 49-55. PMID 2706267 DOI: 10.1021/Bi00427A008 |
0.751 |
|
| 1988 |
Udgaonkar JB, Baldwin RL. NMR evidence for an early framework intermediate on the folding pathway of ribonuclease A. Nature. 335: 694-9. PMID 2845278 DOI: 10.1038/335694A0 |
0.56 |
|
| 1987 |
Udgaonkar JB, Hess GP. Acetylcholine receptor: channel-opening kinetics evaluated by rapid chemical kinetic and single-channel current measurements. Biophysical Journal. 52: 873-83. PMID 2447965 DOI: 10.1016/S0006-3495(87)83281-2 |
0.535 |
|
| 1987 |
Udgaonkar JB, Hess GP. Chemical kinetic measurements of a mammalian acetylcholine receptor by a fast-reaction technique. Proceedings of the National Academy of Sciences of the United States of America. 84: 8758-62. PMID 2447583 DOI: 10.1073/Pnas.84.24.8758 |
0.543 |
|
| 1987 |
Hess GP, Udgaonkar JB, Olbricht WL. Chemical kinetic measurements of transmembrane processes using rapid reaction techniques: acetylcholine receptor. Annual Review of Biophysics and Biophysical Chemistry. 16: 507-34. PMID 2439099 DOI: 10.1146/annurev.bb.16.060187.002451 |
0.517 |
|
| 1987 |
Udgaonkar JB, Hess GP. Isosteric regulation of the acetylcholine receptor Trends in Pharmacological Sciences. 8: 190-192. DOI: 10.1016/0165-6147(87)90165-9 |
0.537 |
|
| 1987 |
Hess GP, Udgaonkar JB. Voltage-dependent inhibition of the acetylcholine receptor Trends in Pharmacological Sciences. 8: 335. DOI: 10.1016/0165-6147(87)90140-4 |
0.485 |
|
| 1986 |
Takeyasu K, Shiono S, Udgaonkar JB, Fujita N, Hess GP. Acetylcholine receptor: characterization of the voltage-dependent regulatory (inhibitory) site for acetylcholine in membrane vesicles from Torpedo californica electroplax. Biochemistry. 25: 1770-6. PMID 3707909 DOI: 10.1021/Bi00355A048 |
0.705 |
|
| 1986 |
Udgaonkar JB, Hess GP. Acetylcholine receptor kinetics: chemical kinetics. The Journal of Membrane Biology. 93: 93-109. PMID 3543374 DOI: 10.1007/Bf01870803 |
0.536 |
|
| 1986 |
Pasquale EB, Udgaonkar JB, Hess GP. Single-channel current recordings of acetylcholine receptors in electroplax isolated from the Electrophorus electricus Main and Sachs' electric organs. The Journal of Membrane Biology. 93: 195-204. PMID 2433452 DOI: 10.1007/Bf01870811 |
0.64 |
|
| 1984 |
Shiono S, Takeyasu K, Udgaonkar JB, Delcour AH, Fujita N, Hess GP. 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). Biochemistry. 23: 6889-93. PMID 6529587 DOI: 10.1021/Bi00321A094 |
0.749 |
|
| 1983 |
Takeyasu K, Udgaonkar JB, Hess GP. Acetylcholine receptor: evidence for a voltage-dependent regulatory site for acetylcholine. Chemical kinetic measurements in membrane vesicles using a voltage clamp. Biochemistry. 22: 5973-8. PMID 6661421 DOI: 10.1021/Bi00294A042 |
0.543 |
|
| 1983 |
Pasquale EB, Takeyasu K, Udgaonkar JB, Cash DJ, Severski MC, Hess GP. Acetylcholine receptor: evidence for a regulatory binding site in investigations of suberyldicholine-induced transmembrane ion flux in Electrophorus electricus membrane vesicles. Biochemistry. 22: 5967-73. PMID 6661420 DOI: 10.1021/Bi00294A041 |
0.715 |
|
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