Prosecution Insights
Last updated: April 19, 2026
Application No. 17/654,984

ENGINEERED ANTIBODIES AS MOLECULAR DEGRADERS THROUGH CELLULAR RECEPTORS

Non-Final OA §103§112§DP
Filed
Mar 15, 2022
Examiner
HIBSHMAN, SARAH GRACE
Art Unit
1693
Tech Center
1600 — Biotechnology & Organic Chemistry
Assignee
Yale University
OA Round
1 (Non-Final)
41%
Grant Probability
Moderate
1-2
OA Rounds
3y 3m
To Grant
87%
With Interview

Examiner Intelligence

Grants 41% of resolved cases
41%
Career Allow Rate
18 granted / 44 resolved
-19.1% vs TC avg
Strong +46% interview lift
Without
With
+46.4%
Interview Lift
resolved cases with interview
Typical timeline
3y 3m
Avg Prosecution
41 currently pending
Career history
85
Total Applications
across all art units

Statute-Specific Performance

§101
2.5%
-37.5% vs TC avg
§103
42.5%
+2.5% vs TC avg
§102
14.6%
-25.4% vs TC avg
§112
23.4%
-16.6% vs TC avg
Black line = Tech Center average estimate • Based on career data from 44 resolved cases

Office Action

§103 §112 §DP
DETAILED ACTION The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA . Status of the Application Receipt is acknowledged of Applicants’ preliminary amendment, filed on 06/03/2025, in which claims 1, 19, 28-29, and 31-34 are amended, claims 2-10, 12-18, 20-24, 26-27, 30, and 37 are cancelled, and claims 38-43 are newly added. Claims 1, 11, 19, 25, 28-29, 31-36, and 38-43 are pending and are examined on the merits herein. Priority The instant application is a CIP of PCT/US2020/055053, filed 10/09/2020, which claims domestic benefit to 62/913,679, filed on 10/10/2019. Information Disclosure Statement The information disclosure statement (IDS) dated 03/21/2022, 03/21/2022, 10/12/2022, 10/02/2023, 03/08/2024, 08/06/2024, 12/23/2024, 12/30/2024, 05/08/2025, and 10/09/2025 comply with the provisions of 37 CFR 1.97, 1.98 and MPEP § 609. Accordingly, the information disclosure statements have been considered by the examiner. Drawings The drawings are objected to because the chemical reactions of Figures 9, 10, 13A-L, 14A, 14F, 14G, 14J, 14K, 14N, 15, and 16 are not sufficiently clear to distinguish all the features of the chemical structures due to being low resolution. Corrected drawing sheets in compliance with 37 CFR 1.121(d) are required in reply to the Office action to avoid abandonment of the application. Any amended replacement drawing sheet should include all of the figures appearing on the immediate prior version of the sheet, even if only one figure is being amended. The figure or figure number of an amended drawing should not be labeled as “amended.” If a drawing figure is to be canceled, the appropriate figure must be removed from the replacement sheet, and where necessary, the remaining figures must be renumbered and appropriate changes made to the brief description of the several views of the drawings for consistency. Additional replacement sheets may be necessary to show the renumbering of the remaining figures. Each drawing sheet submitted after the filing date of an application must be labeled in the top margin as either “Replacement Sheet” or “New Sheet” pursuant to 37 CFR 1.121(d). If the changes are not accepted by the examiner, the applicant will be notified and informed of any required corrective action in the next Office action. The objection to the drawings will not be held in abeyance. Claim Objections Claim 28 is objected to because of the following informalities: are objected to because the chemical structures on pages 7-21, and the text for claim 28 on pages 22-24 are not sufficiently clear to distinguish all the features of the chemical structures due to being low resolution. Appropriate correction is required. Claim Rejections - 35 USC § 112(b) The following is a quotation of 35 U.S.C. 112(b): (b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention. The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph: The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention. Claim 28 is rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention. Claim 28 recites “the ASGPR ligand” in the description of LinkerA on line 29 of page 23. There is insufficient antecedent basis for the limitation of “the ASGPR ligand” in the claim. For purposes of compact prosecution, under broadest reasonable interpretation, the claim will be interpreted as “an ASGPR ligand”. 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 1, 11, 19, 25, 29, 31, 33, 35-36, 38-40, and 42-43 are rejected under 35 U.S.C. 103 as being unpatentable over Zamora-Atenza et. al (Arthritis Research and Therapy, 2014; PTO-892) in view of Bertozzi et al. (ChemRxiv, 2019; PTO-892), Rensen et. al (Journal of Biological Chemistry, 2001; PTO-892), Pickens et. al (Bioconjugate Chemistry, 2018; PTO-892), and BroadPharm (Safety Data Sheet for Propargyl-PEG2-Acid, 2016; PTO-892). Zamora-Atenza teaches methods for treating rheumatoid arthritis (RA) by targeting TNF-α using Adalimumab, which is an anti-TNFα monoclonal antibody that specifically blocks the interaction of TNFα with its receptors and binds both soluble and transmembrane TNFα (abstract). TNFα contributes to joint destruction by attracting leukocytes, inducing inflammatory cytokines, upregulating adhesion molecules on endothelial cells (page 1, paragraph 1). Zamora-Atenza describes adalimumab treatment in human RA patients (abstract). The teachings of Zamora-Atenza differ from that of the instantly claimed invention in that Zamora-Atenza does not teach the conjugation of adalimumab to a CRBM as required by instant claim 1. Bertozzi teaches that a general strategy for targeting secreted and plasma membrane proteins for degradation is an unmet need that could dramatically impact human health (page 1, paragraph 1). Bertozzi thus discloses lysosome targeting chimeras (LYTACs), which represent a modular strategy for directing secreted and membrane proteins for degradation in the context of both basic research and therapy (abstract). The LYTAC platform enables depletion of both secreted and membrane proteins via a mechanism of action that is orthogonal and complementary to existing technologies (paragraph bridging pages 1-2). LYTACs consist of antibodies fused to ligands targeting the protein for degradation, and Bertozzi discloses a proof-of-principle example in which an antibody fused to agonist glycopeptide ligands for the cation-independent mannose-6-phosphate receptor (abstract). The antibody was conjugated by non-specifically labeling lysines of the antibody with bicyclononyne and subsequently conjugating this modified antibody to azide-terminated glycopolypeptides via Cu-free strain-promoted azide-alkyne cycloaddition (page 3, paragraph 1). Bertozzi concludes that the chemical tunability and modularity of LYTACs will offer new opportunities in targeted protein degradation for both research and translational applications (page 5, paragraph 1). Rensen teaches that the hepatic asialoglycoprotein receptor (ASGPr) is expressed on the surface of hepatocytes and plays a role in the clearance (endocytosis and lysosomal degradation) of proteins from the serum (page 37577, paragraph 1). Because of its unique localization, abundance, and high internalization capacity, the ASGPr is widely used as a target for the specific delivery of genes and therapeutic agents to hepatocytes (page 37583, paragraph 4). Rensen further discloses ligands that have the structural requirements for proper recognition by the ASGPr and are useful for the design of systems for ASGPr mediated targeting of drugs to hepatocytes (page 37578, paragraph 3). Rensen describes a novel triantennary N-acetylgalactosamine-terminated cluster (Z-Tris(GalNAc)3) that was synthesized and conjugated to a steroid structure via a tyrosine residue (page 37578, paragraph 6). The triantennary ligand is shown below. PNG media_image1.png 510 1603 media_image1.png Greyscale Rensen shows that the Tris(GalNAc)3 ligand successfully targeted liposomes to hepatocytes in vivo through recognition by ASGPr. Pickens reviews the state of the art in bioconjugation via azide−alkyne cycloaddition. Pickens teaches that the emergence of “click chemistry” has revolutionized bioconjugate chemistry by providing facile reaction conditions amenable to both biologic molecules and small molecule probes such as fluorophores, toxins, or therapeutics (abstract). Of all the bioorthogonal click reactions that have been developed, the most widely applied is the copper-catalyzed azide−alkyne cycloaddition reaction (CuAAC). Pickens provides the following general formula for the outcomes of azide−alkyne click chemistry reactions (Table 1). PNG media_image2.png 73 534 media_image2.png Greyscale In the biopharmaceutical field, click chemistry is an attractive option for antibody-drug conjugates in which click chemistry is being explored for the conjugation of payloads to antibodies, and heterobifunctional linkers have been used to functionalize the payload molecule (page 693, paragraph 1). A large variety of heterobifunctional linkers are commercially available with different of solubilizing moieties like PEG and sulfate groups. PEGylated forms of the heterobifunctional linkers are available in various lengths, which permits precise spacing of the reactive handle. Pickens teaches that including PEG in the linker can improve water solubility and alleviate steric effects between the two molecules (page 692, paragraph 4). Pickens further teaches that linkers employed for installation of a reactive handle include Alk-PEGn-COOH, shown below (Figure 3D). PNG media_image3.png 57 87 media_image3.png Greyscale BroadPharm discloses the compound Propargyl-PEG2-acid, which is shown below (section I). PNG media_image4.png 59 195 media_image4.png Greyscale One of ordinary skill in the art would have been motivated to apply the LYTAC strategy of Bertozzi to the Adalimumab of Zamora-Atenza in order to provide targeted degradation of TNF-α in the treatment of RA because Bertozzi teaches that LYTAC platform enables depletion of both secreted and membrane proteins and Zamora-Atenza teaches that TNFα, which occurs in both soluble and transmembrane forms, contributes to joint destruction in RA. In order to achieve this suggested LYTAC of Adalimumab, it would have been prima facie obvious to combine the teachings of Zamora-Atenza with that of Bertozzi, Rensen, Pickens, and BroadPharm before the effective filing date of the claimed invention by derivatizing the Adalimumab of Zamora-Atenza using a linker composed of the Propargyl-PEG2-acid of BroadPharm joined by CuAAC to an azide modified lysine residue as taught by Pickens in order to provide a linker which can conjugate to the Adalimumab of Zamora-Atenza because Pickens teaches that Alk-PEGn-COOH is employed in the installation of a reactive handle. One of ordinary skill in the art would have been motivated to derivatize Adalimumab using the commercially available Propargyl-PEG2-acid heterobifunctional linker of BroadPharm because Pickens teaches that a large variety of heterobifunctional linkers are commercially available and that including PEG in the heterobifunctional linker can improve water solubility and alleviate steric effects between the two molecules. One of ordinary skill in the art would have been motivated to append the alkyne functionalized linker to the triantennary Tris(GalNAc)3 ligand of Rensen, because Rensen teaches that ASGPr is expressed on the surface of hepatocytes and plays a role in the clearance of proteins from the serum and discloses triantennary ligands for recognition by the ASGPr that are useful for ASGPr mediated targeting of drugs to hepatocytes. This would result is a compound of Formula (I) in which the Ab is adalimumab, the left hand CON is triazole and -h is 1, the linker is Z-D-Z’ in which Z is CH2O, D is (CH2)2, and Z’ is CH2O, the left hand CON is an amide and h’ is 1, and ZB is -C=O-(CH2)IM- where IM is 1. One of ordinary skill in the art would have had a reasonable expectation of success because Bertozzi teaches that antibody conjugates, in which the antibody is linked to a targeting ligand via azide-alkyne cycloaddition, are useful for targeting secreted and membrane proteins for degradation, and Rensen provides ligands targeting drugs to ASGPr expressed on the surface of hepatocytes, which plays a role in the endocytosis and lysosomal degradation of proteins from the serum. Regarding instant claim 25, it would have been prima facie obvious to combine the Tris(GalNAc)3 conjugated Adalimumab suggested by the combined teachings of Zamora-Atenza, Bertozzi, Rensen, Pickens, and BroadPharm with an excipient because Zamora-Atenza teaches that Adalimumab is administered as an injection, which indicates that the antibody is administered as a solution and suggests a composition comprising the excipient water. Regarding instant claims 29, 31, and 35-36, it would have been prima facie obvious to treat RA in a human subject using the Tris(GalNAc)3 conjugated Adalimumab suggested by the combined teachings of Zamora-Atenza, Bertozzi, Rensen, Pickens, and BroadPharm because Zamora-Atenza teaches that Adalimumab is used in the treatment of RA patients, who would be understood by one of ordinary skill in the art to be human subjects. Regarding instant claim 33, the instant specification defines chronic inflammatory diseases as encompassing, among others, rheumatoid arthritis (Specification, page 31, lines 5-7). Regarding instant claim 43, the compound above suggested by the combination of Zamora-Atenza, Bertozzi, Rensen, Pickens, and BroadPharm can also be interpreted as a compound of Formula (I) in which the Ab is adalimumab, the left hand CON is triazole and -h is 1, in the first Z-D-Z’ of the linker Z is CH2O, D is (CH2)2, and Z’ is OCH2, the CON of the linker is an amide, in the second Z-D-Z’ of the linker Z is a bond, D is CH2, and Z’ is a bond, h’ is 0 in the left hand CON, and ZB is -C=O-(CH2)IM- where IM is 0. Claims 1, 11, 19, 29, 32, 34-36, 38-43 are rejected under 35 U.S.C. 103 as being unpatentable over Alfaro et. al (British Journal of Cancer, 2009; PTO-892) in view of Bertozzi et al. (ChemRxiv, 2019; PTO-892), Rensen et. al (Journal of Biological Chemistry, 2001; PTO-892), Pickens et. al (Bioconjugate Chemistry, 2018; PTO-892), and BroadPharm (Safety Data Sheet for Propargyl-PEG2-Acid, 2016; PTO-892). Alfaro discusses effects of soluble VEGF and VEGF-containing supernatants from renal cell carcinoma (RCC) cells and the antibodies bevacizumab, sorafenib and sunitinib on monocytes. VEGF has been described to mediate immunosuppression. Alfaro also teaches that there is potential synergism between anti-angiogenic drugs and DC-based immunotherapy treatments for cancer, specifically in a combined treatment of anti-VEGF antibodies and DC based immunotherapy (paragraph bridging pages 1111-1112). Bevacizumab is a monoclonal antibody inhibiting angiogenesis and neutralizing vascular endothelial growth factor (VEGF), and shows clinical benefit in the treatment of human renal cell carcinoma tumors (page 1111, paragraph 1). The teachings of Alfaro differ from that of the instantly claimed invention in that Alfaro does not teach the conjugation of bevacizumab to a CRBM as required by instant claim 1. Bertozzi teaches that a general strategy for targeting secreted and plasma membrane proteins for degradation is an unmet need that could dramatically impact human health (page 1, paragraph 1). Bertozzi thus discloses lysosome targeting chimeras (LYTACs), which represent a modular strategy for directing secreted and membrane proteins for degradation in the context of both basic research and therapy (abstract). The LYTAC platform enables depletion of both secreted and membrane proteins via a mechanism of action that is orthogonal and complementary to existing technologies (paragraph bridging pages 1-2). LYTACs consist of antibodies fused to ligands targeting the protein for degradation, and Bertozzi discloses a proof-of-principle example in which an antibody fused to agonist glycopeptide ligands for the cation-independent mannose-6-phosphate receptor (abstract). The antibody was conjugated by non-specifically labeling lysines of the antibody with bicyclononyne and subsequently conjugating this modified antibody to azide-terminated glycopolypeptides via Cu-free strain-promoted azide-alkyne cycloaddition (page 3, paragraph 1). Bertozzi concludes that the chemical tunability and modularity of LYTACs will offer new opportunities in targeted protein degradation for both research and translational applications (page 5, paragraph 1). Rensen teaches that the hepatic asialoglycoprotein receptor (ASGPr) is expressed on the surface of hepatocytes and plays a role in the clearance (endocytosis and lysosomal degradation) of proteins from the serum (page 37577, paragraph 1). Because of its unique localization, abundance, and high internalization capacity, the ASGPr is widely used as a target for the specific delivery of genes and therapeutic agents to hepatocytes (page 37583, paragraph 4). Rensen further discloses ligands that have the structural requirements for proper recognition by the ASGPr and are useful for the design of systems for ASGPr mediated targeting of drugs to hepatocytes (page 37578, paragraph 3). Rensen describes a novel triantennary N-acetylgalactosamine-terminated cluster (Z-Tris(GalNAc)3) that was synthesized and conjugated to a steroid structure via a tyrosine residue (page 37578, paragraph 6). The triantennary ligand is shown below. PNG media_image1.png 510 1603 media_image1.png Greyscale Rensen shows that the Tris(GalNAc)3 ligand successfully targeted liposomes to hepatocytes in vivo through recognition by ASGPr. Pickens reviews the state of the art in bioconjugation via azide−alkyne cycloaddition. Pickens teaches that the emergence of “click chemistry” has revolutionized bioconjugate chemistry by providing facile reaction conditions amenable to both biologic molecules and small molecule probes such as fluorophores, toxins, or therapeutics (abstract). Of all the bioorthogonal click reactions that have been developed, the most widely applied is the copper-catalyzed azide−alkyne cycloaddition reaction (CuAAC). Pickens provides the following general formula for the outcomes of azide−alkyne click chemistry reactions (Table 1). PNG media_image2.png 73 534 media_image2.png Greyscale In the biopharmaceutical field, click chemistry is an attractive option for antibody-drug conjugates in which click chemistry is being explored for the conjugation of payloads to antibodies, and heterobifunctional linkers have been used to functionalize the payload molecule (page 693, paragraph 1). A large variety of heterobifunctional linkers are commercially available with different of solubilizing moieties like PEG and sulfate groups. PEGylated forms of the heterobifunctional linkers are available in various lengths, which permits precise spacing of the reactive handle. Pickens teaches that including PEG in the linker can improve water solubility and alleviate steric effects between the two molecules (page 692, paragraph 4). Pickens further teaches that linkers employed for installation of a reactive handle include Alk-PEGn-COOH, shown below (Figure 3D). PNG media_image3.png 57 87 media_image3.png Greyscale BroadPharm discloses the compound Propargyl-PEG2-acid, which is shown below (section I). PNG media_image4.png 59 195 media_image4.png Greyscale One of ordinary skill in the art would have been motivated to apply the LYTAC strategy of Bertozzi to the bevacizumab of Alfaro on order to provide targeted degradation of VEGF in the treatment of RCC because Bertozzi teaches that LYTAC platform enables depletion of both secreted and membrane proteins and Alfaro teaches that VEGF is a protein that mediates immunosuppression in RCC. In order to achieve a LYTAC of bevacizumab, it would have been prima facie obvious to combine the teachings of Alfaro with that of Bertozzi, Rensen, Pickens, and BroadPharm before the effective filing date of the claimed invention by derivatizing the bevacizumab of Alfaro using a linker composed of the Propargyl-PEG2-acid of BroadPharm joined by CuAAC to an azide modified lysine residue as taught by Pickens in order to provide a linker which can conjugate to the bevacizumab of Alfaro because Pickens teaches that Alk-PEGn-COOH is employed in the installation of a reactive handle. One of ordinary skill in the art would have been motivated to derivatize bevacizumab using the commercially available Propargyl-PEG2-acid heterobifunctional linker of BroadPharm because Pickens teaches that a large variety of heterobifunctional linkers are commercially available and that including PEG in the heterobifunctional linker can improve water solubility and alleviate steric effects between the two molecules. It would have further been prima facie obvious to append the alkyne functionalized linker to the triantennary Tris(GalNAc)3 ligand of Rensen, because Rensen teaches that ASPGr is expressed on the surface of hepatocytes and plays a role in the clearance of proteins from the serum and discloses triantennary ligands for recognition by the ASGPr that are useful for ASGPr mediated targeting of drugs to hepatocytes. This would result is a compound of Formula (I) in which the Ab is bevacizumab, the left hand CON is triazole and -h is 1, the linker is Z-D-Z’ in which Z is CH2O, D is (CH2)2, and Z’ is OCH2, the left hand CON is an amide and h’ is 1, and ZB is -C=O-(CH2)IM- where IM is 1. One of ordinary skill in the art would have had a reasonable expectation of success because Bertozzi teaches that antibody conjugates, in which the antibody is linked to a targeting ligand via azide-alkyne cycloaddition, are useful for targeting secreted and membrane proteins for degradation, and Rensen provides ligands targeting drugs to ASGPr expressed on the surface of hepatocytes, which plays a role in the endocytosis and lysosomal degradation of proteins from the serum. Regarding instant claims 29 and 35-36, it would have been prima facie obvious to treat RA in a human subject using the Tris(GalNAc)3 conjugated bevacizumab suggested by the combined teachings of Alfaro, Bertozzi, Rensen, Pickens, and BroadPharm because Alfaro teaches that bevacizumab is used in the treatment of RCC patients, who would be understood by one of ordinary skill in the art to be human subjects. Regarding instant claims 34, it would have been prima facie obvious to administer the additional therapeutic agent of DC based immunotherapy to treat cancer because Alfaro teaches that there is potential synergism between anti-angiogenic drugs and DC-based immunotherapy treatments for cancer, specifically in a combined treatment of anti-VEGF antibodies and DC based immunotherapy. Regarding instant claim 43, the compound above suggested by the combination of Alfaro, Bertozzi, Rensen, Pickens, and BroadPharm can also be interpreted as a compound of Formula (I) in which the Ab is bevacizumab, the left hand CON is triazole and -h is 1, in the first Z-D-Z’ of the linker Z is CH2O, D is (CH2)2, and Z’ is OCH2, the CON of the linker is an amide, in the second Z-D-Z’ of the linker Z is a bond, D is CH2, and Z’ is a bond, h’ is 0 in the left hand CON, and ZB is -C=O-(CH2)IM- where IM is 0. Claim 28 is rejected under 35 U.S.C. 103 as being unpatentable over Liras et. al (US 2015/0329555 A1; PTO-892). Liras teaches compounds for use as asialoglycoprotein receptor (ASGPR) targeting agents (abstract). Liras discloses a compound of Formula (A), shown below. PNG media_image5.png 155 428 media_image5.png Greyscale R1 is selected from, among others, -Z-X-Y, in which Z is selected from, among others, -CH2-O-, X is selected from, among others, a linker, and Y is selected from, among others, an antibody. R2 is selected from, among others, -N(R3)-S(O)2-R3, in which R3 is selected from, among others, H. Liras teaches that the antibody includes an antibody of any class, such as IgG, IgA, or IgM [0055]. The teachings of Liras differ from that of the instantly claimed invention in that Liras does not expressly teach a single embodiment of the compound of instant claim 28. However, it would have been prima facia obvious to select the variables for an asialoglycoprotein receptor targeting agent of Formula (A) in which R1 is -Z-X-Y, Z is -CH2-O-, X is a linker, Y an IgA antibody, R2 is -N(R3)-S(O)2-R3, in which R3 is H because Liras teaches these variables in the selection of ASGPR targeting agents. This corresponds to a compound of instant formula (I) on page 7 of the instant claims, in which an antibody is the extracellular protein targeting ligand, Z-X is Linker B, Linker A is a bond, and R2 is -NR8-S(O)2-R10 -(found in option (iii) on claims, page 22), in which R8 and R10 are H. 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 1, 11, 19, 25, 29, 31-36, and 38-43 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-2, 11-25, 27-29, and 33 of copending Application No. 17/768,145 (reference application). The claims at issue are not identical because ‘984 recites compounds with a broader scope of structures because it does not limit the structure of the antibody, CON, Linker, or CRBM. However, they are not patentably distinct from each other because ‘984 is directed to a compound of the below formula (I). PNG media_image6.png 34 355 media_image6.png Greyscale . Claim 13 further limits that CRPM is selected from, among others, an ASGPR binder. Claim 18 further limits that ASGPRBM has the below structure wherein ZB- may be absent. PNG media_image7.png 229 442 media_image7.png Greyscale . Claim 21 limits that each CON is independently selected from the group consisting of, among others, PNG media_image8.png 75 77 media_image8.png Greyscale and PNG media_image9.png 58 71 media_image9.png Greyscale . Claim 19 further limits that the linker is a polyethylene glycol containing linker having 1-12 ethylene glycol residues. Claim 20 further limits wherein the linker comprises a structure -PEG-CON-PEG. Claim 24 further limits that Ab is selected from, among others, adalimumab. Claim 25 of ‘984 further limits a pharmaceutical composition comprising at least one pharmaceutically acceptable excipient and at least one compound of claim 1, optionally comprising another therapeutically active compound. Claim 27 further limits a method of treating a disease in a subject comprising administering a compound of claim 1, and optionally administering at least one additional therapeutic agent that treats the disorder. Claim 28 further limits wherein the disease comprises an autoimmune disease, cancer, or inflammation. Claim 29 further limits the treatment of, among others, rheumatoid arthritis or renal cancer. Claim 29 further limits that the subject is mammal, optionally human. This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented. Conclusion No claims are allowed. Any inquiry concerning this communication or earlier communications from the examiner should be directed to Sarah Grace Hibshman whose telephone number is (703) 756-5341. The examiner can normally be reached Monday-Thursday 7:30am-5:30pm (EST). 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, Scarlett Goon can be reached on (571) 270-5241. 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. /S.G.H./Examiner, Art Unit 1693 /SCARLETT Y GOON/Supervisory Patent Examiner, Art Unit 1693
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Prosecution Timeline

Mar 15, 2022
Application Filed
Feb 02, 2026
Non-Final Rejection — §103, §112, §DP (current)

Precedent Cases

Applications granted by this same examiner with similar technology

Patent 12551498
TREATMENT OF P53-DEFICIENT CANCERS
2y 5m to grant Granted Feb 17, 2026
Patent 12521360
CALORIC RESTRICTION MIMETIC COMPOSITIONS
2y 5m to grant Granted Jan 13, 2026
Patent 12491191
INHIBITION OF INTERACTION BETWEEN OCT4 AND MAPKAPK2 OR DNA-PKCS TO REGULATE C-MYC IN CANCER
2y 5m to grant Granted Dec 09, 2025
Patent 12448375
KINASE INHIBITORS FOR THE TREATMENT OF NEURODEGENERATIVE DISEASES
2y 5m to grant Granted Oct 21, 2025
Patent 12403154
ADMINISTRATION OF STING AGONIST AND CHECKPOINT INHIBITORS
2y 5m to grant Granted Sep 02, 2025
Study what changed to get past this examiner. Based on 5 most recent grants.

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Prosecution Projections

1-2
Expected OA Rounds
41%
Grant Probability
87%
With Interview (+46.4%)
3y 3m
Median Time to Grant
Low
PTA Risk
Based on 44 resolved cases by this examiner. Grant probability derived from career allow rate.

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