Format
Sort by
Items per page

Send to

Choose Destination

Links from PubMed

Items: 1 to 20 of 88

1.

Expanded monomeric intermediate upon cold and heat unfolding of phosphofructokinase-2 from Escherichia coli.

Baez M, Wilson CA, Ramírez-Sarmiento CA, Guixé V, Babul J.

Biophys J. 2012 Nov 21;103(10):2187-94. doi: 10.1016/j.bpj.2012.09.043. Epub 2012 Nov 20.

2.

Reversible unfolding of dimeric phosphofructokinase-2 from Escherichia coli reveals a dominant role of inter-subunit contacts for stability.

Baez M, Babul J.

FEBS Lett. 2009 Jun 18;583(12):2054-60. doi: 10.1016/j.febslet.2009.05.034. Epub 2009 May 22.

3.

The folding unit of phosphofructokinase-2 as defined by the biophysical properties of a monomeric mutant.

Ramírez-Sarmiento CA, Baez M, Zamora RA, Balasubramaniam D, Babul J, Komives EA, Guixé V.

Biophys J. 2015 May 5;108(9):2350-61. doi: 10.1016/j.bpj.2015.04.001.

4.

Unfolding pathway of the dimeric and tetrameric forms of phosphofructokinase-2 from Escherichia coli.

Baez M, Cabrera R, Guixé V, Babul J.

Biochemistry. 2007 May 22;46(20):6141-8. Epub 2007 May 1.

PMID:
17469854
5.

Folding kinetic pathway of phosphofructokinase-2 from Escherichia coli: a homodimeric enzyme with a complex domain organization.

Baez M, Wilson CA, Babul J.

FEBS Lett. 2011 Jul 21;585(14):2158-64. doi: 10.1016/j.febslet.2011.05.041. Epub 2011 May 27.

6.

Observation of solvent penetration during cold denaturation of E. coli phosphofructokinase-2.

Ramírez-Sarmiento CA, Baez M, Wilson CA, Babul J, Komives EA, Guixé V.

Biophys J. 2013 May 21;104(10):2254-63. doi: 10.1016/j.bpj.2013.04.024.

7.

Role of Cys-295 on subunit interactions and allosteric regulation of phosphofructokinase-2 from Escherichia coli.

Caniuguir A, Cabrera R, Báez M, Vásquez CC, Babul J, Guixé V.

FEBS Lett. 2005 Apr 25;579(11):2313-8.

8.

Kinetically robust monomeric protein from a hyperthermophile.

Mukaiyama A, Takano K, Haruki M, Morikawa M, Kanaya S.

Biochemistry. 2004 Nov 2;43(43):13859-66.

PMID:
15504048
9.

Folding of Escherichia coli DsbC: characterization of a monomeric folding intermediate.

Ke H, Zhang S, Li J, Howlett GJ, Wang CC.

Biochemistry. 2006 Dec 19;45(50):15100-10.

PMID:
17154548
10.

Crystallographic structure of phosphofructokinase-2 from Escherichia coli in complex with two ATP molecules. Implications for substrate inhibition.

Cabrera R, Ambrosio AL, Garratt RC, Guixé V, Babul J.

J Mol Biol. 2008 Nov 14;383(3):588-602. doi: 10.1016/j.jmb.2008.08.029. Epub 2008 Aug 22.

PMID:
18762190
11.

Stability and unfolding of reduced Escherichia coli glutaredoxin 2: a monomeric structural homologue of the glutathione transferase family.

Gildenhuys S, Wallace LA, Dirr HW.

Biochemistry. 2008 Oct 7;47(40):10801-8. doi: 10.1021/bi801272t. Epub 2008 Sep 13.

PMID:
18788752
12.

The unfolding pathway for Apo Escherichia coli aspartate aminotransferase is dependent on the choice of denaturant.

Deu E, Kirsch JF.

Biochemistry. 2007 May 15;46(19):5810-8. Epub 2007 Apr 11.

PMID:
17425331
13.

The partially folded homodimeric intermediate of Escherichia coli aspartate aminotransferase contains a "molten interface" structure.

Deu E, Dhoot J, Kirsch JF.

Biochemistry. 2009 Jan 20;48(2):433-41. doi: 10.1021/bi801431x.

PMID:
19099423
14.

Thermodynamic and structural analysis of the folding/unfolding transitions of the Escherichia coli molecular chaperone DnaK.

Montgomery D, Jordan R, McMacken R, Freire E.

J Mol Biol. 1993 Jul 20;232(2):680-92.

PMID:
8102181
15.
16.

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. Epub 2007 Jun 8.

PMID:
17658212
18.

Domain structure and denaturation of a dimeric Mip-like peptidyl-prolyl cis-trans isomerase from Escherichia coli.

Jana B, Bandhu A, Mondal R, Biswas A, Sau K, Sau S.

Biochemistry. 2012 Feb 14;51(6):1223-37. doi: 10.1021/bi2015037. Epub 2012 Feb 1.

PMID:
22263615
19.

Different unfolding pathways for mesophilic and thermophilic homologues of serine hydroxymethyltransferase.

Bhatt AN, Prakash K, Subramanya HS, Bhakuni V.

Biochemistry. 2002 Oct 8;41(40):12115-23.

PMID:
12356312
20.

Gamma S-crystallin of bovine and human eye lens: solution structure, stability and folding of the intact two-domain protein and its separate domains.

Wenk M, Herbst R, Hoeger D, Kretschmar M, Lubsen NH, Jaenicke R.

Biophys Chem. 2000 Aug 30;86(2-3):95-108.

PMID:
11026675

Supplemental Content

Support Center