Prosecution Insights
Last updated: April 19, 2026
Application No. 17/610,909

METHODS FOR TREATMENT OF OBESITY, ATHEROSCLEROSIS, AND THROMBOSIS

Final Rejection §102§103§112
Filed
Nov 12, 2021
Examiner
SANCHEZ, JUSTIN CHRISTOPHER
Art Unit
1622
Tech Center
1600 — Biotechnology & Organic Chemistry
Assignee
Marshall University Research Corporation
OA Round
2 (Final)
84%
Grant Probability
Favorable
3-4
OA Rounds
3y 5m
To Grant
94%
With Interview

Examiner Intelligence

Grants 84% — above average
84%
Career Allow Rate
27 granted / 32 resolved
+24.4% vs TC avg
Moderate +10% lift
Without
With
+10.0%
Interview Lift
resolved cases with interview
Typical timeline
3y 5m
Avg Prosecution
27 currently pending
Career history
59
Total Applications
across all art units

Statute-Specific Performance

§101
0.9%
-39.1% vs TC avg
§103
29.0%
-11.0% vs TC avg
§102
19.1%
-20.9% vs TC avg
§112
31.6%
-8.4% vs TC avg
Black line = Tech Center average estimate • Based on career data from 32 resolved cases

Office Action

§102 §103 §112
DETAILED ACTION This Office Action is in response to Applicant’s Arguments and Amendment, filed 04 August 2025, wherein the Amendment amended claims 1, 3, 4, 6, 8-10, 12, 14, and 15 and cancelled claim 2. 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 . Rejections – Modified and New Applicant amended independent claim 1, dependent claims 3, 4, 6, 8-10, 12, 14, and 15. Specifically, independent claim 1 has been amended to read as “A method of treating obesity, comprising administering to a subject in need thereof an effective amount of a thymidine phosphorylase inhibitor sufficient to directly reduce an activity of thymidine phosphorylase in the subject”. Claim 3 was amended to be dependent on claim 1. Claims 4, 6, 8-10, 12, 14, and 15 have been amended to add the language “… administering thymidine phosphorylase inhibitor…”. The following 112(a) rejection has been necessitated by the Applicant’s amendment. 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. (New) Claims 1 and 4-16 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. Specifically, claim 1 recites the limitation of an “effective amount of a thymidine phosphorylase inhibitor”, for which the specification does not provide an adequate written description to convey that the inventors were in possession of the scope of the claimed invention. The functional property of the genus of compounds does not permit one to envisage which compounds would have the desired biological function. The instant specification does teach that the thymidine phosphorylase inhibitor is generically a genetic inhibitor such as siRNA, miRNA, shRNA, CRISPR, small molecule inhibitors, peptide or protein inhibitors including antibodies. Additionally, the specification details wherein the thymidine phosphorylase inhibitor is tipiracil, however, there is no written support to identify which compounds are encompassed in the embodiments wherein the thymidine phosphorylase inhibitor is a siRNA, miRNA, shRNA, CRISPR, small molecule inhibitors, peptide or protein inhibitors including antibodies. The Examples provided by the Applicant in the instant specification (pages 28-51) which are drawn to and limited to the use of the small molecule thymidine phosphorylase inhibitor, tipiracil, include experimental data on mice on weight control diets and the effect on liver fat accumulation and atherosclerotic lesions (paragraphs 102-103), thymidine phosphorylase inhibitions relationship to obesity (paragraphs 106-107), and establishes that targeting thymidine phosphorylase with tipiracil is a safe and effective antithrombotic therapy (paragraphs 110-111). As previously mentioned, the instant specification does not teach what is encompassed in the embodiments wherein the thymidine phosphorylase inhibitor is a siRNA, miRNA, shRNA, CRISPR, small molecule inhibitors, peptide or protein inhibitors including antibodies and further does not provide exemplification for any of the categories of thymidine phosphorylase inhibitors outside of the small molecule inhibitor tipiracil. Moreover, it is known in the art that not all siRNA, miRNA, shRNA, CRISPR, small molecule inhibitors, peptide or protein inhibitors would be capable of inhibiting thymidine phosphorylase. For example, Jain et al. ("Molecular therapy using siRNA: Recent trends and advances of multi target inhibition of cancer growth." International journal of biological macromolecules 116 (2018): 880-892.) teaches the use of siRNA-based therapy in the treatment of some cancers (pg. 881, Section “Introduction”, Left Col., 2nd paragraph). Jain also teaches the targets of siRNA cancer therapeutics in clinical trial, shown below, in Table 2 (pg. 889, Section “Clinical trials”). Table 2 taught by Jain. PNG media_image1.png 200 1044 media_image1.png Greyscale Regarding the requirement for adequate written description, the Applicant is directed to MPEP 2163 which states “An applicant shows that the inventor was in possession of the claimed invention by describing the claimed invention with all of its limitations using such descriptive means as words, structures, figures, diagrams, and formulas that fully set forth the claimed invention. Lockwood v. Amer. Airlines, Inc., 107 F.3d 1565, 1572, 41 USPQ2d 1961, 1966 (Fed. Cir. 1997)”. Based on the language of the specification and absence of supporting material, the Examiner concludes that the Applicant does not have possession of the claimed invention with respect to the inclusivity of the alternate thymidine phosphorylase inhibitors. For the above reasons, the recitation of “effective amount of a thymidine phosphorylase inhibitor” is not described in such a way as to reasonably convey to one skilled in the relevant art that the inventor, at the time the application was filed, had possession of the instantly claimed invention. Additionally, as the functional property of the genus of compounds does not permit one to envisage which compounds would have that desired biological function. 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. (Modified) Claims 1, 4-5, 9-10, 12, and 14-16 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Pryor et al. ("Repurposing metformin: an old drug with new tricks in its binding pockets." Biochemical Journal 471.3 (2015): 307-322.) as evidenced Ko et al. ("Metformin Induces Cytotoxicity by Down‐Regulating Thymidine Phosphorylase and Excision Repair Cross‐Complementation 1 Expression in Non‐Small Cell Lung Cancer Cells." Basic & clinical pharmacology & toxicology 113.1 (2013): 56-65.) Pryor teaches a method of treating obesity in a fly model by reducing weight gain, normalizing glucose levels, and increasing survival rates of the fly model subjects (pg. 315, Section “Biguanides and longevity in insects”, 1st para.) by administering the thymidine phosphorylase inhibitor, metformin. Additionally, Pryor teaches wherein the calorie restriction mimicking effects of metformin could be the underlying mechanism responsible for the effect of the improved health span, to include improved fitness and increased insulin sensitivity (pg. 315, Section “Biguanides and longevity in rodents”, 1st para.). The Examiner notes that Applicant defines “subject” on page 27 in paragraph [0075] of the specification filed on November 12, 2021 as, “…the term “subject” includes both humans and animal subjects.” Flies are animals; thus, the administration of metformin to a fly is the administration of metformin to a subject per Applicant’s definition. The Examiner notes that there is evidence that metformin inherently reduces the expression of thymidine phosphorylase and effects other downstream mechanisms which are results of the ubiquitin–26S proteasome-mediated degradation pathway. As evidenced by Ko et al. ("Metformin Induces Cytotoxicity by Down‐Regulating Thymidine Phosphorylase and Excision Repair Cross‐Complementation 1 Expression in Non‐Small Cell Lung Cancer Cells." Basic & clinical pharmacology & toxicology 113.1 (2013): 56- 65.), metformin down-regulated the expression level or activity of TP and ERCC1 protein levels via an ubiquitin–26S proteasome-mediated degradation pathway (pg 57, Section “Results”, 2nd para.). In regards to claim 4, Pryor teaches wherein the reducing the expression level or activity of thymidine phosphorylase reduces the expression level of lipogenesis markers. The reduction of the lipogenesis markers is an inherent property to the administration of metformin through the increase of AMPK which consequently causes suppression of the lipogenesis (pg. 309, Section “AMPK-dependent mechanism”, 1st para. Left column, and Figure 1). "[T]he discovery of a previously unappreciated property of a prior art composition, or of a scientific explanation for the prior art’s functioning, does not render the old composition patentably new to the discoverer." Atlas Powder Co. v. IRECO Inc., 190 F.3d 1342, 1347, 51 USPQ2d 1943, 1947 (Fed. Cir. 1999). See MPEP 2112(I). In regards to claim 5, Pryor teaches wherein the lipogenesis marker is acetyl co- A carboxylase (ACC) (pg. 309, Section “AMPK-dependent mechanism”, 1st para. Left column, and Figure 1). Additionally, Pryor teaches wherein the peroxisome proliferator- activated receptor gamma is down-regulated through the increase of AMPK which consequently increases the presence of SIRT1 and disables CRTC2 which is associated in the up-regulation of the peroxisome proliferator-activated receptor gamma (pg. 308, Section “AMPK-dependent mechanism”, 3rd para.) In regards to claim 9, Pryor teaches wherein reducing the expression level or activity of thymidine phosphorylase blocks the activity of the transcription factor nuclear factor-κB(NK-κB) (pg.312, Section “Metformin and Cancer”, 1st para.) In regards to claim 10, Pryor teaches a method wherein reducing the expression level or activity of thymidine phosphorylase prevents the release of pro-inflammatory cytokines (pg. 312, Figure 2). In regards to claim 12, Pryor teaches wherein reducing the expression level or activity of thymidine phosphorylase down-regulates the expression of fatty acid synthase (pg. 313, Section “AMPK-dependent mechanism”. 2nd para.) In regards to claim 14, Pryor teaches wherein reducing the expression level or activity of thymidine phosphorylase increases glucose tolerance (pg. 314, Figure 3). In regards to claim 15, Pryor teaches wherein reducing the expression level or activity of thymidine phosphorylase promotes weight loss (pg. 313, Figure 3) and can protect against atherosclerosis by preventing the formation of plaques (pg. 311, Section “Metformin and Cardiovascular Disease”, 1st full para.). In regards to claim 16, Pryor teaches wherein the subject is both sexes (pg. 315, Section “Biguanides and longevity in insects”, 1st para.). 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. (Modified) Claims 1 and 3-16 are rejected under 35 U.S.C. 103 as being unpatentable over Pryor et al. ("Repurposing metformin: an old drug with new tricks in its binding pockets." Biochemical Journal 471.3 (2015): 307-322.) in view of Ko et al ("Metformin Induces Cytotoxicity by Down‐Regulating Thymidine Phosphorylase and Excision Repair Cross‐Complementation 1 Expression in Non‐Small Cell Lung Cancer Cells." Basic & clinical pharmacology & toxicology 113.1 (2013): 56-65.) and Li et al. ("Thymidine phosphorylase: A potential new target for treating cardiovascular disease." Trends in cardiovascular medicine 28.3 (2018): 157-171.). The cited prior art and evidentiary references of Pryor et al. and Ko et al., respectively, as set forth above, apply equally to claims 1 and 3-16 under § 103 as well. In regards to claim 3, Li teaches wherein the thymidine phosphorylase inhibitor is tipiracil hydrochloride (pg.165, Section “TYMP is a potential drug target”, sub-section “”TYMP as a target of anti-cancer drugs, 1st para.). One of ordinary skill in the art would have been motivated to modify the teachings of Pryor as evidenced by Ko in combination with the teachings of Li to replace the drug metformin with more potent and FDA approved thymidine phosphorylase inhibitor (pg. 165, Section “TYMP is a potential drug target”, 1st para.), because Li teaches wherein tipiracil (referred to as TPI in Li) inhibits platelet activation in vitro, and thrombosis in vitro without disturbing hemostasis (pg. 166, Section “Safety of TYMP inhibitors”, 1st para.). An ordinary skilled artisan would have had a reasonable expectation of success because Li teaches that tipiracil is the most potent thymidine phosphorylase in clinical use (pg. 165, Section “TYMP is a potential drug target”, 1st para.). Therefore, it would have been prima facie obvious for a person having ordinary skill in the art, prior to the effective filing date of the instantly claimed invention, to combine the teachings of Pryor and Li to arrive at the instantly claimed invention. In regards to claim 6, Li discloses wherein reducing the expression level or activity of thymidine phosphorylase correlates to the suppression of mitogen activated protein kinase (MAPK) (pg. 162, Section “TYMP has an anti-apoptotic effect”, 1st para.). In regards to claim 7, Li teaches wherein the mitogen activated protein kinase is selected from p38 (pg. 162, Section “TYMP has an anti-apoptotic effect”, 1st para.). Ko evidences that metformin induces a decrease in ERK1/2 (pg. 57, Section “Results”, 1st para.) and a decrease in JNK (pg. 61, Section “Discussion”, 1st para.). As evidenced by Ko, metformin works as a thymidine phosphorylase inhibitor and Li teaches that tipiracil is the most potent thymidine phosphorylase inhibitor, thus a person with ordinary skill in the art would reasonably expect that tipiracil would also reduce the expression level of ERK1/2 and JNK2. In regards to claim 11, Pryor teaches a method wherein reducing the expression level or activity of thymidine phosphorylase prevents the release of pro-inflammatory cytokines. However, Pryor does not disclose the types of pro-inflammatory cytokines. Consequently, Li teaches wherein the inflammatory cytokine is TNFα, IL-1, IL-6, IL-8, IL- 7, interferon- gamma and granulocyte-colony stimulating factor (pg.164, Section “TYMP may have dual roles in atherosclerosis”, 2nd and 3rd para.) Claim 8 is rejected under 35 U.S.C. 103 as being unpatentable over Li et al. ("Thymidine phosphorylase: A potential new target for treating cardiovascular disease." Trends in cardiovascular medicine 28.3 (2018): 157-171.) in view of Rojas et al. ("Metformin: an old but still the best treatment for type 2 diabetes." Diabetology & metabolic syndrome 5 (2013): 1-15.). Li discloses the use of tipiracil as a thymidine phosphorylase inhibitor to decrease the thymidine phosphorylase expression level or activity in the treatment of cardiovascular disease. Li does not disclose wherein the use of a thymidine phosphorylase inhibitor increases the expression level of a lipolysis protein, an adipose triglyceride lipase, or a combination thereof. However, Rojas cures this deficiency by teaching wherein the drug metformin, a thymidine phosphorylase inhibitor, activates the AMPK-dependent pathways increasing lipolysis and beta-oxidation in white adipose tissue. One of ordinary skill in the art would have been motivated to modify the teachings of Li by combining the teaching of Rojas because Li teaches that tipiracil is the most potent thymidine phosphorylase inhibitor approved for clinical use (pg. 165, Section “TYMP is a potential drug target”, 1st para.). Thus, a skilled artisan would have a reasonable expectation of success for the reasons mentioned above. It would have been prima facie obvious to a person having ordinary skill in the art, prior to the effective filing date of the instantly claimed invention, to combine the teachings of Li with the teachings of Rojas to arrive at the instantly claimed invention. Claim 13 is rejected under 35 U.S.C. 103 as being unpatentable over Pryor et al. ("Repurposing metformin: an old drug with new tricks in its binding pockets." Biochemical Journal 471.3 (2015): 307-322) in view of Kishton et al. ("AMPK is essential to balance glycolysis and mitochondrial metabolism to control T-ALL cell stress and survival." Cell metabolism 23.4 (2016): 649-662.) and Li et al. ("Thymidine phosphorylase: A potential new target for treating cardiovascular disease." Trends in cardiovascular medicine 28.3 (2018): 157-171.). Pryor discloses wherein reducing the expression level or activity of thymidine phosphorylase down-regulates the expression of fatty acid synthase (pg. 313, Section “AMPK-dependent mechanism”. 2nd para.). Pryor does not disclose wherein the glycolysis-associated protein is selected from fructosebisphosphate aldolase (FBPA), glyceraldehyde-3- phosphate dehydrogenase (GAPDH), and pyruvate kinase muscle isoform M2 (PKM2) but does disclose in Figure 1 how the administration of metformin increases the presence of AMP and thus AMPK. Additionally, Kishton teaches wherein AMPK activation suppressed mTORC1 signaling and glycolysis while supporting mitochondrial metabolism (pg. 3, Section “Introduction”, 2nd full para.). Thus, one having ordinary skill in the art would know that through the suppression of glycolysis, there would inherently be a decreased presence of glycolysis- associated proteins, to include fructosebisphosphate aldolase (FBPA), glyceraldehyde- 3- phosphate dehydrogenase (GAPDH), and pyruvate kinase muscle isoform M2 (PKM2). One of ordinary skill in the art would have been motivated to modify the teachings of Pryor by combining the teaching of Kishton and Li for the reason that a potent thymidine phosphorylase would suppress the glycolysis pathway (pg. 3, Section “Introduction”, 2nd full para.). Thus, a skilled artisan would have a reasonable expectation of success for the reasons mentioned above. It would have been prima facie obvious to a person having ordinary skill in the art, prior to the effective filing date of the instantly claimed invention, to combine the teachings of Pryor with the teachings of Li and Kishton to arrive at the instantly claimed invention. Response to Arguments In the 1st paragraph of page 8 of the Remarks, with respect to the rejection under 35 U.S.C. § 102, Applicant argues that the Pryor reference does not teach wherein the thymidine phosphorylase inhibitor directly reduces an activity of TYMP in a subject. In the 1st paragraph of page 9, the Applicant argues that nowhere in Pryor is there any mention of TYMP at all. This argument has been fully considered, but is not found persuasive. It’s noted that the Examiner references Ko et al. as an evidentiary reference and is not referencing the document as a whole. Ko teaches metformin down-regulated the expression level or activity of TP and ERCC1 protein levels via an ubiquitin–26S proteasome-mediated degradation pathway (pg 57, Section “Results”, 2nd para.). Thus, as taught by Ko, metformin is known to inhibit thymidine phosphorylase, i.e., it is a known thymidine phosphorylase inhibitor. In the 3rd paragraph of page 10 of the Remarks, with respect to the rejection under 35 U.S.C. § 103, Applicant again argues that Pryor does not teach the use of a TYMP inhibitor. For the above reasons, this argument has not been found to be persuasive. Applicant further argues in paragraph 2 of page 11 that Ko provides no discussion that such use of metformin for cancer can be extended to other disease states such as obesity. Again, this argument has been fully considered but has not been found persuasive as the reference in question was used as an evidentiary reference and it’s intended use was not to purport a nexus between cancer and the disease state of obesity but to identify the property of metformin to inhibit thymidine phosphorylase. Conclusion Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a). A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action. Any inquiry concerning this communication or earlier communications from the examiner should be directed to JUSTIN CHRISTOPHER SANCHEZ whose telephone number is (703)756-5336. The examiner can normally be reached Monday -Friday (0730-1700). 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, James H Alstrum-Acevedo can be reached at 571-272-5548. 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. JUSTIN CHRISTOPHER SANCHEZ Examiner Art Unit 1622 /J.C.S./ Examiner, Art Unit 1622 /JAMES H ALSTRUM-ACEVEDO/Supervisory Patent Examiner, Art Unit 1622
Read full office action

Prosecution Timeline

Nov 12, 2021
Application Filed
Mar 31, 2025
Non-Final Rejection — §102, §103, §112
Aug 04, 2025
Response Filed
Sep 29, 2025
Final Rejection — §102, §103, §112 (current)

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Prosecution Projections

3-4
Expected OA Rounds
84%
Grant Probability
94%
With Interview (+10.0%)
3y 5m
Median Time to Grant
Moderate
PTA Risk
Based on 32 resolved cases by this examiner. Grant probability derived from career allow rate.

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