Related Publications

The thioredoxin domain of Neisseria gonorrhoeae PilB can use electrons from DsbD to reduce downstream methionine sulfoxide reductases.
N. Brot , J.-F Collet, L.C. Johnson, T.J. Jonsson, H. Weissbach, WT. Lowther.
J. Biol. Chem. 281 (2006), 32668-32675.

Pathways of disulfide bond formation in Escherichia coli.
J. MESSENS, J.-F. COLLET,
Int. J. Biochem Cell Biol. 38 (2006), 1050-1062.


Evidence for conformational changes within DsbD:  Possible role for  membrane-embedded proline residues.
HINIKER, D. VERTOMMEN, J.C.A. BARDWELL, J.-F. COLLET,
J. Bacteriology, 188 (2006), 7317-7320.

Copper stress causes an in vivo requirement for the disulfide isomerase DsbC.
A. Hiniker, J.F. Collet, J.C. Bardwell,
J Biol Chem. 280 (2005), 33785-33791.

The crystal structure of TrxA(CACA) : insights into the formation of a [2Fe-2S] iron sulfur cluster in an E. coli thioredoxin mutant.
J.F. Collet, D. Peisach, J.C. Bardwell and Z. Xu,
Protein science 14 (2005), 1863-1969

Engineering a de novo pathway for the formation of protein disulfide bonds in bacteria.
L. Masip, J.L. Pan, S. Haldar, J. Penner-Hahn, M. Delisa, G. Georgiou, J. Bardwell, J.-F. Collet.
Science 303 (2004) 1185-1189

Thioredoxin 2, an oxidative-stress induced protein, contains a high affinity zinc binding site.
J.F. COLLET, J.C. D’Souza, U. Jakob, J.C.B. BARDWELL
J. Biol. Chem. 278 (2003), 45325-45332

Oxidative protein folding in bacteria.
J.F. COLLET, J.C.B. BARDWELL,
Mol. Microbiol., 44 (2002), 1-8.    
                                                            

Disulfides out of thin air.                                                                             
J.F. COLLET, J.C.B. BARDWELL,
Nature Struct. Biol. 9(2002), 2-3.

Reconstitution of a disulfide isomerization system.                                      
J.-F. COLLET, J. RIEMER, M.W. BADER, J.C. BARDWELL
J. Biol. Chem., 277 (2002), 26886-26892 

Oxidative  protein folding in bacteria.
J.F. COLLET, J.C. BARDWELL
NATO Science Series. In press.

Catalysis of disulfide bond formation in prokaryotes.
J.F. COLLET, J.C. BARDWELL
Protein Folding Handbook, Buchner, Kiefhaber (Eds), Wiley-VCH. In press.

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Other publications

How calcium inhibits the magnesium-dependent enzyme human phosphoserine phosphatase
Y. Peeraer, A. Rabijns, J.F. Collet, E. Van Schaftingen and C. De Ranter
Eur. J. Biochem. In press.

Mutations responsible for 3-phosphoserine phosphatase deficiency.
M. VEIGA-DA-CUNHA*, J.-F. COLLET*, B. PRIEUR, J. JAEKEN, Y. PEERAER, A. RABIJNS, 
E. VAN SCHAFTINGE(*co-first authors)
Eur. J. Human Genet. 12 (2004) 163-166

High resolution crystal structure of human phosphoserine phosphatase in open conformation.
Y. Peeraer, A. Rabijns, C. Verboven, J.F. Collet, E. Van Schaftingen, C. De Ranter
Acta Crystallogr. D, 59(2003), 971-977

Evidence for phosphotransferases phosphorylated on an aspartate residue in an N-terminal DXDX(T/V) motif.
J.-F. COLLET, V. Stroobant, E. Van Schaftingen,
Meth. Enzymol.,  354 (2002) 177-188

Crystallization and preliminary X-ray diffraction analysis of human phosphoserine phosphatase.
Y. Peeraer, A. Rabijns , C. Verboven, J.F. Collet, E. Van Schaftinghen, C.J. De Ranter,
Acta Crystallogr. D, 58(2002), 133-4

The 2,3-bisphosphoglycerate-independent phosphoglycerate mutase from Trypanosoma brucei: metal-ion dependency and phosphoenzyme formation,
J.-F. COLLET, V. Stroobant, E. Van Schaftingen
FEMS Microbiol. Lett., 204(2001), 39-44.

Mechanistic studies of phosphoserine phosphatase, an enzyme related to P-type ATPases,
J.-F. COLLET, V. STROOBANT, E. VAN SCHAFTINGEN,
J. Biol. Chem., 274 (1999), 33985-33990.

Kinetic properties and tissular distribution of mammalian phosphomannomutase isozymes,
M. PIRARD, Y. ACHOURI, J.-F. COLLET, E. SCHOLLEN, G. MATTHIJS, E. VAN SCHAFTINGEN,
Biochem. J., 339 (1999), 201-207.

Identification of the cDNA encoding human 6-phosphogluconolactonase, the enzyme catalyzing the second step of the pentose phosphate pathway,
F. COLLARD*, J.-F. COLLET*, I. GERIN, M. VEIGA-DA-CUNHA, E. VAN SCHAFTINGEN, (* co-first authors)
FEBS Lett., 459 (1999), 223-226.


A new class of phosphotransferases phosphorylated on an aspartate residue in an amino-terminal DXDX(T/V) motif.
J.-F. COLLET,  V. STROOBANT, M. PIRARD, G. DELPIERRE, E. VAN SCHAFTINGEN
J. Biol. Chem., 273 (1998), 14107-14112.


A new family of phosphotransferases related to P-type ATPases,
J.-F. COLLET, E. VAN SCHAFTINGEN, V. STROOBANT,
TIBS 23 (1998), 284.

Human L-3-phosphoserine phosphatase: sequence, expression and evidence for a phosphoenzyme intermediate,
J.-F. COLLET, I. GERIN, M.H. RIDER, M. VEIGA-DA-CUNHA, E. VAN SCHAFTINGEN
FEBS Lett., 408 (1997), 281-284.

Phosphoserine phosphatase deficiency in a patient with Williams syndrome,
J. JAEKEN, M. DETHEUX, J.-P. FRIJNS, J.-F. COLLET, PH. ALLIET, E. VAN SCHAFTINGEN,
J. Med. Gen., 34 (1997), 594-596.

Comparison of PMM1 with the phosphomannomutases expressed in rat liver and in human cells.
M. PIRARD, J.-F., COLLET, G. MATTHIJS, E. VAN SCHAFTINGEN,
FEBS Lett., 411 (1997), 251-254.

Sequence of a putative glucose 6-phosphate translocase, mutated in glycogen storage disease type Ib,
I. GERIN, M. VEIGA-DA-CUNHA, Y. ACHOURI, J.-F. COLLET, E. VAN SCHAFTINGEN, 
FEBS Lett., 419 (1997) 235-238. 

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