152 related articles for article (PubMed ID: 16533032)
1. Examination of the slow unfolding of pro-nerve growth factor argues against a loop threading mechanism for nerve growth factor.
Kliemannel M; Weininger U; Balbach J; Schwarz E; Rudolph R
Biochemistry; 2006 Mar; 45(11):3517-24. PubMed ID: 16533032
[TBL] [Abstract][Full Text] [Related]
2. RhNGF slow unfolding is not due to proline isomerization: possibility of a cystine knot loop-threading mechanism.
De Young LR; Burton LE; Liu J; Powell MF; Schmelzer CH; Skelton NJ
Protein Sci; 1996 Aug; 5(8):1554-66. PubMed ID: 8844846
[TBL] [Abstract][Full Text] [Related]
3. Oxidative folding of nerve growth factor can be mediated by the pro-peptide of neurotrophin-3.
Hauburger A; Kliemannel M; Madsen P; Rudolph R; Schwarz E
FEBS Lett; 2007 Sep; 581(22):4159-64. PubMed ID: 17698064
[TBL] [Abstract][Full Text] [Related]
4. The mature part of proNGF induces the structure of its pro-peptide.
Kliemannel M; Rattenholl A; Golbik R; Balbach J; Lilie H; Rudolph R; Schwarz E
FEBS Lett; 2004 May; 566(1-3):207-12. PubMed ID: 15147896
[TBL] [Abstract][Full Text] [Related]
5. A common mechanism for recombinant human NGF, BDNF, NT-3, and murine NGF slow unfolding.
De Young LR; Schmelzer CH; Burton LE
Protein Sci; 1999 Nov; 8(11):2513-8. PubMed ID: 10595557
[TBL] [Abstract][Full Text] [Related]
6. Pro-sequence assisted folding and disulfide bond formation of human nerve growth factor.
Rattenholl A; Ruoppolo M; Flagiello A; Monti M; Vinci F; Marino G; Lilie H; Schwarz E; Rudolph R
J Mol Biol; 2001 Jan; 305(3):523-33. PubMed ID: 11152610
[TBL] [Abstract][Full Text] [Related]
7. The pro-peptide of proNGF: structure formation and intramolecular association with NGF.
Kliemannel M; Golbik R; Rudolph R; Schwarz E; Lilie H
Protein Sci; 2007 Mar; 16(3):411-9. PubMed ID: 17242381
[TBL] [Abstract][Full Text] [Related]
8. Characterization of the folding and unfolding reactions of single-chain monellin: evidence for multiple intermediates and competing pathways.
Patra AK; Udgaonkar JB
Biochemistry; 2007 Oct; 46(42):11727-43. PubMed ID: 17902706
[TBL] [Abstract][Full Text] [Related]
9. Intrinsic structural disorder of mouse proNGF.
Paoletti F; Covaceuszach S; Konarev PV; Gonfloni S; Malerba F; Schwarz E; Svergun DI; Cattaneo A; Lamba D
Proteins; 2009 Jun; 75(4):990-1009. PubMed ID: 19089979
[TBL] [Abstract][Full Text] [Related]
10. Unfolding of the tetrameric loop deletion mutant of ROP protein is a second-order reaction.
Lassalle MW; Hinz HJ
Biochemistry; 1998 Jun; 37(23):8465-72. PubMed ID: 9622498
[TBL] [Abstract][Full Text] [Related]
11. Structural and functional properties of mouse proNGF.
Paoletti F; Konarev PV; Covaceuszach S; Schwarz E; Cattaneo A; Lamba D; Svergun DI
Biochem Soc Trans; 2006 Aug; 34(Pt 4):605-6. PubMed ID: 16856872
[TBL] [Abstract][Full Text] [Related]
12. Tetrameric N(5)-(L-1-carboxyethyl)-L-ornithine synthase: guanidine. HCl-induced unfolding and a low temperature requirement for refolding.
Ruvinov SB; Thompson J; Sackett DL; Ginsburg A
Arch Biochem Biophys; 1999 Nov; 371(1):115-23. PubMed ID: 10525296
[TBL] [Abstract][Full Text] [Related]
13. [Expression, purification and renaturation of proNGF in Escherichia coli].
Jiang H; Chai X; He B; Zhao J; Yu X
Sheng Wu Gong Cheng Xue Bao; 2008 Mar; 24(3):509-14. PubMed ID: 18589832
[TBL] [Abstract][Full Text] [Related]
14. Biophysical comparison of BMP-2, ProBMP-2, and the free pro-peptide reveals stabilization of the pro-peptide by the mature growth factor.
Hillger F; Herr G; Rudolph R; Schwarz E
J Biol Chem; 2005 Apr; 280(15):14974-80. PubMed ID: 15695507
[TBL] [Abstract][Full Text] [Related]
15. Unfolding and refolding pathways of a major kinetic trap in the oxidative folding of alpha-lactalbumin.
Salamanca S; Chang JY
Biochemistry; 2005 Jan; 44(2):744-50. PubMed ID: 15641801
[TBL] [Abstract][Full Text] [Related]
16. Revealing a concealed intermediate that forms after the rate-limiting step of refolding of the SH3 domain of PI3 kinase.
Wani AH; Udgaonkar JB
J Mol Biol; 2009 Mar; 387(2):348-62. PubMed ID: 19356591
[TBL] [Abstract][Full Text] [Related]
17. Probing conformational changes in orphan nuclear receptor: the NGFI-B intermediate is a partially unfolded dimer.
Garcia W; Figueira AC; de Oliveira Neto M; de Guzzi CA; Buzzá HH; Portugal RV; Calgaro MR; Polikarpov I
Biophys Chem; 2008 Oct; 137(2-3):81-7. PubMed ID: 18676081
[TBL] [Abstract][Full Text] [Related]
18. Effect of signal peptide on the stability and folding kinetics of maltose binding protein.
Beena K; Udgaonkar JB; Varadarajan R
Biochemistry; 2004 Mar; 43(12):3608-19. PubMed ID: 15035631
[TBL] [Abstract][Full Text] [Related]
19. Accumulation of partly folded states in the equilibrium unfolding of ervatamin A: spectroscopic description of the native, intermediate, and unfolded states.
Nallamsetty S; Dubey VK; Pande M; Ambasht PK; Jagannadham MV
Biochimie; 2007 Nov; 89(11):1416-24. PubMed ID: 17658212
[TBL] [Abstract][Full Text] [Related]
20. Conformational characterization of nerve growth factor-β reveals that its regulatory pro-part domain stabilizes three loop regions in its mature part.
Trabjerg E; Kartberg F; Christensen S; Rand KD
J Biol Chem; 2017 Oct; 292(40):16665-16676. PubMed ID: 28798232
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]