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Extract from the Register of European Patents

EP About this file: EP4043562

EP4043562 - MUTATED ARYLSULFATASE A WITH INCREASED STABILITY [Right-click to bookmark this link]
StatusThe application is deemed to be withdrawn
Status updated on  30.06.2023
Database last updated on 28.09.2024
FormerThe application has been published
Status updated on  15.07.2022
Most recent event   Tooltip30.06.2023Application deemed to be withdrawnpublished on 02.08.2023  [2023/31]
Applicant(s)For all designated states
Rheinische Friedrich-Wilhelms-Universität Bonn
Regina-Pacis-Weg 3
53113 Bonn / DE
[2022/33]
Inventor(s)01 / Matzner, Ulrich
53113 Bonn / DE
02 / Gieselmann, Volkmar
53347 Bonn-Alfter / DE
 [2022/33]
Representative(s)Kuttenkeuler, David
SKM-IP PartGmbB
Oberanger 45
80331 München / DE
[N/P]
Former [2022/33]Kuttenkeuler, David
Boehmert & Boehmert
Anwaltspartnerschaft mbB
Pettenkoferstrasse 22
80336 München / DE
Application number, filing date21157346.416.02.2021
[2022/33]
Filing languageEN
Procedural languageEN
PublicationType: A1 Application with search report 
No.:EP4043562
Date:17.08.2022
Language:EN
[2022/33]
Search report(s)(Supplementary) European search report - dispatched on:EP14.07.2021
ClassificationIPC:C12N9/16, A61K38/46
[2022/33]
CPC:
C12Y301/06008 (EP,IL,US); C12N9/16 (EP,IL,US); A61K38/00 (EP,IL,US);
A61P25/00 (US); C07K14/775 (US); C07K2319/01 (EP,IL);
C07K2319/31 (EP,IL,US) (-)
Designated contracting statesAL,   AT,   BE,   BG,   CH,   CY,   CZ,   DE,   DK,   EE,   ES,   FI,   FR,   GB,   GR,   HR,   HU,   IE,   IS,   IT,   LI,   LT,   LU,   LV,   MC,   MK,   MT,   NL,   NO,   PL,   PT,   RO,   RS,   SE,   SI,   SK,   SM,   TR [2022/33]
Extension statesBANot yet paid
MENot yet paid
Validation statesKHNot yet paid
MANot yet paid
MDNot yet paid
TNNot yet paid
TitleGerman:MUTIERTE ARYLSULFATASE A MIT ERHÖHTER STABILITÄT[2022/33]
English:MUTATED ARYLSULFATASE A WITH INCREASED STABILITY[2022/33]
French:ARYLSULFATASE A MUTÉE PRÉSENTANT UNE STABILITÉ AMÉLIORÉE[2022/33]
Examination procedure18.02.2023Application deemed to be withdrawn, date of legal effect  [2023/31]
14.03.2023Despatch of communication that the application is deemed to be withdrawn, reason: examination fee not paid in time  [2023/31]
Fees paidPenalty fee
Additional fee for renewal fee
28.02.202303   M06   Not yet paid
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Patent Court		 See the Register of the Unified Patent Court for opt-out data
Responsibility for the accuracy, completeness or quality of the data displayed under the link provided lies entirely with the Unified Patent Court.
Documents cited:Search[ID]WO2018141958  (UNIV BONN RHEINISCHE FRIEDRICH WILHELMS [DE]) [ID] 1-16 * the abstract; page 9455 * * page 27 - page 28; examples 5,6; claim -; sequence 4 *;
 [I]  - VON BÜLOW RIXA ET AL, "Defective Oligomerization of Arylsulfatase A as a Cause of Its Instability in Lysosomes and Metachromatic Leukodystrophy", JOURNAL OF BIOLOGICAL CHEMISTRY, US, (20020102), vol. 277, no. 11, doi:10.1074/jbc.M111993200, ISSN 0021-9258, pages 9455 - 9461, XP055820743 [I] 1-16 * page 9458, column l, paragraph 1 * * the abstract * * abstract; page 9457, paragraph last - column r; figure 3 *

DOI:   http://dx.doi.org/10.1074/jbc.M111993200
 [I]  - VAGEDES PETER ET AL, "Driving Forces of Protein Association: The Dimer-Octamer Equilibrium in Arylsulfatase A", BIOPHYSICAL JOURNAL, AMSTERDAM, NL, (20021201), vol. 83, no. 6, doi:10.1016/S0006-3495(02)75311-3, ISSN 0006-3495, pages 3066 - 3078, XP055820736 [I] 1-16 * abstract; page 3066 - page 3067 * * page 3069, column l, paragraph 4 - column r; figures 6,7 *

DOI:   http://dx.doi.org/10.1016/S0006-3495(02)75311-3
 [I]  - SIMONIS HEIDI ET AL, "Evolutionary redesign of the lysosomal enzyme arylsulfatase A increases efficacy of enzyme replacement therapy for metachromatic leukodystrophy", HUMAN MOLECULAR GENETICS, vol. 28, no. 11, doi:10.1093/hmg/ddz020, ISSN 0964-6906, (20190601), pages 1810 - 1821, URL: https://watermark.silverchair.com/ddz020.pdf?token=AQECAHi208BE49Ooan9kkhW_Ercy7Dm3ZL_9Cf3qfKAc485ysgAAAtQwggLQBgkqhkiG9w0BBwagggLBMIICvQIBADCCArYGCSqGSIb3DQEHATAeBglghkgBZQMEAS4wEQQMX7200E1paP41bFeQAgEQgIICh3mGLWSXi8dGKm-JKCAsgA1uC5gSwbz_ZZPVDlhrvam_Kwq0-DDt38HM0cimWxp8i0YdOzKops95bt9EVvhSXRcPeS7lS, (20210705), XP055821250 [I] 1-16 * page 1811 - page 1812 *

DOI:   http://dx.doi.org/10.1093/hmg/ddz020
 [I]  - LUKATEKA G ET AL, "Crystal Structure of Human Arylsulfatase A: The Aldehyde Function and the Metal Ion at the Active Site Suggest a Novel Mechanism of Sulfate Ester Hydrolysis", BIOCHEMISTRY,, vol. 37, doi:10.1021/BI9714924, ISSN 0006-2960, (19980101), pages 3654 - 3664, (19980228), XP008104159 [I] 1-16 * page 3662, column r, paragraph 3 - paragraph 5 *

DOI:   http://dx.doi.org/10.1021/bi9714924
 [AD]  - SEVIN C ET AL, "Enzyme, cell and gene-based therapies for metachromatic leukodystrophy", JOURNAL OF INHERITED METABOLIC DISEASE, KLUWER ACADEMIC PUBLISHERS, DO, (20070308), vol. 30, no. 2, doi:10.1007/S10545-007-0540-Z, ISSN 1573-2665, pages 175 - 183, XP019478094 [AD] 1-16 * the whole document *

DOI:   http://dx.doi.org/10.1007/s10545-007-0540-z
by applicantUS6534300
 US6537785
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