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 .
Priority
This application is a 371 of PCT/KR2021/010001, filed on 07/30/2021, claiming priority to foreign application KR 10-2020-0095988, filed on 07/31/2020.
Claims Status
Claims 1-5, 7-8 are canceled. Claims 6 and 9-11 are pending and under examination. Acknowledgement is made of the receipt and entry of the amendment to the claims filed on August 19, 2026.
Action Summary
Claims 6 and 9-11 rejected under 35 U.S.C. 103 as being unpatentable over Sim et al (US2019/0047993 A1) in view of Shivakrupa et al. (Cancer Research 63, 4412–4419, August 1, 2003) Jack Longley. et al (Proc. Natl. Acad. Sci. USA Vol. 96, pp. 1609±1614, February 1999), and Crew et al (US2006/0063773 A1), are maintained.
The disclosure is objected to because the terminology “novel” appearing in paragraph [0007] is improper as it implies a conclusion regarding the patentability of the claimed invention, is withdrawn in light of the deletion of “novel.”
Claims 6 and 9-11 rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1 and 10 of U.S. Patent No. US10,442,796 B2 in view Shivakrupa et al. (Cancer Research 63, 4412–4419, August 1, 2003) Jack Longley. et al (Proc. Natl. Acad. Sci. USA Vol. 96, pp. 1609±1614, February 1999), and Crew et al (US2006/0063773 A1), are maintained.
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.
Claims 6 and 9-11 remain rejected under 35 U.S.C. 103 as being unpatentable over Sim et al (US2019/0047993 A1) in view of Shivakrupa et al. (Cancer Research 63, 4412–4419, August 1, 2003) Jack Longley. et al (Proc. Natl. Acad. Sci. USA Vol. 96, pp. 1609±1614, February 1999), and Crew et al (US2006/0063773 A1).
Sim teaches a teach a method for the treatment, prevention, and alleviation of acute myeloid leukemia, the method comprising administering a pharmaceutical composition comprising as an active ingredient, a 2,3,5-substituted thiophene compound, preferably (S)-5-((3-fluorophenyl) ethynyl)-N-(piperidin-3-yl)-3-ureidothiophene-2-carboxamide
PNG
media_image1.png
364
605
media_image1.png
Greyscale
. (See claims 1, 9, 10, and paragraph [0299].)
This compound corresponds to compound of Example 22. Moreover, Sim teaches the 2,3,5-substituted thiophene compound is excellent in ability to inhibit activity of Kit among other proteins. (See paragraph [0023].)
Sim does not teach systematic mastocytosis wherein the systematic mastocytosis is caused by substitution of histidine for aspartic acid at amino acid position 816 of c-kit protein and by substitution of aspartic acid for valine at amino acid position 559 of c-kit protein.
Shivakrupa teaches Kit, a type III receptor tyrosine kinase, binds to ligand SCF3 and initiates signals critical for the growth and development of mast cells, melanocytes, hematopoietic stem cells, and the interstitial cells of Cajal. Gain-of-function mutations in Kit are associated with a number of cancers in humans. Substitution of tyrosine/valine/ histidine for aspartic acid in codon 816 of the catalytic domain of the human gene (codon 814 of the murine gene) is found in patients with mastocytosis and mast cell leukemia, as well as some patients with acute myelogenous leukemia and germ cell tumors. (See first paragraph under Introduction Section of the left column of page 4412.) Moreover, Shivakrupa teaches because many patients with mastocytosis have mutations in codon 816, identification of signaling components activated by this mutant in mast cells could lead to identification of pharmaceuticals useful in the treatment of this disease. (See third paragraph of the right column of page 4412.)
Jack Longley Jr. teaches human mastocytosis is characterized by increased mast cells. It usually occurs as a sporadic disease including systemic involvement that is often transient and limited in children and persistent or progressive in adults. The c-KIT protooncogene encodes KIT, a tyrosine kinase that is the receptor for mast cell growth factor. Because mutated KIT can transform cells, we examined c-KIT in skin lesions of 22 patients with sporadic mastocytosis and 3 patients with familial mastocytosis. All patients with adult sporadic mastocytosis had somatic c-KIT mutations in codon 816 causing substitution of valine for aspartate and spontaneous activation of mast cell growth factor receptor. (See Abstract and Table 1.) Moreover, Jack Longley Jr. teaches most known c-KIT mutations cause loss of function of KIT, resulting in piebaldism in humans and the W spotted phenotype in the mouse. However, c-KIT mutations in codon 816 causing substitution of aspartate or tyrosine for valine, and a codon 559 mutation causing substitution of valine for glycine, have been found in neoplastic mast cell lines and have been reported to cause constitutive phosphorylation and activation of KIT. (See last paragraph of the right column of page 1609.)
Crew teaches a compound represented by the formula (I)
PNG
media_image2.png
728
468
media_image2.png
Greyscale
having cKIT activity for treating tumors or cancers such as mastocytosis/mast cell leukemia among others. (See Abstract, claim 1, and paragraph [0079].)
It would have been prima facie obvious to one of ordinary skill in the art at the time the invention was filed to administer the Kit inhibitory compound taught by Sim for treating mastocytosis and mast cell leukemia caused by activating c-KIT mutations, including substitution of histidine for aspartic acid at amino acid position 816 of c-KITt protein and by substitution of aspartic acid for valine at amino acid position 559 of c-kIT protein. Sime teaches the same compound recited in the instant claims and teaches that the compound is excellent in its ability to inhibit KIT activity. Shivakrupa and Jack Longley Jr. teach that mastocytosis and mast cell leukemia are associated with activating c-KIT, including codon 816 and 559 mutations and that such mutations result in constitutive activation of KIT signaling. Mast cell leukemia is a systemic mastocytosis. Crew is relied upon not for the claimed compound, but for the further teaching that cKIT activity is therapeutically relevant to mastocytosis/mast cell leukemia and that c KIT inhibitors are useful for treating such diseases.
Therefore, one of ordinary skill in the art would have been motivated to use Sim’s KIT inhibitor in a patient having mastocytosis and mast cell leukemia (systemic mastocytosis) caused by activating c-KIT mutations because the cited art identifies aberrant KIT activation as a cause or driver of mastocytosis/mast cell leukemia and teaches treatment of such diseases through inhibition of cKIT activity. The motivation is not based on bodily incorporation of Crew’s compound into Sim, but on the combined teachings that: (1) Sim provides the same claimed active compound and teaches KIT inhibition; (2) Shivakrupa and Jack Longley Jr. identity the claimed c-KIT mutations as activating mutations associated with mastocytosis/mast cell leukemia; and (3) Crew confirms that cKIT inhibition is a recognized therapeutic approach for mastocytosis/mast cell leukemia.
One of ordinary skill in the art would have had a reasonably expectation of success because the claimed disease is characterized by aberrant KIT activation, and Sim’s compound is expressly taught to inhibit cKIT activity. Thus, using Sim’s KIT inhibitor to treat a KIT-driven mastocytosis/mast cell leukemia would have been predictable use of a known KIT inhibitor for its established purpose, namely inhibiting KIT signaling in a disease in which KIT activation is implicated. The fact that Crew discloses different cKIT inhibitors does not detract from the rejection because Crew is cited to show the known therapeutic relevance of cKIT inhibition in mastocytosis/mast cell leukemia, not to supply the claimed compound.
Additionally, Crew’s compounds are noted to possess a structurally similar heteroaryl kinase-inhibitor scaffold and are likewise disclosed as possessing cKIT inhibitory activity useful for treating mastocytosis/mast cell leukemia. Thus, Crew further evidences that compounds having kinase-inhibitory scaffolds and cKIT inhibitory activity were recognized in the art as useful for treating c-KTI-driven mastocytosis disorders including mast cell leukemia, a systemic mastocytosis.
Applicant’s arguments
Acknowledgement is made of the receipt and entry of Applicant’s arguments/remarks filed on August 19, 2026. Applicant arguments have been considered but are not persuasive.
Applicant argues that because Shivakrupa teaches away from the claimed invention because Shivakrupa states that “[t]here are no drugs that inhibit the activity of Kit catalytic domain mutants to a greater extent than wild-type kit.” Applicant further argues that, because D816H mutation recited in claim 6 is located in the KIT catalytic domain, one of ordinary skill in the art would not have reasonably expected Sim’s compound to successfully treat mastocytosis associated with the D816H mutation
In response, Applicant’s argument is not persuasive because Applicant reads the cites statement more broadly that its express teaching. Shivakrupa does not state that KIT catalytic-domain mutants cannot be pharmacologically inhibited, that inhibition of such mutants would be therapeutically ineffective, or that persons of ordinary skill should refrain from pursuing pharmacological inhibition of signaling associated with such mutants. Rather, Shivakrupa states that, at the time of that study, there were no drugs that inhibit KIT catalytic-domain mutants to a greater extent than wild-type Kit. The statement concerns the relative degree or selectivity of inhibition of mutant Kit compared to Wild-type Kit, rather than an inability to inhibit mutant Kit. See Abstract.
Indeed, Shivakrupa expressly identifies gain-of-function mutation at codon 816 of the KIT catalytic domain as occurring in patients having mastocytosis and leukemia and explains that the purpose of studying signaling pathways activated by mutant KIT was to identify molecular targets for pharmacological intervention. Shivakrupa further concludes that its findings may provide insight into strategies for treatment of mastocytosis and other diseases associated with mutation in the KIT catalytic domain. (See pp. 4417 and 4418.) Accordingly, when Shivakrupa is considered as a whole rather than by isolating the sentence relied upon by Applicant, the reference does not criticize discredit, or otherwise discourage therapeutic intervention directed to signaling driven by KIT catalytic-domain mutations.
Applicant’s argument does not address the rejection based upon the combined teachings of the references. Sim expressly discloses the same active compound recited in claims 6 and 9, i.e., the compound of Example 22, and teaches that its 2,3,5-substituted thiophene compounds possess excellent KIT inhibitory activity. (See ¶ [0023], claims 1, 9 and 10, ¶[0299].). Shivakrupa establishes that gain-of-function mutations at KIT codon 816 are associated with mastocytosis and mast cell leukemia and result in constitutive mutant KIT signaling. Longley likewise establishes the relationship between activating KIT mutations and mastocytosis and identifies constitutively activating KIT mutations in neoplastic mast cells. Crew further evidences that c-KIT was recognized in the art as a therapeutic approach for mastocytosis/mast cell leukemia. See Abstract, claim 1, and ¶ [0079].)
Thus, the rejection does not rely upon Shivakrupa as teaching that Sim’s particular compound had previously been tested against D816H, nor does the rejection rely upon Crew as disclosing Sim’s compound. Rather, Sim supplies the claimed active compound and its KIT inhibitory activity; Shivakrupa and Longley supply the biological relationship between activating KIT mutations and mastocytosis/mast cell leukemia; and Crew further establishes the recognized therapeutic relevance of c-KIT inhibition for mastocytosis/mast cell leukemia. Considered together, these teachings would have provided one of ordinary skill in the art with a reason to investigate and use Sim’s known KIT-inhibitory compound for treatment of mastocytosis driven by an activating KIT mutation.
Applicant further argues that D816H is an extremely rare clinical variant and that the cited prior art contains no experimental data demonstrating successful inhibition of D816H by Sim’s compound.
In response, this argument is not persuasive. The obviousness inquiry does not require the prior art to contain an actual working example of the precise claimed method, nor does it require absolute predictability of success. The relevant inquiry is whether the teachings of the prior art would have provided a person of ordinary skill with a reason to pursue the claimed method with a reasonable expectation of success.
Here, the cited art expressly identified codon 816 substitutions, including substitution of histidine for aspartic acid at codon 816, as gain-of-function mutations associated with mastocytosis/mast cell leukemia. (See Introduction Section, p. 4412.) The fact that D816H may have been less prevalent than D816V does not negate its express identification in the prior art as a disease-associated activating KIT mutation. Obviousness is not determined by whether the claimed embodiment was the most prevalent or preferred embodiment in the art.
Moreover, the claims do not require that PHI-101 selectively inhibit mutant KIT over wild-type KIT, completely overcome resistance to conventional therapies, possess a particular nanomolar Kd value, produce a specified GI5 value, achieve a particular percentage of tumor-growth inhibition, or provide any particular magnitude of improvement over imatinib, sunitinib, or ponatinib. Those properties and comparative results therefore cannot be imported into claims 6, and 9-11 as limitations when determining the scope of the claimed subject matter.
Applicant’s reliance upon the experimental results reported in Tables 2-5 of the specification has also been considered. The Examiner does not dispute that the reported results may demonstrate that PHI-101 possesses substantial activity against certain KIT mutants. However, unexpected results are relevant to obviousness only to the extent that they are commensurate in scope with the claims and constitute a comparison having sufficient nexus to the claimed invention.
In particular, Applicant relies upon Kd of 4.8 nM for KIT (D816H), 13 nM for KIT (A829P), 16 nM for KIT (V559D), and 26 nM for KIT (V559D/V654A). Those absolute binding-affinity values establish potency, but an absolute result, without an appropriate comparison demonstrating what would have been expected from the closest prior art, does not by itself establish that the result was unexpected. The relevant question is not merely whether well, but whether it performs differently in kind or degrees from what one of ordinary skll reasonably would have expected based upon the prior art.
Applicant’s comparison with imatinib, sunitinb and ponatinib likewise do not establish that Sim’s compound, i.e., the closest compound relied upon in the rejection and the very compound administered by the claims, would have been expected to perform differently. Sim already teaches the claimed compound and identifies KIT inhibitory activity. Accordingly, superior performance relative to other KIT inhibitors does not, without more, rebut the prima facie case arising from the prior-art teaching of the same compound together with known disease-associated KIT pathway.
Further, Applicant relies upon HMC-1.2 cellular and xenograft data involving the D816V/V560G double-mutant system, whereas claim 6 is directed to mastocytosis associated with D816H and amended claim 9 recites A829P, L576P, V559D, V559D/T670I, or V559D/V645A. The HMC-1.2 comparative results therefore do not correspond to several of the specific mutant populations presently claimed. Applicant has not established that the comparative results obtained from the D816V/560G model reasonably represent the full scope of the separately claimed mutant-defined patient populations.
Nor is Applicant’s hindsight argument persuasive. The rationale for the combination is supplied by the references themselves rather than Applicant’s disclosure. Sim provides the claimed compound and identifies its KIT inhibitory activity; Shivakrupa and Longley identify activating KIT mutations as associated with mastocytosis/mast cell leukemia; and Crew identifies c-KIT inhibition as therapeutically relevant to mastocytosis/mast cell leukemia. Thus, Applicant’s specification is not required as a roadmap to identify either the claimed compound, KIT as the relevant biological target, the relationship between activating KIT mutations and mastocytosis, or the therapeutic relevance of KIT inhibition.
The Examiner further notes that notes that obviousness does not require a reasonable expectation that the claimed method would achieve the degree of efficacy subsequently demonstrated by Applicant. The pertinent question is whether one of ordinary skill in the art would have reasonably expected KIT inhibitor to provide treatment of mastocytosis associated with the activating KIT mutations identified by the cited art. Applicant’s showing that the compound subsequently exhibited unexpectedly high potency or superior efficacy does not, without showing commensurate with the claimed scope and appropriately compared with the closest prior art, establish that the claimed method of treatment itself would have been nonobvious.
Accordingly, Applicant’s arguments and evidence have been considered but are not sufficient to outweigh the evidence of obviousness presented by the combined teachings of Sim, Shivakrupa, Longley, and Crew. The rejection of claims 6 and 9-11 under 35 U.S.C. 103 is therefore maintained,
New Rejection necessitated by claim amendment
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 6 and 9-11 remain rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1 and 10 of U.S. Patent No. US10,442,796 B2 in view Shivakrupa et al. (Cancer Research 63, 4412–4419, August 1, 2003) Jack Longley. et al (Proc. Natl. Acad. Sci. USA Vol. 96, pp. 1609±1614, February 1999), and Crew et al (US2006/0063773 A1).
The U.S. patent claims teach a method for the treatment, prevention, and alleviation of acute myeloid leukemia, the method comprising administering a pharmaceutical composition comprising as an active ingredient, a 2,3,5-substituted thiophene compound, preferably (S)-5-((3-fluorophenyl) ethynyl)-N-(piperidin-3-yl)-3-ureidothiophene-2-carboxamide
PNG
media_image1.png
364
605
media_image1.png
Greyscale
as the active ingredient. (See claims 1 and 10)
Although, the U.S. patent claims do not teach the compound is excellent in ability to inhibit activity of Kit among other proteins, the specification of the U.S. patent claims disclose the compound is excellent in ability to inhibit activity of Kit. (See paragraph [0023].)
The U.S. patent claims do not systematic mastocytosis wherein the systematic mastocytosis is caused by substitution of histidine for aspartic acid at amino acid position 816 of c-kit protein and by substitution of aspartic acid for valine at amino acid position 559 of c-kit protein.
Shivakrupa teaches Kit, a type III receptor tyrosine kinase, binds to ligand SCF3 and initiates signals critical for the growth and development of mast cells, melanocytes, hematopoietic stem cells, and the interstitial cells of Cajal. Gain-of-function mutations in Kit are associated with a number of cancers in humans. Substitution of tyrosine/valine/ histidine for aspartic acid in codon 816 of the catalytic domain of the human gene (codon 814 of the murine gene) is found in patients with mastocytosis and mast cell leukemia, as well as some patients with acute myelogenous leukemia and germ cell tumors. (See first paragraph under Introduction Section of the left column of page 4412.) Moreover, Shivakrupa teaches because many patients with mastocytosis have mutations in codon 816, identification of signaling components activated by this mutant in mast cells could lead to identification of pharmaceuticals useful in the treatment of this disease. (See third paragraph of the right column of page 4412.)
Jack Longley Jr. teaches human mastocytosis is characterized by increased mast cells. It usually occurs as a sporadic disease including systemic involvement that is often transient and limited in children and persistent or progressive in adults. The c-KIT protooncogene encodes KIT, a tyrosine kinase that is the receptor for mast cell growth factor. Because mutated KIT can transform cells, we examined c-KIT in skin lesions of 22 patients with sporadic mastocytosis and 3 patients with familial mastocytosis. All patients with adult sporadic mastocytosis had somatic c-KIT mutations in codon 816 causing substitution of valine for aspartate and spontaneous activation of mast cell growth factor receptor. (See Abstract and Table 1.) Moreover, Jack Longley Jr. teaches most known c-KIT mutations cause loss of function of KIT, resulting in piebaldism in humans and the W spotted phenotype in the mouse. However, c-KIT mutations in codon 816 causing substitution of aspartate or tyrosine for valine, and a codon 559 mutation causing substitution of valine for glycine, have been found in neoplastic mast cell lines and have been reported to cause constitutive phosphorylation and activation of KIT. (See last paragraph of the right column of page 1609.)
Crew teaches a compound represented by the formula (I)
PNG
media_image2.png
728
468
media_image2.png
Greyscale
having cKIT activity for treating tumors or cancers such as mastocytosis/mast cell leukemia among others. (See Abstract, claim 1, and paragraph [0079].)
It would have been prima facie obvious to one of ordinary skill in the art at the time the invention was filed to administer the Kit inhibitory compound taught by Sim for treating mastocytosis and mast cell leukemia caused by activating c-KIT mutations, including substitution of histidine for aspartic acid at amino acid position 816 of c-KITt protein and by substitution of aspartic acid for valine at amino acid position 559 of c-kIT protein. Sime teaches the same compound recited in the instant claims and teaches that the compound is excellent in its ability to inhibit KIT activity. Shivakrupa and Jack Longley Jr. teach that mastocytosis and mast cell leukemia are associated with activating c-KIT, including codon 816 and 559 mutations and that such mutations result in constitutive activation of KIT signaling. Mast cell leukemia is a systemic mastocytosis. Crew is relied upon not for the claimed compound, but for the further teaching that cKIT activity is therapeutically relevant to mastocytosis/mast cell leukemia and that c KIT inhibitors are useful for treating such diseases.
Therefore, one of ordinary skill in the art would have been motivated to use U.S. patent claims’ KIT inhibitor in a patient having mastocytosis and mast cell leukemia (systemic mastocytosis) caused by activating c-KIT mutations because the cited art identifies aberrant KIT activation as a cause or driver of mastocytosis/mast cell leukemia and teaches treatment of such diseases through inhibition of cKIT activity. The motivation is not based on bodily incorporation of Crew’s compound into Sim, but on the combined teachings that: (1) Sim provides the same claimed active compound and teaches KIT inhibition; (2) Shivakrupa and Jack Longley Jr. identity the claimed c-KIT mutations as activating mutations associated with mastocytosis/mast cell leukemia; and (3) Crew confirms that cKIT inhibition is a recognized therapeutic approach for mastocytosis/mast cell leukemia.
One of ordinary skill in the art would have had a reasonably expectation of success because the claimed disease is characterized by aberrant KIT activation, and the U.S. patent claims’ compound is expressly taught to inhibit cKIT activity. Thus, using the U.S. patent claims’ KIT inhibitor to treat a KIT-driven mastocytosis/mast cell leukemia would have been predictable use of a known KIT inhibitor for its established purpose, namely inhibiting KIT signaling in a disease in which KIT activation is implicated. The fact that Crew discloses different cKIT inhibitors does not detract from the rejection because Crew is cited to show the known therapeutic relevance of cKIT inhibition in mastocytosis/mast cell leukemia, not to supply the claimed compound.
Additionally, Crew’s compounds are noted to possess a structurally similar heteroaryl kinase-inhibitor scaffold and are likewise disclosed as possessing cKIT inhibitory activity useful for treating mastocytosis/mast cell leukemia. Thus, Crew further evidences that compounds having kinase-inhibitory scaffolds and cKIT inhibitory activity were recognized in the art as useful for treating c-KTI-driven mastocytosis disorders including mast cell leukemia, a systemic mastocytosis
Applicant’s arguments regarding the nonstatutory obviousness-type double patenting rejection have been fully considered but are not persuasive for substantially the same reasons discussed above with respect to the rejection under 35 U.S.C. 103.
As explained above, Sim teaches the same compound recited in the instant claims and further teaches KIT inhibitory activity. Shivakrupa and Jack Longley Jr and Crew collectively teach that activating c-KT mutations are associated with mastocytosis/mast cell leukemia and that inhibition of cKIT activity is a recognized therapeutic strategy for such disorders. Therefore, one would expect the compound taught by Sim to successfully treat mastocytosis associated with the recited cKIT mutations claimed wither a reasonable expectation of success.
Conclusion
Claims 6 and 9-11 are not allowed.
THIS ACTION IS MADE FINAL. 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 JEAN P CORNET whose telephone number is (571)270-7669. The examiner can normally be reached Monday-Thursday from 7.00am-5.30pm.
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, Amy L Clark can be reached at 571-272-1310. 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.
/JEAN P CORNET/ Primary Examiner, Art Unit 1628
Prosecution Insights