The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The requested target—UniProt Q15005—corresponds to human SPCS2 (signal peptidase complex subunit 2), also known as SPC25 / KIAA0102. This identity is consistent with an independent target registry (Open Targets) listing approved symbol SPCS2 and approved name “signal peptidase complex subunit 2” (ENSG00000118363). (OpenTargets Search: -SPCS2)
The signal peptidase complex (SPC) is an essential endoplasmic reticulum (ER) membrane complex that cleaves signal peptides from secretory and membrane proteins entering the secretory pathway. In eukaryotes, SPC is described as a four-subunit complex consisting of SPCS1, SPCS2, SPCS3, and Sec11. In mammals, Sec11 is represented by two paralogous catalytic subunits, SEC11A or SEC11C, forming two SPC variants. (chung2024spc2modulatessubstrate pages 1-2, kozono2023cleavageofthe pages 1-4)
SPCS2 is generally described as a non-catalytic / accessory SPC subunit, distinct from the catalytic subunits (SEC11A/SEC11C) and a proposed catalytic “core” involving SEC11A/C and SPCS3. (zanotti2023characterisationofthe pages 53-57, zanotti2023characterisationofthe pages 57-60)
Beyond canonical N-terminal signal peptide cleavage, recent work supports an expanded role for SPC in post-translocational “quality control” cleavage of cryptic/noncanonical sites in certain membrane proteins—often exposed by misfolding or failed assembly—thereby linking SPC processing to ER protein quality control and degradation pathways. (zanotti2023characterisationofthe pages 57-60, zanotti2023characterisationofthe pages 38-43, zanotti2023characterisationofthe pages 30-34)
SPCS2 is not itself the catalytic peptidase; rather, mechanistic work (in yeast Spc2 and extrapolated via structural conservation to human SPCS2) indicates that Spc2/SPCS2 modulates substrate discrimination and cleavage-site selection by the SPC. Specifically, loss or mutation of Spc2 compromises substrate discrimination and cleavage-site identification. (chung2024spc2modulatessubstrate pages 1-2)
A proposed mechanism is that Spc2/SPCS2 helps shape the local membrane environment—promoting “membrane thinning” at the SPC center—thereby affecting how signal peptides with different hydrophobic segment properties are positioned for cleavage. (chung2024spc2modulatessubstrate pages 1-2)
A key mechanistic concept is the functional coupling of SPC to co-translational translocation at the ER. Spc2/SPCS2 has been reported to mediate transient interactions with the Sec61 translocon via the Sec61 β subunit, consistent with a role in coordinating signal peptide cleavage with translocation. (chung2024spc2modulatessubstrate pages 1-2)
SPCS2 is a membrane subunit of the ER-localized SPC. Structural/topological inference indicates Spc2/SPCS2 contributes substantially to the cytosolic face of the SPC and includes transmembrane helices as part of the complex’s membrane architecture. (chung2024spc2modulatessubstrate pages 1-2, chung2024spc2modulatessubstrate pages 2-3)
A 2024 Journal of Cell Biology study in yeast directly examined Spc2 function and emphasized conservation to human SPCS2 (noting structural similarity and that human SPCS2 constitutes much of the cytosolic SPC portion). The study concluded that Spc2 influences substrate selection and cleavage-site recognition, supported by experiments across signal sequence variants and complemented strains; experiments were performed with replication (e.g., n = 3 per data point in specific assays). (chung2024spc2modulatessubstrate pages 4-4, chung2024spc2modulatessubstrate pages 2-3)
Although conducted in yeast, it is one of the most direct recent mechanistic sources relevant to human SPCS2 due to explicit structural cross-referencing of human SPCS2. (chung2024spc2modulatessubstrate pages 1-2, chung2024spc2modulatessubstrate pages 2-3)
A 2023 Journal of Cell Science study identified Jaw1 (IRAG2/LRMP) as a noncanonical SPC substrate: Jaw1’s C-terminal region is cleaved after insertion by the SPC, and the SEC11A-containing SPC (but not SEC11C-containing SPC) specifically cleaves Jaw1. Functionally, cleavage enhanced Jaw1’s augmentative effect on IP3 receptor–mediated Ca2+ release, linking SPC activity to ER Ca2+ signaling phenotypes. (kozono2023cleavageofthe pages 1-4)
This work does not assign a unique role to SPCS2, but it is directly relevant because SPCS2 is one of the accessory subunits of the human SPC complexes executing this cleavage. (kozono2023cleavageofthe pages 1-4)
A 2023 research thesis presents a detailed model of the human SPC as a quality-control enzyme cleaving cryptic sites in membrane proteins. It provides experimentally supported examples (connexins such as Cx32, iRhom2, and Hrd1 contexts) and argues that SPC can act post-translationally when cryptic sites become accessible. In this framework, SPCS2 (alongside SPCS1 and SPCS3) affects noncanonical cleavage “to varying extents,” and removal of individual subunits can destabilize the complex. (zanotti2023characterisationofthe pages 53-57, zanotti2023characterisationofthe pages 57-60)
This work also reports quantitative/statistical elements for certain substrates (e.g., iRhom2 cleavage quantification with n = 3–6 and significance thresholds; Cx32C201R cleavage quantification n = 3 with significance markers). (zanotti2023characterisationofthe pages 38-43)
A key practical tool for SPC biology is cavinafungin, described as an inhibitor of SPC catalytic subunits (SEC11A/SEC11C) and reported to cause a complete block of noncanonical cleavage in the cited human SPC quality-control work. (zanotti2023characterisationofthe pages 57-60)
While cavinafungin is not SPCS2-specific, it is the main small-molecule tool in the retrieved evidence for perturbing SPCS2-containing SPC complexes and is discussed as a route to block SPC-dependent processing. (zanotti2023characterisationofthe pages 26-30, zanotti2023characterisationofthe pages 57-60)
Multiple virus-focused studies implicate the SPC (including SPCS2) as a host machinery engaged by viral proteins:
These findings support the real-world relevance of SPCS2-containing SPC complexes in viral glycoprotein maturation/assembly contexts at the ER. (chen2021comprehensiveanalysisof pages 8-11, matthaei2024landscapeofproteinprotein pages 14-16)
The 2024 mechanistic study and the 2023 quality-control framework converge on an interpretation that SPCS2 is an accessory factor shaping how SPC engages substrates: SPCS2 contributes to the architecture and cytosolic face of the complex and modulates how cleavage sites are selected—likely by coordinating with Sec61-mediated translocation and membrane-shaping effects—rather than providing catalytic residues itself. (chung2024spc2modulatessubstrate pages 1-2, zanotti2023characterisationofthe pages 53-57)
Recent work emphasizes that SPC may serve as a broader ER protease involved in noncanonical cleavage of membrane proteins (including substrates that are not classical secretory precursors), with physiological outcomes such as altered Ca2+ signaling (Jaw1) and potential coupling to ERAD. (kozono2023cleavageofthe pages 1-4, zanotti2023characterisationofthe pages 57-60)
Open Targets lists SPCS2 associations with several diseases/traits with modest-to-moderate association scores, including neurodegenerative disease (0.5271), dengue disease (0.4629), and type 2 diabetes mellitus (0.2845) (as well as alcohol drinking and abruptio placentae with lower scores). (OpenTargets Search: -SPCS2)
These are aggregated associations and should be interpreted as hypothesis-generating rather than direct mechanistic attribution to SPCS2. (OpenTargets Search: -SPCS2)
A pooled genome-wide CRISPR/Cas9 screen in human trophoblasts (Jeg-3) identified signal peptide processing genes including SPCS2 as part of enriched host factors “crucial for ZIKV replication,” although the provided excerpt does not include per-gene effect sizes for SPCS2. (rother2021signalpeptidasecomplex pages 1-2)
A CRISPR screen in murine lung adenocarcinoma models identified SPCS2 among genes reaching significance in Keap1-mutant dependency analysis, and gene set enrichment on differential gene scores indicated enrichment of ER stress/UPR pathways (FDR = 0.0073). (romero2020keap1mutationrenders pages 2-4)
The following table compiles key concepts, evidence types, quantitative details, and primary sources.
| Topic | Key claim | Evidence type | Specific quantitative/statistical detail if available | Source with year and URL/DOI |
|---|---|---|---|---|
| Identity / complex membership | Human SPCS2 (UniProt Q15005) is the signal peptidase complex subunit 2, a conserved non-catalytic/accessory subunit of the ER signal peptidase complex (SPC), which in higher eukaryotes contains SPCS1, SPCS2, SPCS3, and either SEC11A or SEC11C. Structural/functional work places SPCS2 outside the SEC11A/C+SPCS3 catalytic core. (chung2024spc2modulatessubstrate pages 1-2, zanotti2023characterisationofthe pages 53-57, zanotti2023characterisationofthe pages 57-60) | Structure; comparative cell biology; complex biochemistry | No direct human stoichiometric value reported in the cited excerpts; two SPC paralogs distinguished by SEC11A vs SEC11C. (chung2024spc2modulatessubstrate pages 1-2, zanotti2023characterisationofthe pages 57-60) | Chung et al., 2024, https://doi.org/10.1083/jcb.202211035; Zanotti, 2023, https://doi.org/10.11588/heidok.00033417 |
| Localization / topology | SPCS2 is an ER membrane component of SPC. Conserved structural analysis indicates Spc2/SPCS2 contributes much of the cytosolic face of the complex and includes additional transmembrane helices; SPC catalysis occurs at the ER lumenal side near the membrane. (chung2024spc2modulatessubstrate pages 1-2, zanotti2023characterisationofthe pages 57-60, chung2024spc2modulatessubstrate pages 2-3) | Structure; topology inference; comparative modeling | In yeast-based comparative analysis, human SPCS2 was noted to be structurally conserved with yeast Spc2 and to constitute most of the cytosolic part of SPC. (chung2024spc2modulatessubstrate pages 2-3) | Chung et al., 2024, https://doi.org/10.1083/jcb.202211035; Zanotti, 2023, https://doi.org/10.11588/heidok.00033417 |
| Mechanistic role | SPCS2/Spc2 helps determine substrate discrimination and cleavage-site selection by SPC, likely by promoting local membrane thinning and by presenting features of signal peptides/signal anchors to the complex. In mammals and yeast, Spc2/SPCS2 is also reported to mediate transient interaction with the Sec61 translocon via Sec61β. (chung2024spc2modulatessubstrate pages 1-2, zanotti2023characterisationofthe pages 53-57, chung2024spc2modulatessubstrate pages 3-4, chung2024spc2modulatessubstrate pages 2-3) | Genetics/mutagenesis; computational/MD; structure | Yeast functional data: Spc2 promotes cleavage of signal sequences with short n-regions and reduces cleavage of long n-region substrates; N# >16 substrates were more efficiently cleaved when Spc2 was absent or C-terminally truncated; at least n=3 independent replicates/data point in cited figure context; ~10% reduction in Sec11 and Spc3 abundance in spc2Δ cells in one quantitative analysis. (chung2024spc2modulatessubstrate pages 4-4, chung2024spc2modulatessubstrate pages 3-4, chung2024spc2modulatessubstrate pages 2-3) | Chung et al., 2024, https://doi.org/10.1083/jcb.202211035; Zanotti, 2023, https://doi.org/10.11588/heidok.00033417 |
| Noncanonical substrates / quality control | Beyond canonical signal peptide removal, human SPC participates in ER quality control by cleaving cryptic/noncanonical sites in membrane proteins; SPCS2 affects this process to varying extents, although SPCS1 appears more central as a recruitment/exosite factor. Validated or discussed substrates include Cx32, Cx26, Cx30.3, iRhom2, Hrd1, and Jaw1/IRAG2. (zanotti2023characterisationofthe pages 53-57, zanotti2023characterisationofthe pages 57-60, zanotti2023characterisationofthe pages 38-43, kozono2023cleavageofthe pages 1-4, zanotti2023characterisationofthe pages 30-34) | Biochemistry; knockdown/KO; pulse-chase; inhibitor studies | Computational screening identified 262 membrane proteins with putative N-terminal cryptic SPC sites in one filtered set and ~1300 candidate proteins in a broader screen; iRhom2 cleavage quantification was reported with n=3–6 and significance markers P<0.05, P<0.001; Cx32C201R cleavage quantification n=3 with *P<0.05, P<0.01; post-translational Cx32C201R processing initiated ~30 min after synthesis. (zanotti2023characterisationofthe pages 26-30, zanotti2023characterisationofthe pages 38-43, zanotti2023characterisationofthe pages 30-34) | Zanotti, 2023, https://doi.org/10.11588/heidok.00033417; Kozono et al., 2023, https://doi.org/10.1242/jcs.260439 |
| Catalytic paralog specificity | Some noncanonical substrates show catalytic paralog selectivity: Jaw1/IRAG2 is cleaved by the SEC11A-containing SPC, not SEC11C. For Cx32, SEC11A knockdown did not block cleavage, consistent with possible compensation by SEC11C; cavinafungin blocked cleavage, indicating catalytic SPC dependence. SPCS2 is listed as an accessory component in these pathways. (kozono2023cleavageofthe pages 1-4, zanotti2023characterisationofthe pages 57-60) | Biochemistry; knockdown; pharmacology | SEC11A depletion alone did not impair Cx32 cleavage in cited experiments; cavinafungin caused a complete block of noncanonical cleavage. (zanotti2023characterisationofthe pages 57-60) | Kozono et al., 2023, https://doi.org/10.1242/jcs.260439; Zanotti, 2023, https://doi.org/10.11588/heidok.00033417 |
| Viral interactions | SPCS2 is repeatedly identified as a host factor/interactor for viral proteins processed or assembled at the ER. In SARS-CoV-2 host–virus interactome studies, spike protein significantly bound the signal peptidase complex including SPCS2. In HCV AP-MS studies, SPCS2 interacted with both p7 and E2. (chen2021comprehensiveanalysisof pages 39-40, chen2021comprehensiveanalysisof pages 8-11, matthaei2024landscapeofproteinprotein pages 1-2, matthaei2024landscapeofproteinprotein pages 11-14, matthaei2024landscapeofproteinprotein pages 14-16) | AP-MS interactome; proximity labeling / affinity purification | HCV study scale: 12 p7 binders, 7 primary E2 interactors, and 24 NS4B interactors were detected; SPCS2 was among the host proteins interacting with both p7 and E2. SARS-CoV-2 interactome used SFB-TAP and BioID2 mapping approaches. (chen2021comprehensiveanalysisof pages 39-40, matthaei2024landscapeofproteinprotein pages 1-2) | Chen et al., 2021, https://doi.org/10.1101/2020.12.31.424961 and https://doi.org/10.15252/embj.2021107776; Matthaei et al., 2024, https://doi.org/10.1128/spectrum.02562-22 |
| Inhibition / therapeutic angle | SPC catalytic activity can be chemically inhibited by cavinafungin, which experimentally abolishes noncanonical SPC cleavage and is discussed as a way to perturb viral protein maturation and SPC-dependent processing. This is a catalytic SPC/SEC11 inhibitor, not an SPCS2-specific inhibitor, but it is directly relevant to SPCS2-containing complexes. (zanotti2023characterisationofthe pages 26-30, zanotti2023characterisationofthe pages 57-60) | Pharmacology; substrate-processing assays | Cavinafungin produced a “complete block” of Cx32/noncanonical cleavage in the cited human SPC quality-control work. (zanotti2023characterisationofthe pages 26-30, zanotti2023characterisationofthe pages 57-60) | Zanotti, 2023, https://doi.org/10.11588/heidok.00033417 |
| Disease / translational associations | Disease linkage for SPCS2 itself is presently indirect in the cited evidence: Open Targets lists modest disease associations including dengue disease (score 0.4629), neurodegenerative disease (0.5271), type 2 diabetes mellitus (0.2845), alcohol drinking (0.0527), and abruptio placentae (0.0483), but these appear evidence-aggregated rather than gene-specific mechanistic validation. In membrane-protein QC, SPC activity is relevant to disease-linked Cx32 mutants (>200 known variants reported for Cx32 in the cited thesis). (OpenTargets Search: -SPCS2, zanotti2023characterisationofthe pages 26-30) | Database aggregation; disease-substrate functional context | Open Targets evidence counts shown as 5 for each listed association; association scores: neurodegenerative disease 0.5271, dengue disease 0.4629, T2DM 0.2845, alcohol drinking 0.0527, abruptio placentae 0.0483. Cx32 noted to have >200 disease-linked variants. (OpenTargets Search: -SPCS2, zanotti2023characterisationofthe pages 26-30) | Open Targets context (OpenTargets Search: -SPCS2); Zanotti, 2023, https://doi.org/10.11588/heidok.00033417 |
Table: This table summarizes the best-supported findings about human SPCS2 and the ER signal peptidase complex from the cited context. It highlights what is directly known for SPCS2 versus what is inferred from SPC-wide, structural, and comparative studies.
References
(OpenTargets Search: -SPCS2): Open Targets Query (-SPCS2, 5 results). Buniello, A. et al. (2025). Open Targets Platform: facilitating therapeutic hypotheses building in drug discovery. Nucleic Acids Research.
(chung2024spc2modulatessubstrate pages 1-2): Yeonji Chung, Chewon Yim, Gilberto P. Pereira, Sungjoon Son, Lisbeth R. Kjølbye, Lauren E. Mazurkiewicz, Amy M. Weeks, Friedrich Förster, Gunnar von Heijne, Paulo C.T. Souza, and Hyun Kim. Spc2 modulates substrate- and cleavage site-selection in the yeast signal peptidase complex. Journal of Cell Biology, Nov 2024. URL: https://doi.org/10.1083/jcb.202211035, doi:10.1083/jcb.202211035. This article has 4 citations and is from a highest quality peer-reviewed journal.
(kozono2023cleavageofthe pages 1-4): Takuma Kozono, Chifuyu Jogano, Wataru Okumura, Hiroyuki Sato, Hitomi Matsui, Tsubasa Takagi, Nobuaki Okumura, Toshifumi Takao, Takashi Tonozuka, and Atsushi Nishikawa. Cleavage of the jaw1 c-terminal region enhances its augmentative effect on the ca2+ release via ip3 receptors. Journal of cell science, Feb 2023. URL: https://doi.org/10.1242/jcs.260439, doi:10.1242/jcs.260439. This article has 4 citations and is from a domain leading peer-reviewed journal.
(zanotti2023characterisationofthe pages 53-57): Andrea Zanotti. Characterisation of the human signal peptidase complex as a quality control enzyme for membrane proteins. Text, Jan 2023. URL: https://doi.org/10.11588/heidok.00033417, doi:10.11588/heidok.00033417. This article has 0 citations and is from a peer-reviewed journal.
(zanotti2023characterisationofthe pages 57-60): Andrea Zanotti. Characterisation of the human signal peptidase complex as a quality control enzyme for membrane proteins. Text, Jan 2023. URL: https://doi.org/10.11588/heidok.00033417, doi:10.11588/heidok.00033417. This article has 0 citations and is from a peer-reviewed journal.
(zanotti2023characterisationofthe pages 38-43): Andrea Zanotti. Characterisation of the human signal peptidase complex as a quality control enzyme for membrane proteins. Text, Jan 2023. URL: https://doi.org/10.11588/heidok.00033417, doi:10.11588/heidok.00033417. This article has 0 citations and is from a peer-reviewed journal.
(zanotti2023characterisationofthe pages 30-34): Andrea Zanotti. Characterisation of the human signal peptidase complex as a quality control enzyme for membrane proteins. Text, Jan 2023. URL: https://doi.org/10.11588/heidok.00033417, doi:10.11588/heidok.00033417. This article has 0 citations and is from a peer-reviewed journal.
(chung2024spc2modulatessubstrate pages 2-3): Yeonji Chung, Chewon Yim, Gilberto P. Pereira, Sungjoon Son, Lisbeth R. Kjølbye, Lauren E. Mazurkiewicz, Amy M. Weeks, Friedrich Förster, Gunnar von Heijne, Paulo C.T. Souza, and Hyun Kim. Spc2 modulates substrate- and cleavage site-selection in the yeast signal peptidase complex. Journal of Cell Biology, Nov 2024. URL: https://doi.org/10.1083/jcb.202211035, doi:10.1083/jcb.202211035. This article has 4 citations and is from a highest quality peer-reviewed journal.
(chung2024spc2modulatessubstrate pages 4-4): Yeonji Chung, Chewon Yim, Gilberto P. Pereira, Sungjoon Son, Lisbeth R. Kjølbye, Lauren E. Mazurkiewicz, Amy M. Weeks, Friedrich Förster, Gunnar von Heijne, Paulo C.T. Souza, and Hyun Kim. Spc2 modulates substrate- and cleavage site-selection in the yeast signal peptidase complex. Journal of Cell Biology, Nov 2024. URL: https://doi.org/10.1083/jcb.202211035, doi:10.1083/jcb.202211035. This article has 4 citations and is from a highest quality peer-reviewed journal.
(zanotti2023characterisationofthe pages 26-30): Andrea Zanotti. Characterisation of the human signal peptidase complex as a quality control enzyme for membrane proteins. Text, Jan 2023. URL: https://doi.org/10.11588/heidok.00033417, doi:10.11588/heidok.00033417. This article has 0 citations and is from a peer-reviewed journal.
(chen2021comprehensiveanalysisof pages 8-11): Zhen Chen, Chao Wang, Xu Feng, Litong Nie, Mengfan Tang, Huimin Zhang, Yun Xiong, Samuel K. Swisher, Mrinal Srivastava, and Junjie Chen. Comprehensive analysis of the host-virus interactome of sars-cov-2. bioRxiv, Jan 2021. URL: https://doi.org/10.1101/2020.12.31.424961, doi:10.1101/2020.12.31.424961. This article has 19 citations.
(matthaei2024landscapeofproteinprotein pages 14-16): Alina Matthaei, Sebastian Joecks, Annika Frauenstein, Janina Bruening, Dorothea Bankwitz, Martina Friesland, Gisa Gerold, Gabrielle Vieyres, Lars Kaderali, Felix Meissner, and Thomas Pietschmann. Landscape of protein-protein interactions during hepatitis c virus assembly and release. Feb 2024. URL: https://doi.org/10.1128/spectrum.02562-22, doi:10.1128/spectrum.02562-22. This article has 9 citations and is from a domain leading peer-reviewed journal.
(rother2021signalpeptidasecomplex pages 1-2): Marion Rother and Michael Naumann. Signal peptidase complex subunit 1 is an essential zika virus host factor in placental trophoblasts. Apr 2021. URL: https://doi.org/10.1016/j.virusres.2021.198338, doi:10.1016/j.virusres.2021.198338. This article has 4 citations and is from a peer-reviewed journal.
(romero2020keap1mutationrenders pages 2-4): Rodrigo Romero, Francisco J. Sánchez-Rivera, Peter M. K. Westcott, Kim L. Mercer, Arjun Bhutkar, Alexander Muir, Tania J. González Robles, Swanny Lamboy Rodríguez, Laura Z. Liao, Sheng Rong Ng, Leanne Li, Caterina I. Colón, Santiago Naranjo, Mary Clare Beytagh, Caroline A. Lewis, Peggy P. Hsu, Roderick T. Bronson, Matthew G. Vander Heiden, and Tyler Jacks. Keap1 mutation renders lung adenocarcinomas dependent on slc33a1. Jun 2020. URL: https://doi.org/10.1038/s43018-020-0071-1, doi:10.1038/s43018-020-0071-1. This article has 75 citations and is from a highest quality peer-reviewed journal.
(chung2024spc2modulatessubstrate pages 3-4): Yeonji Chung, Chewon Yim, Gilberto P. Pereira, Sungjoon Son, Lisbeth R. Kjølbye, Lauren E. Mazurkiewicz, Amy M. Weeks, Friedrich Förster, Gunnar von Heijne, Paulo C.T. Souza, and Hyun Kim. Spc2 modulates substrate- and cleavage site-selection in the yeast signal peptidase complex. Journal of Cell Biology, Nov 2024. URL: https://doi.org/10.1083/jcb.202211035, doi:10.1083/jcb.202211035. This article has 4 citations and is from a highest quality peer-reviewed journal.
(chen2021comprehensiveanalysisof pages 39-40): Zhen Chen, Chao Wang, Xu Feng, Litong Nie, Mengfan Tang, Huimin Zhang, Yun Xiong, Samuel K. Swisher, Mrinal Srivastava, and Junjie Chen. Comprehensive analysis of the host-virus interactome of sars-cov-2. bioRxiv, Jan 2021. URL: https://doi.org/10.1101/2020.12.31.424961, doi:10.1101/2020.12.31.424961. This article has 19 citations.
(matthaei2024landscapeofproteinprotein pages 1-2): Alina Matthaei, Sebastian Joecks, Annika Frauenstein, Janina Bruening, Dorothea Bankwitz, Martina Friesland, Gisa Gerold, Gabrielle Vieyres, Lars Kaderali, Felix Meissner, and Thomas Pietschmann. Landscape of protein-protein interactions during hepatitis c virus assembly and release. Feb 2024. URL: https://doi.org/10.1128/spectrum.02562-22, doi:10.1128/spectrum.02562-22. This article has 9 citations and is from a domain leading peer-reviewed journal.
(matthaei2024landscapeofproteinprotein pages 11-14): Alina Matthaei, Sebastian Joecks, Annika Frauenstein, Janina Bruening, Dorothea Bankwitz, Martina Friesland, Gisa Gerold, Gabrielle Vieyres, Lars Kaderali, Felix Meissner, and Thomas Pietschmann. Landscape of protein-protein interactions during hepatitis c virus assembly and release. Feb 2024. URL: https://doi.org/10.1128/spectrum.02562-22, doi:10.1128/spectrum.02562-22. This article has 9 citations and is from a domain leading peer-reviewed journal.