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 .
Election/Restrictions
Applicant’s election without traverse of the following species: a nucleic acid within Genus T, SEQ ID NO: 15 within Genus N, and Amyotrophic Lateral Sclerosis (ALS) within Genus D, in the reply filed on 04/22/2026 is acknowledged.
Claim 25-31, 34-36, and 38-39 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected species, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 04/22/2026. It is noted the applicant asserts in the reply filed on 04/22/2026 that the election of a nucleic acid within Genus T reads on claims 32-36 and 41. However, applicant was further required to elect a single species within Genus N upon electing a nucleic acid species in Genus T; therefore, claims 34-36 respectively reciting antisense oligonucleotide, siRNA, and Ribozyme do not read on applicant’s elected species SEQ ID NO: 15 within Genus N. Thus, the examiner is withdrawing claims 34-36 as reading on non-elected species.
Claims 24, 32-33, 37, and 40-41 are under examination in this office action.
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.
The applicant claims priority to previously filed international application no. PCT/CA2022/050665 filed 04/29/2022 and US provisional application no. 63181452 filed 04/29/2021. The examiner finds support for all claimed limitations in the US provisional application and is considering 04/29/2021 as the effective filing date.
Information Disclosure Statement
The listing of references in the specification is not a proper information disclosure statement. 37 CFR 1.98(b) requires a list of all patents, publications, or other information submitted for consideration by the Office, and MPEP § 609.04(a) states, "the list may not be incorporated into the specification but must be submitted in a separate paper." Therefore, unless the references have been cited by the examiner on form PTO-892, they have not been considered.
The applicant lists references on pages 45-47. As stated above, the examiner is not considering them as a proper submission of an information disclosure statement.
Specification
The disclosure is objected to because it contains an embedded hyperlinks and/or other form of browser-executable code. Applicant is required to delete the embedded hyperlinks and/or other form of browser-executable code; references to websites should be limited to the top-level domain name without any prefix such as http:// or other browser-executable code. See MPEP § 608.01.
There are at least five occurrences that the examiner has identified, four on page 39 and one on page 47. The applicant is required to identify each and every occurrence the examiner has or has not noted and amend appropriately.
The use of the terms Lipofectamine 2000, NanoDrop, AlexaFluor, GraphPad Prism, FLUOVIEW, and among many others which is a trade name or a mark used in commerce, has been noted in this application. The term should be accompanied by the generic terminology; furthermore, the term should be capitalized wherever it appears or, where appropriate, include a proper symbol indicating use in commerce such as ™, SM , or ® following the term.
Although the use of trade names and marks used in commerce (i.e., trademarks, service marks, certification marks, and collective marks) are permissible in patent applications, the proprietary nature of the marks should be respected and every effort made to prevent their use in any manner which might adversely affect their validity as commercial marks.
There are numerous instances of such trade names without proper marks. Applicant is required to identify any and all occurrences the examiner has or has not noted and amend appropriately.
Claim Objections
Claim 40 is objected to because of the following informalities: it is missing the transition after the word “further” (for example, further comprising). Appropriate correction is required.
Claim Rejections - 35 USC § 112
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.
Claim 24 is 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.
Claim 24 (when considered with respect to the elected therapeutic of a nucleic acid within Genus T per the species election requirement) recites a method for treating a condition associated with TDP-43 toxicity in a subject, the method comprising administering to the subject an effective amount of a TDP-43 antagonist, wherein the TDP-43 antagonist is a substance or molecule that increases the endogenous expression of RGNEF or of a fragment of the RGNEF in the subject, thereby treating the condition associated with TDP-43 toxicity.
The recited “a substance or molecule” as claimed represents an open-ended functional genus defined by the desired result (increases the endogenous expression of RGNEF or of a fragment of the RGNEF in the subject) rather than any structure-function relationship. A person having ordinary skill in the art (PHOSITA) would recognize that this broad genus encompasses completely divergent structural modalities, including but not limited to: (1) small-molecule chemical compounds, (2) CRISPR complexes utilizing dCas9, (3) epigenome editing, (4) antisense oligonucleotide therapeutics, and (5) engineered zinc-finger or TALE transcription factors, Butterfield GL. et al., (Molecular Therapy; 33, 2104-2122, published 2025).
Furthermore, the phrase “a condition associated with TDP-43 toxicity” sets forth a broad genus of clinically and etiologically distinct neurodegenerative and neuromuscular pathologies that span different cell types. The genus includes but it not limited to: “amyotrophic lateral sclerosis (ALS), frontotemporal dementia (FTD), Alzheimer’s disease (AD), and limbic predominant age-related TDP-43 encephalopathy (LATE)”, Jo M et al. (Exp Mol Med 52, 1652–1662, published 10/13/2020). Furthermore, Jo et al., suggest “the molecular mechanism underlying TDP-43 propagation is still unclear” and “further in-depth studies are warranted to fully elucidate whether different propagation mechanisms occur in each of the various cell types in the central nervous system,” see conclusion.
To satisfy the written description requirement for a broad genus, the specification must disclose a representative number of species or identifying characteristics common to the members of the genus such that a PHOSITA can visualize or recognize the identity of the members of the genus.
A review of the specification reveals that the applicant does not provide structural characterization, working examples, or identification of specific species for small molecules, CRISPR platforms, epigenetic modifier, or engineered transcription factors capable of driving endogenous expression of RGNEF or a fragment of the RGNEF. The disclosure is limited vector-mediated delivery of exogenous transgenic copies of a specific N-terminal RGNEF leucine rich fragment in in vitro models and in invertebrate models. The specification lacks a representative number od species or a structural description linking these vast chemical modalities. Similarly, the specification fails to provide written description demonstrating that the claimed mechanism can treat distinct anatomical pathologies across the entire spectrum of TDP-43 proteinopathies, such as ALS, AD, FTD, and LATE.
Therefore, the applicant was not in possession of the broad genus of claimed methods as of the filing date.
Claim Rejections - 35 USC § 102
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
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 24, 32-33, and 41 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Withers BM. (Western University. Electronic Thesis and Dissertation Repository. 6012. Published 01/25/2019) as evidenced by Cheung K. et al., (Molecular and Cellular Neuroscience, Volume 82, Pages 88-95, published 05/08/2017).
Regarding claim 24, 32-33, and 41, Withers teaches a method of administering a nucleic acid construct comprising a nucleic acid sequence encoding for a peptide comprising the N-terminus domain of the RGNEF, “L-Rich” (i.e., “an amino-terminal fragment of RGNEF containing a Leucine-rich domain”) to a subject exhibiting human TDP-43 neurotoxicity to treat/ameliorate a pathological condition, see abstract, Figure 3 page 15, Figure 10A page 45, and page 72. Specifically, Withers teaches double transgenic Drosophila lines carrying both the L-Rich transgene and human wild-type TDP-43 transgene configured for either pan-neuronal expression (Elav-gal4), motor neuron expression (D42-gal4), or expression in the eye (GMR-gal4) to allow for more direct observation of pathology, see Pg. 63. Withers teaches that L-Rich treats conditions associated with TDP-43 toxicity; for example, L-Rich in the double transgenic Drosophila lines was able to rescue lifespan (“flies expressing the Leucine-rich domain of RGNEF and TDP-43 showed an increased lifespan compared to single transgenic TDP-43,” See Pg 65 and Figure 26-27); mitigate motor deficit (“L-Rich expression reduced motor deficit induced by TDP-43,” See Page 69 and Figure 28), and rescue neurodegeneration (“Leucine-rich domain of RGNEF decreases eye degeneration of TDP-43 in flies with eye specific expression,” See Pg. 71 and Figure 29). Withers teaches that L-Rich interacts/binds with TDP-43 and modulates its activity, thereby providing a protective role in conditions associated with TDP-43 toxicity in a subject, see page 78 and the rest of discussion. Withers teaches his work furthers our understanding of “the relationship of L-Rich and TDP-43” and “the minimal protective unit of RGNEF,” and suggests L-Rich as “a potential therapeutic target for a future treatment of this devastating disease” (i.e., ALS), see page 2.
Regarding claim 33 and SEQ ID NO: 15, Withers teaches that in his “thesis, ‘Leucine-rich domain’ refers to the domain exclusively, while ‘L-Rich’ refers to the amino-terminal fragment of RGNEF used in this thesis that includes a Leucine-rich domain,” see Pg. 18 last paragraph. As visually characterized in Wither’s Figure 10A page 45, the administered L-Rich construct is an isolated structural domain that cuts
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off shortly after the Leucine-rich region, omitting downstream structural domains such as the Zinc-finger region, etc. While Withers notes that this functional fragment is interchangeably referred to as the Leucine-rich domain or LeuR within the laboratory repository, the primary structural sequence of the RGNEF gene from which this fragment is derived is expressly provided by the lab’s foundational characterizations in Cheung et al., see Pg 2 and Pg. 18. Cheung et al., which is explicitly cited and incorporated in to the baseline disclosure of Withers, provides the definitive structural sequence for the underlying RGNEF gene locus. When mapped to the full-length sequence provided by Cheung (see supplemental figure 1), the structural boundaries of the N-terminal L-Rich domain segment, beginning from the initial start codon of the protein and running through the Leucine-rich domain as mapped out in Wither’s Figure 10A, encompasses the 726-nucleotide blueprint matching the instant SEQ ID NO: 15 with 100% identity.
Claim Rejections - 35 USC § 103
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
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.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
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 24, 32-33, 37, and 41 are rejected under 35 U.S.C. 103 as being unpatentable over Withers BM. (Western University. Electronic Thesis and Dissertation Repository. 6012. Published 01/25/2019) as evidenced by Cheung K. et al., (Molecular and Cellular Neuroscience, Volume 82, Pages 88-95, published 05/08/2017) in view of Droppelmann CA. et al., (Scientific Reports volume 9, Article number: 19928, published 12/27/2019) and Walker AK. et al., (Acta Neuropathol.;130(5):643-60, published 07/22/2015).
The teaching of Withers and as evidenced by Cheung are incorporated herein by reference to the 102 rejection above.
Withers does not teach treating ALS per se in a subject.
Droppelmann teaches the structural cellular mechanics, precise amino acid fragment boundaries, and in vivo mammalian delivery system of the identical RGNEF Leucine-rich domain as employed by Withers to target TDP-43 aggregation dynamics. Droppelmann isolates the first 242 amino acids of the RGNEF protein and names this specific construct “f-LeuR” or “LeuR” (see Pg. 8, Section “Plasmid and Cloning”: “To study the subcellular localization of RGNEF’s LeuR under stress we made a construct expressing a flag-tagged version of the first 242 amino acids of RGNEF containing the LeuR domain (f-LeuR)…”). Droppelmann further teaches that this exact structural segment is the essential domain required to bind and disrupts pathological TDP-42 inclusion bodies observed in ALS patients (see Abstract: “we observed that the leucine-rich domain of RGNEF is critical for its interaction with TDP-43 and localization in micronuclei,” and Pg. 5: “our results suggest that the TDP-43 aggregates observed within micronuclei are pathological in nature”). Crucially, Droppelmann teaches incorporating the LeuR nucleic acid expression construct into a viral vector and delivering to the central nervous system of a mammalian rat model, confirming successful tissue and cell type targeting (see Pg. 3 “we observed a high degree of co-localization between endogenous TDP-43 and f-LeuR in brain neuronal cells (Fig. 3D)” and “this observation strongly suggests that RGNEF and TDP-43 are also able to interact through RGNEF’s LeuR domain under physiological conditions in vivo”).
Walker teaches the generation of a new mouse model “with doxycycline (Dox)-suppressible expression of human TDP-43 (hTDP-43) harboring a defective nuclear localization signal (ΔNLS) under the control of the neurofilament heavy chain promoter,” and that “expression of hTDP-43ΔNLS in these ‘regulatable NLS’ (rNLS) mice resulted in the accumulation of insoluble, phosphorylated cytoplasmic TDP-43 in brain and spinal cord, loss of endogenous nuclear mouse TDP-43 (mTDP-43), brain atrophy, muscle denervation, dramatic motor neuron loss, and progressive motor impairments leading to death,” see abstract. Walker further teaches that “suppression of hTDP-43ΔNLS expression by return of Dox to rNLS mice after disease onset caused a dramatic decrease in phosphorylated TDP-43 pathology, an increase in nuclear mTDP-43 to control levels, and the prevention of further motor neuron loss,” and that “rNLS mice back on Dox also showed a significant increase in muscle innervation, a rescue of motor impairments, and a dramatic extension of lifespan,” see abstract. Walker concludes and suggests that “the rNLS mice are new TDP-43 mouse models that delineate the timeline of pathology development, muscle denervation and neuron loss in ALS/FTLD-TDP,” and “importantly, even after neurodegeneration and onset of motor dysfunction, removal of cytoplasmic TDP-43 and the concomitant return of nuclear TDP-43 led to neuron preservation, muscle re-innervation and functional recovery,” see abstract. In summary, Walker provides a “newly generated rNLS mice faithfully recapitulate many of the pathological features of ALS and FTLD-TDP,” and demonstrated that “the exquisite ability of the CNS to recover from disease-associated dysfunction even at advanced stages of disease in new models of ALS/FTLD-TDP,” thereby explicitly inviting investigators to utilize this mammalian model to test potential therapeutics that could ameliorate the toxicity of cytoplasmic TDP-43 in ALS, see discussion first and last paragraphs.
It would have been obvious to a person having ordinary skill in the art (PHOSITA) before the effective filing date to administer the nucleic acid molecule of Withers and Droppelmann that encodes a peptide comprising the N-terminus domain of the RGNEF that binds to TDP-43 and inhibits TDP-43 toxicity in the TDP-43 murine model of Walker, thereby treating ALS in a subject.
A PHOSITA would have been motivated to do so because the references are all directed to the identical clinical and molecular imperative: neutralizing the neurotoxic cytoplasmic aggregates of TDP-43 that drive the pathogenesis of ALS. Withers provides the functional proof-of-concept that administering a nucleic acid construct encoding the Leucine-rich domain acts as a therapeutic antagonist that successfully clears TDP-43 toxicity, rescues motor neuron deficits, and extends lifespan in an in vitro invertebrate model. To advance this therapeutic approach toward a human clinical application for ALS as suggested by Withers, a PHOSITA would naturally seek to validate this mechanism in a complex, high-order mammalian model that faithfully mirrors human clinical disease hallmarks. Walker provides this necessary mammalian model (rNLS mice) that recapitulates the pathological hallmarks of human ALS, including insoluble cytoplasmic TDP-43 accumulation, motor neuron loss, muscle denervation, and progressive motor impairment leading to death. Crucially, Walker’s data demonstrating that even at advanced stages of neurodegeneration, the central nervous system maintains an “exquisite ability” to structurally recover and reverse motor impairment if the toxic cytoplasmic TDP-43 is cleared or neutralized. Droppelmann bridges this translational gap by providing the precise structural mechanics and delivery tools required to execute Withers’ therapeutic method inside a mammalian model of ALS. Droppelmann teaches that the 242-amaino acid segment (LeuR) is the essential binding domain to physically interact with and disrupt pathological TDP-43 aggregate inclusions, and demonstrates that the LeuR construct can be successfully packaged into a viral gene-therapy vector that safely crosses the blood-brain barrier to target brain neuronal cells in vivo. Therefore, a PHOSITA would have been motivated to combine these teachings and administer the LeuR/L-Rich expression vector to the rNLS mice to test if disrupting cytoplasmic TDP-43 aggregates would trigger the neuroprotective benefits, muscle re-innervation, and functional recovery observed by Walker when retracting TDP-43 transgene expression in his mouse model.
A PHOSITA would have had a reasonable expectation of success because the combined references demonstrate predictable, reinforcing data across in vitro and both invertebrate and vertebrate in vivo models. First, Droppelmann establishes an expectation of success regarding the physical delivery and expression of the therapeutic payload within a mammalian central nervous system, proving that the 242-amino acid sequence successfully gets expressed in relevant tissues and co-localizes with TDP-43 inside rodent brain neurons without causing toxic side effects or inflammatory cellular rejection. Second, Withers demonstrates the functional efficacy of this interaction by showing that when LeuR/L-Rich domain binds to human TDP-43, it reliably rescues living organisms from neurodegeneration, halts motor neuron decline, and significantly extends lifespan. Lastly, Walker validates that the mammalian neurological infrastructure is capable of achieving functional recovery and arresting motor neuron loss once the underlying pressure of cytoplasmic TDP-43 toxicity s relieved. Thus, because the molecular target (pathogenic cytoplasmic TDP-43 aggregation) is identical across all three references, and because Droppelmann’s mammalian viral vector provides predictable means of delivering the functional therapeutic sequence validated by Withers into for example Walker’s highly responsive mammalian model disease of ALS, a PHOSITA would have had a reasonable expectation of success to treat ASL in a subject.
Claim 24, 32-33, 37, and 40-41 are rejected under 35 U.S.C. 103 as being unpatentable over Withers BM. (Western University. Electronic Thesis and Dissertation Repository. 6012. Published 01/25/2019) as evidenced by Cheung K. et al., (Molecular and Cellular Neuroscience, Volume 82, Pages 88-95, published 05/08/2017) in view of Droppelmann CA. et al., (Scientific Reports volume 9, Article number: 19928, published 12/27/2019) and Walker AK. et al., (Acta Neuropathol.;130(5):643-60, published 07/22/2015) as applied to claims 24, 32-33, 37, and 41 above, and further in view of Mora et al., (Amyotroph Lateral Scler Frontotemporal Degener.;21(1-2):5-14, published 07/07/2019).
The teachings of Withers, Droppelmann, and Walker are incorporated herein by reference to the 102 and 103 rejections above.
Neither Withers, Droppelmann, or Walker teach administering a TDP-43 antagonist (i.e., a nucleic acid molecule encoding a peptide comprising a leucine-rich RGNEF domain) in combination with an additional agent that enhances its effect.
It is noted that, in view of the instant specification at page 20 lines 8-13, it appears that the intended agent that enhances the effect of the TDP-43 antagonist embraces or is defined as one or more of riluzole, baclofen, diazepam, gabapentin arimoclomol, and trihexyphenidyl. Therefore, the examiner will interpret the co-administered agent in claim 40 as reading on any one of the aforementioned agents disclosed at Pg. 20 of the specification.
Mora teaches the clinical co-administration of an emerging, targeted neuroprotective therapeutic agent, Masitinib, in combination with a continuous baseline regimen of Riluzole to treat patients suffering from ALS. Mora reports a working clinical paradigm where a second agent is administered as an “add-on therapy to Riluzole” to achieve an enhanced multi-pronged therapeutic effect compared to Riluzole monotherapy. Mora teaches motivation for combination therapy for ALS: “despite significant effort, the overwhelming majority of clinical trials have failed to demonstrate efficacy, highlighting an urgent unmet medical need,” and that “Riluzole, a glutamate antagonist, is the only widely available disease modifying drug for ALS patients, although its benefits are a very modest increase in survival, with no improvement in quality-of-life or slowing of functional loss,” see Introduction. Mora reports that “Masitinib showed significant benefit in ΔALSFRS-R over placebo for the study’s predefined primary efficacy population, exceeding the clinically meaningful target of slowing ALSFRS-R decline by ≥20%,” see Discussion. Thus, Mora teaches that neuroprotective agents co-administered with Riluzole was safe, well-tolerated and can benefit patients with ALS, see Discussion.
It would have been obvious to a person having ordinary skill in the art (PHOSITA) before the effective filing date to administer the therapeutic nucleic acid molecule encoding the TDP-43 antagonist fragment of Withers and Droppelmann in combination with an additional agent that enhances its effect, for example, with the additional agent, Riluzole, as broadly encompassed by claim 40.
A PHOSITA would have been motivated to do so because Mora demonstrates an established, successful clinical trial design where a second neuroprotective agent is administered as an “add-on therapy to Riluzole” to treat patients suffering from ALS. The prior art combination of Withers and Droppelmann establish that the RGNEF L-Rich/LeuR is a neuroprotective agent that acts by ameliorating TDP-43-induced neurotoxicity. Thus, an artisan would be highly motivated to combine traditional baseline therapies such as Riluzole with the neuroprotective effects of RGNEF LeuR fragment based with hopes to recapitulate the enhanced therapeutic effect Mora reports for the combination therapy.
A PHOSITA would have had a reasonable expectation of success because first, compounds such as Riluzole have been characterized and clinically approved as standard-of-care with a predictable safety, metabolic, and pharmacokinetic profile, and second, Mora establishes a functional, peer-reviewed clinical trial proving that the co-administration of a neuroprotective agents alongside Riluzole is safe, well-tolerated, and achieves significant benefits over baseline, monotherapy treatment. Thus, an artisan would have reasonable expected that co-administering Riluzole with the nucleic acid molecule encoding a peptide comprising the neuroprotective leucine rich domain of RGNEF to similarly have an enhanced effect as observed by Mora with the combination of neuroprotective, Masitinib, with Riluzole.
Conclusion
No claims are allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to COREY LANE BRETZ whose telephone number is (571)272-7299. The examiner can normally be reached M-F 7:30am - 6:30pm.
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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.
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/COREY LANE BRETZ/Patent Examiner, 1635
/RAM R SHUKLA/Supervisory Patent Examiner, Art Unit 1635
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