DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Application Status
The preliminary amendment filed October 18, 2024 is acknowledged. Claims 178-193 are pending and under examination.
Priority
Applicant's claim for the benefit of a prior-filed application under 35 U.S.C. 119(e) or under 35 U.S.C. 120, 121, 365(c), or 386(c) is acknowledged. Applicant has not complied with one or more conditions for receiving the benefit of an earlier filing date under 35 U.S.C. 119(e) as follows:
The later-filed application must be an application for a patent for an invention which is also disclosed in the prior application (the parent or original nonprovisional application or provisional application). The disclosure of the invention in the parent application and in the later-filed application must be sufficient to comply with the requirements of 35 U.S.C. 112(a) or the first paragraph of 35 U.S.C. 112 (pre-AlA). See Transco Products, Inc. v. Performance Contracting, Inc., 38 F.3d 551, 32 USPQ2d 1077 (Fed. Cir. 1994).
The disclosure of the prior-filed application, Application No. 62674940 fail(s) to provide adequate support or enablement in the manner provided by 35 U.S.C. 112(a) for one or more claims of this application. The applications fail to provide support for the claims under examination, since there is no disclosure therein of modulating transcription of a gene comprising a trinucleotide repeat sequence CTG including in the genes DMPK or TCF4. The first evidence of support for the claimed method is in the PCT application PCT/US2019/033624 (filed May 22, 2019). As such, the effective filing date for all claims is May 22, 2019.
Claim Rejections - 35 USC § 112(a)
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 178-193 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
MPEP 2163.II.A3.(a).(i) states, “whether the specification shows that applicant was in possession of the claimed invention is not a single, simple determination, but rather is a factual determination reached by considering a number of factors. Factors to be considered in determining whether there is sufficient evidence of possession include the level of skill and knowledge in the art, partial structure, physical and/or chemical properties, functional characteristics alone or coupled with a known or disclosed correlation between structure and function, and the method of making the claimed invention.”
Claim 178 recites the limitation "the second terminus comprises a protein-binding moiety capable of binding to a regulatory molecule that modulates an expression of the gene comprising the nucleotide repeat sequence CTG" in the definition for a transcription modulator molecule having a first terminus, a second terminus, and an oligomeric linker moiety, in the method for which the specification does not provide an adequate written description to convey that the inventors where in possession of the full scope of the claimed invention.
Regarding the requirement for adequate written description of chemical entities, Applicant's attention is directed to the MPEP §2163. In particular, Regents of the University of California v. Eli Lilly & Co., 119 F .3d 1559, 1568 (Fed. Cir. 1997), cert. denied, 523 U.S. 1089, 118 S. Ct. 1548 (1998), holds that an adequate written description requires a precise definition, such as by structure, formula, chemical name, or physical properties, "not a mere wish or plain for obtaining the claimed chemical invention." Eli Lilly, 119 F.3d at 1566. The Federal Circuit has adopted the standard set forth in the Patent and Trademark Office ("PTO") Guidelines for Examination of Patent Applications under the 35 U.S.C. 112.1 "Written Description" Requirement ("Guidelines"), 66 Fed. Reg. 1099 (Jan. 5, 2001 ), which state that the written description requirement can be met by "showing that an invention is complete by disclosure of sufficiently detailed, relevant identifying characteristics," including, inter aria, "functional characteristics when coupled with a known or disclosed correlation between function and structure ... " Enzo Biochem, Inc. v. Gen-Probe Inc., 296 F.3d 316, 1324-25 (Fed. Cir. 2002) (quoting Guidelines, 66 Fed. Reg. at 1106 (emphasis added)). Moreover, although Eli Lilly and Enzo were decided within the factual context of DNA sequences, this does not preclude extending the reasoning of those cases to chemical structures in general. Univ. of Rochester v. G.D. Searle & Co., 249 Supp. 2d 216, 225 (W.D.N.Y. 2003). Lastly, For claims drawn to a genus, MPEP 2163.II.A3.(a).(ii) states, “written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species” where “representative number of species' means that the species which are adequately described are representative of the entire genus. Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus.”
Medicinal chemistry and pharmacology are unpredictable areas. Even carefully designed transcription modulator molecules do not always function as expected. It is generally unpredictable whether a molecule would possess the ability to modulate the expression of a specific gene since its modulation depends on the context in which it binds DNA, e.g., promoter vs enhancer vs 1st intron vs 3’ UTR. For strong modulation, for example, some structure activity-relationship may be ascertained from structurally similar derivatives; however, the degree of structural similar must be high in order to expect similar properties. For few or untested compounds, modulating the expression of any particular gene, especially when it does not bind promoter is largely unpredictable.
The Specification provides a laundry list of small molecules that have previously been shown to bind various DNA modifiers (Table 2). However, for at least some of them, the compounds are known inhibitors of the protein they bind. For instance, curcumin is a known inhibitor of the p300/CBP histone aceytyltransferase (Balasubramanyam et al., Journal of Biological Chemistry (2004), 279: 51163-51171). Although p300/CBP would be recruited to the CTG repeat if curcumin was conjugated to a CTG-binding polyamide, the p300/CBP protein would be inhibited and there might not be any change in the chromatin structure or transcriptional activity of the CTG-containing gene. As such, curcumin would not predictably function as “a protein-binding moiety capable of binding to a regulatory molecule that modulates expression of the gene”.
The claimed method requires the “protein-binding moiety” to bind/recruit the regulator molecule, but not inhibit its function at the CTG site. Given that many or even most of the small molecules in Table 2 are inhibitors of the proteins they bind, the Specification does not provide sufficient written description of molecules that could function as claimed for the second terminus.
Claims 179-180 and 187-193 do not reduce the genus size of the “protein-binding moieties capable of binding to a regulator molecule” and are not sufficiently described for the reasons recited above for claim 178.
Also, regrading claims 189-193, it is noted that the CTG-expansion occurs in the 3’ UTR of the DMPK gene and the first intron of the TCF4 gene. There is no evidence either in the Specification or in the prior art that recruiting chromatin-modifiers to the 3’ UTR or first intron of the DMPK and TCF4 genes, respectively, have any effect on the transcription of the respective genes. Therefore, it was highly unpredictable which enzymes should even be recruited to the CTG-expansion to reduce DMPK and TCF4 expression, and in turn, what the protein-binding moieties should be in order to reduce transcription of the DMPK and TCF4 genes and treat DM1 or FECD.
Claim 181 limits the regulatory molecules of which the protein-binding moiety binds. However, the claims still do not name the protein-binding moiety by name or structure, the and laundry list of small molecules in Table A which were addressed above for claim 178, could not predictably recruit the regulator molecule such that there would be capable of modulating transcription of the CTG-containing gene.
Claim 182 requires the protein-binding moiety to be an inhibitor of known transcriptional regulators. It is not known how the regulator would function at the CTG containing gene if it were being recruited by an inhibitor. As such using an inhibitor to recruit a regulator would not predictably result in “an agent having regulatory molecule that is capable of modulating expression of the CTG-comprising gene”.
Claims 183-184 only further limit the protein-binding moiety by what it is not. The Specification only provides a working example for JQ1 and BRD4 (i.e., a bromodomain protein). Thus, claims 183-184 remove the options for the only example for which there would be a predictable recruitment of a protein to the CTG-comprising region.
Claims 185-186 recite additional functional language for the protein-binding moiety and regulatory molecule without providing any structural limitations. As such, they are not sufficiently described for the reasons recited above for claim 178.
Claim Rejections - 35 USC § 102
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claims 178-182, 185-188 and 191-192 is rejected under 35 U.S.C. 102(a)(1) and 102(a)(2) as being anticipated by Ansari (US 20180280541 A1, published October 4, 2018, filed March 29, 2018). Claim 185 is evidenced by Tocris ((+)-JQ1, https://www.tocris.com/products/plus-jq1_4499 [retrieved July 10, 2026]).
As indicated above in paragraph 5, the effective filing date of the claimed invention is May 22, 2019. The Ansari reference has a single common inventor with the examined application. The Ansari reference names two additional inventors. As such the Ansari reference is prior art under 102(a)(1) and 102(a)(2).
Regarding claim 178, 187 and 188, Ansari teaches DM type 1 is caused by a CTG nucleotide expansion with the DMPK gene ([0080]). Ansari teaches the present technology related to methods for modulating gene expression of DMPK1 using an agent with the formula A-L-B, wherein A is a Brd4 binding moiety (i.e., a second terminus comprising a protein-binding moiety capable of binding the regulatory molecule Brd4), wherein in B is a polyamide that specifically binds to CTG repeats (i.e., a first terminus comprising a DNA-binding moiety capable of noncovalently biding to a CTG repeat sequence), wherein L is a linker ([0081], Claim 1). Ansari teaches the structure of the CTG repeat binding moiety (Fig 14-15). Ansari teaches contacting a cell with the agent for modulating expression (claim 6).
Regarding claim 179, Ansari teaches the CTG-binding moieties are hairpin polyamides (Fig 14-15).
Regarding claim 180, Ansari teaches the CTG-repeats in DM type 1 in the DMPK gene are over 38 or over 49 repeats ([0080]).
Regarding claims 181-182, Ansari teaches the protein-binding moiety JQ1 binds and recruits Brd4 (i.e., a bromodomain-containing protein) ([0081], Fig 12) and is a bromodomain inhibitor ([0087]).
Regarding claim 185, Ansari is silent regarding the affinity between JQ1 and Brd4. However, Tocris teaches that JQ1 binds Brd4 with an affinity of 49 nM (i.e., less than 200 nM). Thus, the CTG-binding polyamide-linker-JQ1 agent taught in Ansari inherently comprised a protein-binding moiety that bound its regulatory molecule with an affinity less than 200 nM.
Regarding claim 186, Ansari teaches the linker of the present technology is PEG6, which has a length of ~ 27 Angstroms ([0034], Fig 5).
Regarding claims 191-192, Ansari teaches using the CTG-targeted polyamide-linker-JQ1 agent for treating DM type 1 ([0206]).
Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 178-188 and 191-192 are rejected under 35 U.S.C. 103 as being unpatentable over Nagase (US 20110160399 A1) in view of Nageshwaran (Nageshwaran et al., Frontiers in Neurology (2015), 6:262, pages 1-9) and Kang (JeenJoo Sophia Kang. Targeting DNA repeat sequences with Py-Im polyamides. California Institute of Technology, 2015). Claim 185 is evidenced by MedChemExpress (Vorinostat (Synonyms: SAHA; Suberoylanilide hydroxamic acid), www.medchemexpress.com/Vorinostat.html, [retrieved July 10, 2026]). Claim 186 is evidenced by Bioquest (AAT Bioquest, SMPEG2, https://www.aatbio.com/products/smpeg2, [retrieved July 13, 2026]).
Regarding claim 178-179, 181-182 and 187-188, Nagase teaches a gene-specific histone modification regulator comprising conjugates between a hairpin polyamide (i.e., a first terminus comprising a DNA-binding moiety capable of noncovalently binding to a specific sequence) and a histone modification regulator binding molecule (i.e., a second terminus comprising a protein binding moiety capable of binding to a regulatory molecule) (Abstract; structures 1-3). Nagase teaches conjugating a polyamide targeting the p16 tumor suppressor gene (abbreviated PIP) to SAHA, an inhibitor of histone deacetylases (HDACs) ([0008], [0116]-[0117]). Nagase also teaches a linker between PIP and SAHA comprising PEG ([0165]). Nagase teaches the PIP-PEG-SAHA conjugate had anti-HDAC activity (i.e., SAHA could bind to HDAC) ([0169]). Nagase teaches contacting cells with the PIP-SAHA conjugates and inhibited cell proliferation (i.e., modulated p16 transcription ([0172]-[0174]). Nagase teaches that polyamides that target any desired sequences can be designed according to known combinations, for example, a Pyrrole/Imidazole pair binds to a G-C pair ([0083]). Nagase suggests using polyamide-inhibitor conjugates to target a variety of genes (embodiment 18).
Nagase does not teach a polyamide structure that can bind a CTG repeat in the DMPK gene.
Nageshwaran teaches that myotonic dystrophy type 1 (DM1) is caused by a CTG expansion in the 3’ UTR of the DMPK 1 gene (page 5, ¶2). Nageshwaran teaches the CTG repeat has been shown to influence chromatin, making it less permissive for transcription (page 5, ¶3). Nageshwaran teaches the CTG expansion renders a SIX5 enhancer present in the DMPK 3’ UTR inaccessible to transcription factors causing downregulation of SIX5 expression (page 5, ¶3). Nageshwaran teaches repression of SIX5 gene leads to development of cataracts in mice, which is a dominant symptom of DM1 (page 5, ¶3).
Kang teaches the structure of a Py-Im hairpin polyamide targeted to the CTG repeat of DM1 (Chapter 4, title; Figure 4.2).
It would have been obvious to one skilled in the art before the effective filing date of the claimed invention to have used Kang’s CTG-targeted polyamide in place of the p16-targeted polyamide in Nagase’s PIP-PEG-SAHA to modulate histone acetylation and gene transcription in CTG-expanded cells. It would have amounted to the simple combination of elements by known means to yield predictable results. The skilled artisan would have predicted Kang’s polyamide structure could be used in Nagase’s PIP-PEG-SAHA conjugate because Nagase makes clear that polyamides are routine to design and synthesize and proposes using PIP-PEG-SAHA conjugates to a variety of gene targets. The skilled artisan would have been motivated to use a DMPK-(CTG expansion)-targeted PIP-PEG-SAHA agent in DM1 cells to promote euchromatin structure around the 3’ UTR, thereby increasing expression of a gene element affected by the CTG expansion as suggested by Nageshwaran. It would have been entirely predictable that the DMPK-(CTG expansion)-targeted PIP-PEG-SAHA could increase expression by inhibiting histone deacetylation in DMPK CTG expanded cells because Nagase demonstrated increase p16 expression when targeting PIP-PEG-SAHA to the p16 promoter.
Regarding claim 180, Nageshwaran teaches CTG repeats of over 50 results in DM1 (page 5, ¶2).
Regarding claims 183-184, the obvious DMPK-(CTG expansion)-targeted PIP-PEG-SAHA does not comprise a molecule that binds to a bromodomain protein or any of the moieties recited in claim 184.
Regarding claim 185, Nagase is silent regarding the affinity between SAHA and HDAC. However, MedChemExpress teaches that SAHA has affinity for HDAC1 and HDAC3 from 10-20 nM. Therefore, the obvious DMPK-(CTG expansion)-targeted PIP-PEG-SAHA conjugate inherently comprises a protein-binding moiety that binds a regulator molecule with affinity of less than 200 nM.
Regarding claim 186, Nagase teaches the PEG linker in PIP-PEG-SAHA is two units ([0165]), but is silent on the length of the PEG2 linker. Bioquest teaches that an SM-PEG2 linker is about 17.6 angstroms (page 1), therefore the PEG2 linker alone in Nagase must inherently have been less than 50 Angstroms.
Regarding claims 191-192, it also would have been obvious before the effective filing date of the claimed invention to have use the obvious DMPK-(CTG expansion)-targeted PIP-PEG-SAHA agent for the treatment of DM1. The skilled artisan would have predicted the obvious agent could treat DM1 because it would have been predicted to promote euchromatin structure around the 3’ UTR, thereby increasing expression of a SIX5, which is affected by the DMPK CTG expansion as taught by Nageshwaran.
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claims 178-182 and 185-188 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-30 of U.S. Patent No. 11759533.
Patented claim 5 recites a method for modulating mRNA levels produced from a gene in a cell comprising contacting the cell with an effective amount of the agent of claim 1, wherein the gene comprises more than one repeat of the target oligonucleotide sequence. Patented claim 6 recites wherein the gene comprises at least about 30 repeats of the target oligonucleotide sequence. Patented claim 29 recites wherein the gene is dystrophia myotonica protein kinase (DMPK). Patented claim 1 recites An agent having a formula A-L-B, wherein: -L- is a linker; A- is a Brd4 binding moiety (i.e., a a second terminus comprising a protein-binding moiety capable of binding a regulator molecule that modulates expression of the gene comprising a CTG repeat)…, and wherein the nucleic acid binding moiety —B is a polyamide that specifically binds to the one or more repeats of the target oligonucleotide sequence selected from the group consisting of CGG, CTG, and CCTG (i.e., a first terminus comprising a DNA-binding moiety capable of binding the CTG repeat sequence). Patented claims 16 and 17 recite linkers that are oligomeric. Therefore, the patented claims anticipate examined claims 178-182 and 185-188.
Claims 178, 180-182 and 185-186 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 6-7, 9-11, 13, 18-19, 21, 28, 31, 34, 39, 62, 65-66 of copending Application No. 18218325 (reference application).
Copending claim 1 recites a method for modulating transcription of a gene that comprises at least one oligonucleotide repeat comprising a sequence of CGG, CTG, or CCTG by contacting a cell comprising the gene with an agent having a formula A-L-B, wherein L is a linker, B is a nucleic acid binding moiety, and A is a bromodomain binding moiety (i.e., the instantly claimed second terminus), thereby modulating transcription of the gene in the cell. Copending claims 15 recites wherein the linker comprises at least 10 contiguous atoms (i.e., has an oligomeric backbone). Copending claims 17 recites wherein the at least one oligonucleotide repeat comprises at least about 6 repeats, at least about 30 repeats. Copending claim 24 recites A method of treating a subject with a genetic condition associated with a gene comprising a plurality of repeats of a CGG, CTG, or CCTG oligonucleotide sequence, comprising administering to the subject a therapeutically effective amount of a compound of claim 5. Therefore the copending claims anticipate examined claims 178, 180-182, 185-186.
Claims 178-182, 185-188 and 191-193 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 6-7, 9-11, 13, 18-19, 21, 28, 31, 34, 39, 62, 65-66 of copending Application No. 18256864 (reference application).
Copending claim 1 recites A transcription modulator molecule having a first terminus, a second terminus, and a linker moiety, or a pharmaceutically acceptable salt or solvate thereof, wherein: a) the first terminus comprises a DNA-binding moiety capable of noncovalently binding to a nucleotide repeat sequence CTG; b) the second terminus comprises a protein-binding moiety capable of binding to a regulatory molecule that modulates an expression of a gene comprising the nucleotide repeat sequence CTG; and c) the linker moiety connecting the first terminus and the second terminus. Copending claim 21 recites various oligomeric linkers. Copending claims 18 recites wherein the linker has a length of less than about 50 Angstroms. Copending claim 34 recites wherein the second terminus is selected from a bromodomain inhibitor, a BPTF inhibitor, a methylcytosine dioxygenase inhibitor, a DNA demethylase inhibitor, a helicase inhibitor, an acetyltransferase inhibitor, a histone deacetylase inhibitor, a CDK-9 inhibitor, a positive transcription elongation factor inhibitor, and a polycomb repressive complex inhibitor. Copending claims 65-66 recite A method of treating myotonic dystrophy type 1 (DM1) or Fuchs' Endothelial Corneal Dystrophy (FECD) in a subject in need thereof, comprising administering to the subject a therapeutically effective amount of a transcription modulator molecule of claim 1. Therefore the copending claims anticipate examined claims 178-182, 185-188 and 191-193.
Conclusion
No claims are allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to CATHERINE KONOPKA whose telephone number is (571)272-0330. The examiner can normally be reached Mon - Fri 7- 4.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Ram Shukla can be reached at (571)272-0735. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/CATHERINE KONOPKA/Primary Examiner, Art Unit 1635
Prosecution Insights