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Extract from the Register of European Patents

EP About this file: EP1925664

EP1925664 - Artificial binding proteins based on a modified alpha helical region of ubiquitin [Right-click to bookmark this link]
StatusThe application is deemed to be withdrawn
Status updated on  15.05.2009
Database last updated on 25.09.2024
Most recent event   Tooltip15.05.2009Application deemed to be withdrawnpublished on 17.06.2009  [2009/25]
Applicant(s)For all designated states
Scil Proteins GmbH
Heinrich-Damerow-Strasse 1
06120 Halle/Saale / DE
[2008/22]
Inventor(s)01 / Schräml, Michael, Dr.
Carl-von-Ossietzky-Strasse 22
D-06114 Halle / DE
02 / Fiedler, Erik, Dr.
Körnerstrasse 26
D-06114 Halle / DE
 [2008/22]
Representative(s)Isarpatent
Patent- und Rechtsanwälte Barth
Charles Hassa Peckmann & Partner mbB
Friedrichstrasse 31
80801 München / DE
[N/P]
Former [2008/22]Reinhard - Skuhra - Weise & Partner
Patent- und Rechtsanwälte Friedrichtstrasse 31
80801 München / DE
Application number, filing date06124137.815.11.2006
[2008/22]
Filing languageEN
Procedural languageEN
PublicationType: A1 Application with search report 
No.:EP1925664
Date:28.05.2008
Language:EN
[2008/22]
Search report(s)(Supplementary) European search report - dispatched on:EP03.07.2007
ClassificationIPC:C12N15/10, C07K14/47, G01N33/50
[2008/22]
CPC:
C07K14/00 (EP,US); G01N33/6803 (EP,US)
Designated contracting states[2009/06]
Former [2008/22]AT,  BE,  BG,  CH,  CY,  CZ,  DE,  DK,  EE,  ES,  FI,  FR,  GB,  GR,  HU,  IE,  IS,  IT,  LI,  LT,  LU,  LV,  MC,  NL,  PL,  PT,  RO,  SE,  SI,  SK,  TR 
TitleGerman:Künstliche Bindungsproteine auf Grundlage einer modifizierten alpha-Helix Region von Ubiquitin[2008/22]
English:Artificial binding proteins based on a modified alpha helical region of ubiquitin[2008/22]
French:Protéines de liaison artificielles basées sur une région modifiée de type hélice alpha de l'ubiquitine[2008/22]
Examination procedure29.11.2008Application deemed to be withdrawn, date of legal effect  [2009/25]
13.01.2009Despatch of communication that the application is deemed to be withdrawn, reason: examination fee not paid in time  [2009/25]
Fees paidPenalty fee
Additional fee for renewal fee
30.11.200803   M06   Not yet paid
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Documents cited:Search[DX]WO2004106368  (SCIL PROTEINS GMBH [DE], et al) [DX] 1-32 * the whole document *;
 [A]WO2005044845  (UNIV YALE [US], et al) [A] 1 * the whole document *;
 [A]WO2005059131  (UNIV YALE [US], et al) [A] * the whole document *;
 [X]  - YEH E T H ET AL, "Ubiquitin-like proteins: new wines in new bottles", GENE, ELSEVIER, AMSTERDAM, NL, (200005), vol. 248, no. 1-2, ISSN 0378-1119, pages 1 - 14, XP004198791 [X] 1-18,28 * the whole document *

DOI:   http://dx.doi.org/10.1016/S0378-1119(00)00139-6
 [X]  - ERMOLENKO DMITRI N ET AL, "Noncharged amino acid residues at the solvent-exposed positions in the middle and at the C terminus of the alpha-helix have the same helical propensity.", PROTEIN SCIENCE, (200306), vol. 12, no. 6, ISSN 0961-8368, pages 1169 - 1176, XP002437917 [X] 1-18,28 * the whole document *

DOI:   http://dx.doi.org/10.1110/ps.0304303
 [X]  - KRANTZ B A ET AL, "Discerning the Structure and Energy of Multiple Transition States in Protein Folding using psi-Analysis", JOURNAL OF MOLECULAR BIOLOGY, LONDON, GB, (20040319), vol. 337, no. 2, ISSN 0022-2836, pages 463 - 475, XP004493197 [X] 1-32 * the whole document *

DOI:   http://dx.doi.org/10.1016/j.jmb.2004.01.018
 [X]  - BOFILL ET AL, "Engineering Stabilising beta-Sheet Interactions into a Conformationally Flexible Region of the Folding Transition State of Ubiquitin", JOURNAL OF MOLECULAR BIOLOGY, LONDON, GB, (20051021), vol. 353, no. 2, ISSN 0022-2836, pages 373 - 384, XP005086541 [X] 1-18,28 * the whole document *

DOI:   http://dx.doi.org/10.1016/j.jmb.2005.08.044
 [A]  - YANG LORETTA ET AL, "Relationship between folding and function in a sequence-specific miniature DNA-binding protein.", BIOCHEMISTRY 24 MAY 2005, (20050524), vol. 44, no. 20, ISSN 0006-2960, pages 7469 - 7478, XP002437916 [A] * the whole document *

DOI:   http://dx.doi.org/10.1021/bi050121h
 [A]  - LOLADZE VAKHTANG V ET AL, "Both helical propensity and side-chain hydrophobicity at a partially exposed site in alpha-helix contribute to the thermodynamic stability of ubiquitin.", PROTEINS 1 JAN 2005, (20050101), vol. 58, no. 1, ISSN 1097-0134, pages 1 - 6, XP002437914 [A] * the whole document *

DOI:   http://dx.doi.org/10.1002/prot.20283
The EPO accepts no responsibility for the accuracy of data originating from other authorities; in particular, it does not guarantee that it is complete, up to date or fit for specific purposes.