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Items: 1 to 20 of 113

1.

Nuclear magnetic resonance characterization of the N-terminal thioredoxin-like domain of protein disulfide isomerase.

Kemmink J, Darby NJ, Dijkstra K, Scheek RM, Creighton TE.

Protein Sci. 1995 Dec;4(12):2587-93.

2.
3.

The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules.

Kemmink J, Darby NJ, Dijkstra K, Nilges M, Creighton TE.

Curr Biol. 1997 Apr 1;7(4):239-45.

4.

Functional properties of the individual thioredoxin-like domains of protein disulfide isomerase.

Darby NJ, Creighton TE.

Biochemistry. 1995 Sep 19;34(37):11725-35.

PMID:
7547904
5.

Identifying and characterizing a structural domain of protein disulfide isomerase.

Darby NJ, Kemmink J, Creighton TE.

Biochemistry. 1996 Aug 13;35(32):10517-28.

PMID:
8756708
7.
8.

Thioredoxin fold as homodimerization module in the putative chaperone ERp29: NMR structures of the domains and experimental model of the 51 kDa dimer.

Liepinsh E, Baryshev M, Sharipo A, Ingelman-Sundberg M, Otting G, Mkrtchian S.

Structure. 2001 Jun;9(6):457-71.

9.

Electrostatic interactions in the active site of the N-terminal thioredoxin-like domain of protein disulfide isomerase.

Kortemme T, Darby NJ, Creighton TE.

Biochemistry. 1996 Nov 19;35(46):14503-11.

PMID:
8931546
10.
11.

A 21-kDa C-terminal fragment of protein-disulfide isomerase has isomerase, chaperone, and anti-chaperone activities.

Puig A, Primm TP, Surendran R, Lee JC, Ballard KD, Orkiszewski RS, Makarov V, Gilbert HF.

J Biol Chem. 1997 Dec 26;272(52):32988-94.

12.

DSBC protein: a new member of the thioredoxin fold-containing family.

Frishman D.

Biochem Biophys Res Commun. 1996 Feb 27;219(3):686-9.

PMID:
8645242
13.

Structural elements responsible for transglutaminase activity of protein disulphide isomerases and thioredoxins.

Blaskó B, Mádi A, Fésüs L.

J Biol Regul Homeost Agents. 2004 Jan-Mar;18(1):1-8.

PMID:
15323354
14.

Molecular characterization of the principal substrate binding site of the ubiquitous folding catalyst protein disulfide isomerase.

Pirneskoski A, Klappa P, Lobell M, Williamson RA, Byrne L, Alanen HI, Salo KE, Kivirikko KI, Freedman RB, Ruddock LW.

J Biol Chem. 2004 Mar 12;279(11):10374-81. Epub 2003 Dec 18.

15.

Structural and functional relations among thioredoxins of different species.

Eklund H, Gleason FK, Holmgren A.

Proteins. 1991;11(1):13-28.

PMID:
1961698
16.

Identification and characterization of structural domains of human ERp57: association with calreticulin requires several domains.

Silvennoinen L, Myllyharju J, Ruoppolo M, Orrù S, Caterino M, Kivirikko KI, Koivunen P.

J Biol Chem. 2004 Apr 2;279(14):13607-15. Epub 2004 Jan 19.

17.

The relative protein disulphide isomerase (PDI) activities of gonadotrophins, thioredoxin and PDI.

Chew CC, Magallon T, Martinat N, Lecompte F, Combarnous Y, Gosling JP.

Biochem Soc Trans. 1995 May;23(2):394S. No abstract available.

PMID:
7672429
18.
19.

The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites.

Tian G, Xiang S, Noiva R, Lennarz WJ, Schindelin H.

Cell. 2006 Jan 13;124(1):61-73. Erratum in: Cell. 2006 Mar 10;124(5):1085-8.

20.

Peptide binding to protein disulfide isomerase occurs at a site distinct from the active sites.

Noiva R, Freedman RB, Lennarz WJ.

J Biol Chem. 1993 Sep 15;268(26):19210-7.

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