Erratum to: Strategies for identifying synthetic peptides to act as ...

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Sep 13, 2013 - The Julius Friedrich Cohnheim Laboratory of Phagocyte. Research, Department of Clinical Microbiology and. Immunology, Sackler School of ...

Cell. Mol. Life Sci. (2013) 70:4199–4200 DOI 10.1007/s00018-013-1473-3

Cellular and Molecular Life Sciences

ERRATUM

Erratum to: Strategies for identifying synthetic peptides to act as inhibitors of NADPH oxidases, or ‘‘All that you did and did not want to know about Nox inhibitory peptides’’ Iris Dahan · Edgar Pick 

Published online: 13 September 2013 © Springer Basel 2013

Erratum to: Cell. Mol. Life Sci. (2012) 69:2283–2305 DOI 10.1007/s00018‑012‑1007‑4 The original publication of this article unfortunately contained an error in figure. In page number 2286, Fig. 3: 1. The activation domain in p67phox (residues 199–210), was mislabelled as D. This is now corrected to AD; 2. The numbering of residues in the SH3-N region of p67phox was erroneously shown as starting at 243 and ending at 289. The correct numbering should start with 243 and end with 298. The correct figure is given below.

The online version of the original article can be found under doi:10.1007/s00018-012-1007-4. I. Dahan · E. Pick (*)  The Julius Friedrich Cohnheim Laboratory of Phagocyte Research, Department of Clinical Microbiology and  Immunology, Sackler School of Medicine, Tel Aviv University, Tel Aviv, Israel e-mail: [email protected]

13

4200

I. Dahan, E. Pick 4

121

p47phox 1

3

p67phox 1

36

1

1

40

Switch I

TPR 4

60

AD

67

PRR

Switch II

284 292 340

SH3-C

298

351

PX

429

135 159 162

460

228 SH3

515 526

SH3-C

183 188 189

p67phox BD 2

173

390

PRR

PB1

Insert

136

363 368

polybasic

SH3-N

124

Fig. 3  ‘‘The mechanics - those who make the engine work’’. Mapping the protein–protein interaction domains in the cytosolic NADPH oxidase components. The presentation of the domains was inspired by [4]. PX phox homology domain, SH3-N N-terminal src 3 homology domain, SH3-C C-terminal src 3 homology domain, PRR proline-rich

13

229

199- 226210 236 243

70 104 120 153

18

p40phox

214

SH3-N

TPR 1 TPR 2 TPR 3

30

Rac1

159

PX

polybasic

237

192 CLLL

192

329 PB1

339

region, TPR tetratricopeptide repeat, AD activation domain, PB1 Phox and Bem domain, Insert insert region characteristic of Rho proteins, p67phox BD2 second Rac-binding domain on p67phox (in addition to switch I), CLLL C-terminal residues in Rac1 involved in isoprenylation, carboxymethylation, and cleavage of the three leucines

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