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Items: 1 to 50 of 82

1.

Crystal structure of phosphoribulokinase from Synechococcus sp. strain PCC 6301.

Wilson RH, Hayer-Hartl M, Bracher A.

Acta Crystallogr F Struct Biol Commun. 2019 Apr 1;75(Pt 4):278-289. doi: 10.1107/S2053230X19002693. Epub 2019 Apr 2.

PMID:
30950829
2.

Improved recombinant expression and purification of functional plant Rubisco.

Wilson RH, Thieulin-Pardo G, Hartl FU, Hayer-Hartl M.

FEBS Lett. 2019 Mar;593(6):611-621. doi: 10.1002/1873-3468.13352. Epub 2019 Mar 14.

PMID:
30815863
3.

Rubisco condensate formation by CcmM in β-carboxysome biogenesis.

Wang H, Yan X, Aigner H, Bracher A, Nguyen ND, Hee WY, Long BM, Price GD, Hartl FU, Hayer-Hartl M.

Nature. 2019 Feb;566(7742):131-135. doi: 10.1038/s41586-019-0880-5. Epub 2019 Jan 23.

PMID:
30675061
4.

Life of proteins: from nascent chain to degradation.

Herrmann JM, Carvalho P, Hayer-Hartl M, Yoshihisa T.

Nat Struct Mol Biol. 2018 Nov;25(11):996-999. doi: 10.1038/s41594-018-0150-5. No abstract available.

PMID:
30374085
5.

Tc toxin activation requires unfolding and refolding of a β-propeller.

Gatsogiannis C, Merino F, Roderer D, Balchin D, Schubert E, Kuhlee A, Hayer-Hartl M, Raunser S.

Nature. 2018 Nov;563(7730):209-213. doi: 10.1038/s41586-018-0556-6. Epub 2018 Sep 19.

PMID:
30232455
6.

Pathway of Actin Folding Directed by the Eukaryotic Chaperonin TRiC.

Balchin D, Miličić G, Strauss M, Hayer-Hartl M, Hartl FU.

Cell. 2018 Sep 6;174(6):1507-1521.e16. doi: 10.1016/j.cell.2018.07.006. Epub 2018 Aug 9.

PMID:
30100183
7.

Complex Chaperone Dependence of Rubisco Biogenesis.

Wilson RH, Hayer-Hartl M.

Biochemistry. 2018 Jun 12;57(23):3210-3216. doi: 10.1021/acs.biochem.8b00132. Epub 2018 Apr 4. Review.

PMID:
29589905
8.

GroEL Ring Separation and Exchange in the Chaperonin Reaction.

Yan X, Shi Q, Bracher A, Miličić G, Singh AK, Hartl FU, Hayer-Hartl M.

Cell. 2018 Jan 25;172(3):605-617.e11. doi: 10.1016/j.cell.2017.12.010. Epub 2018 Jan 11.

9.

Plant RuBisCo assembly in E. coli with five chloroplast chaperones including BSD2.

Aigner H, Wilson RH, Bracher A, Calisse L, Bhat JY, Hartl FU, Hayer-Hartl M.

Science. 2017 Dec 8;358(6368):1272-1278. doi: 10.1126/science.aap9221.

PMID:
29217567
10.

From chaperonins to Rubisco assembly and metabolic repair.

Hayer-Hartl M.

Protein Sci. 2017 Dec;26(12):2324-2333. doi: 10.1002/pro.3309. Epub 2017 Oct 10. Review.

11.

Mechanism of Enzyme Repair by the AAA+ Chaperone Rubisco Activase.

Bhat JY, Miličić G, Thieulin-Pardo G, Bracher A, Maxwell A, Ciniawsky S, Mueller-Cajar O, Engen JR, Hartl FU, Wendler P, Hayer-Hartl M.

Mol Cell. 2017 Sep 7;67(5):744-756.e6. doi: 10.1016/j.molcel.2017.07.004. Epub 2017 Aug 10.

12.

Rubisco Activases: AAA+ Chaperones Adapted to Enzyme Repair.

Bhat JY, Thieulin-Pardo G, Hartl FU, Hayer-Hartl M.

Front Mol Biosci. 2017 Apr 10;4:20. doi: 10.3389/fmolb.2017.00020. eCollection 2017. Review.

13.

Biogenesis and Metabolic Maintenance of Rubisco.

Bracher A, Whitney SM, Hartl FU, Hayer-Hartl M.

Annu Rev Plant Biol. 2017 Apr 28;68:29-60. doi: 10.1146/annurev-arplant-043015-111633. Epub 2017 Jan 11. Review.

PMID:
28125284
14.

Soluble Oligomers of PolyQ-Expanded Huntingtin Target a Multiplicity of Key Cellular Factors.

Kim YE, Hosp F, Frottin F, Ge H, Mann M, Hayer-Hartl M, Hartl FU.

Mol Cell. 2016 Sep 15;63(6):951-64. doi: 10.1016/j.molcel.2016.07.022. Epub 2016 Aug 25.

15.

In vivo aspects of protein folding and quality control.

Balchin D, Hayer-Hartl M, Hartl FU.

Science. 2016 Jul 1;353(6294):aac4354. doi: 10.1126/science.aac4354. Review.

PMID:
27365453
16.

Failure of RQC machinery causes protein aggregation and proteotoxic stress.

Choe YJ, Park SH, Hassemer T, Körner R, Vincenz-Donnelly L, Hayer-Hartl M, Hartl FU.

Nature. 2016 Mar 10;531(7593):191-5. doi: 10.1038/nature16973. Epub 2016 Feb 29.

PMID:
26934223
17.

Structure of human heat-shock transcription factor 1 in complex with DNA.

Neudegger T, Verghese J, Hayer-Hartl M, Hartl FU, Bracher A.

Nat Struct Mol Biol. 2016 Feb;23(2):140-6. doi: 10.1038/nsmb.3149. Epub 2016 Jan 4.

PMID:
26727489
18.

The GroEL-GroES Chaperonin Machine: A Nano-Cage for Protein Folding.

Hayer-Hartl M, Bracher A, Hartl FU.

Trends Biochem Sci. 2016 Jan;41(1):62-76. doi: 10.1016/j.tibs.2015.07.009. Epub 2015 Sep 25. Review.

PMID:
26422689
19.

Structural Analysis of the Rubisco-Assembly Chaperone RbcX-II from Chlamydomonas reinhardtii.

Bracher A, Hauser T, Liu C, Hartl FU, Hayer-Hartl M.

PLoS One. 2015 Aug 25;10(8):e0135448. doi: 10.1371/journal.pone.0135448. eCollection 2015.

20.

Structure and mechanism of the Rubisco-assembly chaperone Raf1.

Hauser T, Bhat JY, Miličić G, Wendler P, Hartl FU, Bracher A, Hayer-Hartl M.

Nat Struct Mol Biol. 2015 Sep;22(9):720-8. doi: 10.1038/nsmb.3062. Epub 2015 Aug 3.

PMID:
26237510
21.

Chaperonin-Assisted Protein Folding: Relative Population of Asymmetric and Symmetric GroEL:GroES Complexes.

Haldar S, Gupta AJ, Yan X, Miličić G, Hartl FU, Hayer-Hartl M.

J Mol Biol. 2015 Jun 19;427(12):2244-55. doi: 10.1016/j.jmb.2015.04.009. Epub 2015 Apr 23.

PMID:
25912285
22.

Opposing effects of folding and assembly chaperones on evolvability of Rubisco.

Durão P, Aigner H, Nagy P, Mueller-Cajar O, Hartl FU, Hayer-Hartl M.

Nat Chem Biol. 2015 Feb;11(2):148-55. doi: 10.1038/nchembio.1715. Epub 2015 Jan 5.

PMID:
25558973
23.

Role of auxiliary proteins in Rubisco biogenesis and function.

Hauser T, Popilka L, Hartl FU, Hayer-Hartl M.

Nat Plants. 2015 Jun 2;1:15065. doi: 10.1038/nplants.2015.65. Review.

PMID:
27250005
24.

Degradation of potent Rubisco inhibitor by selective sugar phosphatase.

Bracher A, Sharma A, Starling-Windhof A, Hartl FU, Hayer-Hartl M.

Nat Plants. 2015 Jan 8;1:14002. doi: 10.1038/nplants.2014.2.

PMID:
27246049
25.

Role of small subunit in mediating assembly of red-type form I Rubisco.

Joshi J, Mueller-Cajar O, Tsai YC, Hartl FU, Hayer-Hartl M.

J Biol Chem. 2015 Jan 9;290(2):1066-74. doi: 10.1074/jbc.M114.613091. Epub 2014 Nov 4.

26.

Active cage mechanism of chaperonin-assisted protein folding demonstrated at single-molecule level.

Gupta AJ, Haldar S, Miličić G, Hartl FU, Hayer-Hartl M.

J Mol Biol. 2014 Jul 29;426(15):2739-54. doi: 10.1016/j.jmb.2014.04.018. Epub 2014 May 6.

PMID:
24816391
27.

GroEL/ES chaperonin modulates the mechanism and accelerates the rate of TIM-barrel domain folding.

Georgescauld F, Popova K, Gupta AJ, Bracher A, Engen JR, Hayer-Hartl M, Hartl FU.

Cell. 2014 May 8;157(4):922-934. doi: 10.1016/j.cell.2014.03.038.

28.

Interplay of acetyltransferase EP300 and the proteasome system in regulating heat shock transcription factor 1.

Raychaudhuri S, Loew C, Körner R, Pinkert S, Theis M, Hayer-Hartl M, Buchholz F, Hartl FU.

Cell. 2014 Feb 27;156(5):975-85. doi: 10.1016/j.cell.2014.01.055.

29.

The first chaperonin.

Hartl FU, Hayer-Hartl M.

Nat Rev Mol Cell Biol. 2013 Oct;14(10):611. doi: 10.1038/nrm3665. No abstract available.

PMID:
24061226
30.

PolyQ proteins interfere with nuclear degradation of cytosolic proteins by sequestering the Sis1p chaperone.

Park SH, Kukushkin Y, Gupta R, Chen T, Konagai A, Hipp MS, Hayer-Hartl M, Hartl FU.

Cell. 2013 Jul 3;154(1):134-45. doi: 10.1016/j.cell.2013.06.003. Epub 2013 Jun 20.

31.

Molecular chaperone functions in protein folding and proteostasis.

Kim YE, Hipp MS, Bracher A, Hayer-Hartl M, Hartl FU.

Annu Rev Biochem. 2013;82:323-55. doi: 10.1146/annurev-biochem-060208-092442. Review.

PMID:
23746257
32.

DnaK functions as a central hub in the E. coli chaperone network.

Calloni G, Chen T, Schermann SM, Chang HC, Genevaux P, Agostini F, Tartaglia GG, Hayer-Hartl M, Hartl FU.

Cell Rep. 2012 Mar 29;1(3):251-64. doi: 10.1016/j.celrep.2011.12.007. Epub 2012 Mar 8.

33.

Chaperonin cofactors, Cpn10 and Cpn20, of green algae and plants function as hetero-oligomeric ring complexes.

Tsai YC, Mueller-Cajar O, Saschenbrecker S, Hartl FU, Hayer-Hartl M.

J Biol Chem. 2012 Jun 8;287(24):20471-81. doi: 10.1074/jbc.M112.365411. Epub 2012 Apr 19.

34.

Structure of green-type Rubisco activase from tobacco.

Stotz M, Mueller-Cajar O, Ciniawsky S, Wendler P, Hartl FU, Bracher A, Hayer-Hartl M.

Nat Struct Mol Biol. 2011 Nov 6;18(12):1366-70. doi: 10.1038/nsmb.2171.

PMID:
22056769
35.

Structure and function of the AAA+ protein CbbX, a red-type Rubisco activase.

Mueller-Cajar O, Stotz M, Wendler P, Hartl FU, Bracher A, Hayer-Hartl M.

Nature. 2011 Nov 2;479(7372):194-9. doi: 10.1038/nature10568.

PMID:
22048315
36.

Molecular chaperones in protein folding and proteostasis.

Hartl FU, Bracher A, Hayer-Hartl M.

Nature. 2011 Jul 20;475(7356):324-32. doi: 10.1038/nature10317. Review.

PMID:
21776078
37.

Crystal structure of a chaperone-bound assembly intermediate of form I Rubisco.

Bracher A, Starling-Windhof A, Hartl FU, Hayer-Hartl M.

Nat Struct Mol Biol. 2011 Jul 17;18(8):875-80. doi: 10.1038/nsmb.2090.

PMID:
21765418
38.

Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions.

Olzscha H, Schermann SM, Woerner AC, Pinkert S, Hecht MH, Tartaglia GG, Vendruscolo M, Hayer-Hartl M, Hartl FU, Vabulas RM.

Cell. 2011 Jan 7;144(1):67-78. doi: 10.1016/j.cell.2010.11.050.

39.

Protein folding in the cytoplasm and the heat shock response.

Vabulas RM, Raychaudhuri S, Hayer-Hartl M, Hartl FU.

Cold Spring Harb Perspect Biol. 2010 Dec;2(12):a004390. doi: 10.1101/cshperspect.a004390. Review.

40.

Chaperonin-catalyzed rescue of kinetically trapped states in protein folding.

Chakraborty K, Chatila M, Sinha J, Shi Q, Poschner BC, Sikor M, Jiang G, Lamb DC, Hartl FU, Hayer-Hartl M.

Cell. 2010 Jul 9;142(1):112-22. doi: 10.1016/j.cell.2010.05.027.

41.

Coupled chaperone action in folding and assembly of hexadecameric Rubisco.

Liu C, Young AL, Starling-Windhof A, Bracher A, Saschenbrecker S, Rao BV, Rao KV, Berninghausen O, Mielke T, Hartl FU, Beckmann R, Hayer-Hartl M.

Nature. 2010 Jan 14;463(7278):197-202. doi: 10.1038/nature08651.

PMID:
20075914
42.

Differential substrate specificity of group I and group II chaperonins in the archaeon Methanosarcina mazei.

Hirtreiter AM, Calloni G, Forner F, Scheibe B, Puype M, Vandekerckhove J, Mann M, Hartl FU, Hayer-Hartl M.

Mol Microbiol. 2009 Dec;74(5):1152-68. doi: 10.1111/j.1365-2958.2009.06924.x. Epub 2009 Oct 15.

43.

Converging concepts of protein folding in vitro and in vivo.

Hartl FU, Hayer-Hartl M.

Nat Struct Mol Biol. 2009 Jun;16(6):574-81. doi: 10.1038/nsmb.1591. Review.

PMID:
19491934
44.

Essential role of the chaperonin folding compartment in vivo.

Tang YC, Chang HC, Chakraborty K, Hartl FU, Hayer-Hartl M.

EMBO J. 2008 May 21;27(10):1458-68. doi: 10.1038/emboj.2008.77. Epub 2008 Apr 17.

45.

Monitoring protein conformation along the pathway of chaperonin-assisted folding.

Sharma S, Chakraborty K, Müller BK, Astola N, Tang YC, Lamb DC, Hayer-Hartl M, Hartl FU.

Cell. 2008 Apr 4;133(1):142-53. doi: 10.1016/j.cell.2008.01.048.

46.

SnapShot: molecular chaperones, Part I.

Chang HC, Tang YC, Hayer-Hartl M, Hartl FU.

Cell. 2007 Jan 12;128(1):212. No abstract available.

47.

Structure and function of RbcX, an assembly chaperone for hexadecameric Rubisco.

Saschenbrecker S, Bracher A, Rao KV, Rao BV, Hartl FU, Hayer-Hartl M.

Cell. 2007 Jun 15;129(6):1189-200.

48.

SnapShot: molecular chaperones, Part II.

Tang YC, Chang HC, Hayer-Hartl M, Hartl FU.

Cell. 2007 Jan 26;128(2):412. No abstract available.

49.

A simple semiempirical model for the effect of molecular confinement upon the rate of protein folding.

Hayer-Hartl M, Minton AP.

Biochemistry. 2006 Nov 7;45(44):13356-60.

PMID:
17073456
50.

Real-time observation of trigger factor function on translating ribosomes.

Kaiser CM, Chang HC, Agashe VR, Lakshmipathy SK, Etchells SA, Hayer-Hartl M, Hartl FU, Barral JM.

Nature. 2006 Nov 23;444(7118):455-60. Epub 2006 Oct 15.

PMID:
17051157

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