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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 S. pombe gene SPAC1071.03c (UniProt Q9UTR0), designated sil1, encodes an uncharacterized protein of 442 amino acids. No primary literature directly investigating this gene in fission yeast was identified. However, the protein's domain architecture—comprising an ARM-like domain (IPR011989), an ARM-type fold (IPR016024), and membership in the SIL1/FES1/HPBP1 family (IPR050693)—unambiguously identifies it as an ortholog of the well-characterized SIL1/SLS1 nucleotide exchange factors described in Saccharomyces cerevisiae, Yarrowia lipolytica, and mammals. Consequently, this report infers the function of the S. pombe sil1 gene product based on extensive ortholog evidence, which is summarized in the table below.
| Property | Description | Evidence Source | Organism Studied |
|---|---|---|---|
| Gene identity / inference scope | S. pombe SPAC1071.03c (UniProt Q9UTR0) is uncharacterized directly, but its ARM-like and SIL1/FES1/HPBP1 family annotations strongly support orthology to fungal/mammalian SIL1/Sls1 proteins; functional assignment is therefore inferred from orthologs rather than direct fission-yeast experiments. | UniProt/domain context summarized from the research prompt; ortholog-based family/function reviews (ichhaporia2021roleofthe pages 4-5, bracher2015grpehsp110grp170hspbp1sil1 pages 11-14) | S. pombe inferred from orthologs; family evidence from budding yeast and mammals |
| Molecular function | Canonical function is a nucleotide exchange factor (NEF) for the ER Hsp70 chaperone BiP/Kar2, promoting ADP release and ATP rebinding to reset the chaperone cycle and release bound substrates. | (ichhaporia2021roleofthe pages 4-5, david2019redoxsignalingthrough pages 29-33, ichhaporia2021roleofthe pages 1-3) | S. cerevisiae, mammals |
| Structural features | SIL1-family proteins have an elongated ARM-domain architecture: ~16 α-helices arranged into 4 armadillo repeats that form a curved superhelical scaffold specialized for BiP binding. | (ichhaporia2021roleofthe pages 4-5, bracher2015grpehsp110grp170hspbp1sil1 pages 11-14) | Yeast, mammals |
| NEF mechanism | The ARM domain wraps around lobe IIb of BiP/Kar2’s nucleotide-binding domain, with additional contacts to lobe Ib; this rotates the lobes apart, destabilizes ADP binding, and drives nucleotide exchange. | (ichhaporia2021roleofthe pages 4-5, bracher2015grpehsp110grp170hspbp1sil1 pages 11-14) | Yeast, mammals |
| N-terminal regulatory region | Beyond the ARM core, the N-terminal region can contact BiP’s substrate-binding domain as a pseudo-substrate-like regulatory element, modulating substrate release and BiP activity. | (pareja2018arolefor pages 31-36, pareja2018arolefor pages 26-31) | Yeast, mammals |
| Subcellular localization | SIL1 orthologs are ER-luminal proteins. They carry an N-terminal ER signal sequence and typically a C-terminal ER-retention motif; ER retention may also be reinforced by strong binding to abundant BiP. | (pareja2018arolefor pages 26-31, pareja2018arolefor pages 31-36, ichhaporia2021roleofthe pages 4-5) | Yeast, mammals |
| Protein translocation into ER | SIL1/Sls1 contributes to protein import/translocation into the ER lumen by supporting the Kar2/BiP cycle associated with the Sec61/Sec63 translocon. Loss of both SIL1 and the alternative NEF Lhs1 causes severe translocation failure. | (bracher2015grpehsp110grp170hspbp1sil1 pages 19-21, ichhaporia2021roleofthe pages 4-5, verghese2012biologyofthe pages 24-25) | S. cerevisiae, Yarrowia lipolytica |
| Protein folding / ER proteostasis | By regenerating ATP-bound BiP, SIL1 supports protein folding, client release, and general ER proteostasis; single-mutant phenotypes are often mild because the ER has a second BiP NEF, Lhs1/GRP170. | (ichhaporia2021roleofthe pages 1-3, bracher2015grpehsp110grp170hspbp1sil1 pages 19-21, ichhaporia2018theroleof pages 42-46) | Yeast, mammals |
| ER-associated degradation (ERAD) | Ortholog studies indicate SIL1 also supports ERAD, with loss of Sil1 reducing fitness in ERAD-defective backgrounds and slowing degradation of some ERAD substrates. | (pareja2018arolefor pages 26-31, delic2013thesecretorypathway pages 10-13) | Primarily S. cerevisiae |
| Reductant function | In addition to NEF activity, yeast Sil1 has an unexpected reductant role: it reduces oxidized BiP and helps restore normal ATP-dependent chaperone activity after oxidative ER stress. | (siegenthaler2017anunexpectedrole pages 1-2, david2019redoxsignalingthrough pages 66-70) | S. cerevisiae |
| Redox-active cysteines | This reductant function depends on an N-terminal cysteine pair (Cys52/Cys57 in yeast Sil1). Removing both cysteines abolishes reduction of oxidized/glutathionylated BiP, while NEF activity remains intact. | (siegenthaler2017anunexpectedrole pages 3-5, siegenthaler2017anunexpectedrole pages 8-9, siegenthaler2017anunexpectedrole pages 6-7) | S. cerevisiae |
| Relationship with Lhs1/GRP170 | SIL1 and Lhs1/GRP170 are the two ER BiP NEFs. They are partially redundant but mechanistically distinct: double loss is lethal, yet they bind/activate BiP differently and may not serve identical substrate sets. | (bracher2015grpehsp110grp170hspbp1sil1 pages 19-21, ichhaporia2021roleofthe pages 4-5, ichhaporia2018theroleof pages 42-46) | Yeast, mammals |
| Stress regulation / UPR connection | SIL1-family factors are integrated into ER stress responses. SIL1 and Lhs1 can be upregulated during ER stress, helping expand ER folding capacity and reshape BiP-dependent quality control. | (bracher2015grpehsp110grp170hspbp1sil1 pages 19-21, pareja2018arolefor pages 31-36) | Yeast, mammals |
| Regulation by N-glycosylation | In budding yeast, Sil1 is Ost3-dependent N-glycosylated under basal conditions, but this glycosylation is selectively reduced under reductive ER stress. The unglycosylated form remains active and can better compensate for Lhs1 loss, suggesting adaptive tuning of BiP co-chaperone function by ER redox state. | (stevens2017diminishedost3dependentnglycosylation pages 1-2, stevens2017diminishedost3dependentnglycosylation pages 4-5, stevens2017diminishedost3dependentnglycosylation pages 2-3, stevens2017diminishedost3dependentnglycosylation pages 3-4) | S. cerevisiae |
| Disease relevance | In humans, loss-of-function mutations in SIL1 cause Marinesco-Sjögren syndrome, establishing the biological importance of SIL1-mediated ER proteostasis and supporting the functional significance of SIL1 orthologs across eukaryotes. | (ichhaporia2021roleofthe pages 1-3, ichhaporia2018theroleof pages 42-46) | Human, mouse |
| Best functional annotation for S. pombe sil1 | The most defensible annotation for SPAC1071.03c/Q9UTR0 is: ER-luminal BiP/Kar2 nucleotide exchange factor of the SIL1 family, likely participating in ER protein translocation, folding, quality control, and possibly redox-responsive regulation, with partial functional overlap with Lhs1/GRP170. | Inference integrating ortholog evidence (ichhaporia2021roleofthe pages 4-5, bracher2015grpehsp110grp170hspbp1sil1 pages 11-14, bracher2015grpehsp110grp170hspbp1sil1 pages 19-21, pareja2018arolefor pages 26-31) | S. pombe inferred from orthologs |
Table: This table summarizes the most likely functions and properties of S. pombe sil1/SPAC1071.03c (Q9UTR0) based on ortholog evidence from yeast and mammals. It is useful for functional annotation because direct literature on the fission-yeast protein is lacking, so the strongest evidence comes from conserved SIL1-family mechanisms.
The primary function of SIL1-family proteins is to serve as a nucleotide exchange factor (NEF) for the endoplasmic reticulum (ER) Hsp70 chaperone BiP (called Kar2 in yeast). BiP/Kar2 is a central regulator of ER function: it binds unfolded client proteins in an ADP-bound state and releases them upon ATP binding. SIL1 catalyzes the critical step of promoting ADP release from BiP's nucleotide-binding domain (NBD), allowing ATP to bind and triggering conformational changes that open BiP's substrate-binding domain (SBD) and release the polypeptide client, enabling it to fold (ichhaporia2021roleofthe pages 4-5, ichhaporia2021roleofthe pages 1-3). The mammalian SIL1 homolog (BAP, BiP-associated protein) stimulates BiP's ATP hydrolysis activity approximately two-fold independently and up to four-fold when combined with J-domain co-chaperones such as ERdj4 (pareja2018arolefor pages 26-31).
SIL1-family proteins adopt an elongated, kidney-bean-shaped structure composed of approximately 16 α-helices organized into four armadillo (ARM) repeats (ARM1–ARM4), each consisting of three α-helices packed into a superhelix (ichhaporia2021roleofthe pages 4-5). The ARM domain wraps around lobe IIb of BiP's NBD while making additional contacts with lobe Ib. This interaction introduces torsional strain that causes the two lobes to rotate apart, breaking the hydrogen bonds that coordinate the bound ADP molecule and facilitating its release (ichhaporia2021roleofthe pages 4-5).
This mechanism is structurally distinct from that of the cytosolic paralog HspBP1, which distorts lobe I of the Hsp70 NBD rather than acting primarily through lobe IIb. Despite sharing a conserved ARM-repeat core fold, yeast Sil1p and mammalian HspBP1 employ different binding geometries to achieve nucleotide exchange (bracher2015grpehsp110grp170hspbp1sil1 pages 11-14). In addition to the core ARM domain, the N-terminal region of Sil1 contacts BiP's SBD and functions as a pseudo-substrate, modulating BiP's ATPase activity and promoting coordinated substrate release (pareja2018arolefor pages 31-36).
SIL1 orthologs are ER-luminal proteins. They contain an N-terminal ER signal sequence that directs co-translational translocation into the ER lumen, and a C-terminal ER-retention motif (KELR in yeast Sls1p) (pareja2018arolefor pages 26-31, ichhaporia2018theroleof pages 34-38, ichhaporia2021roleofthe pages 4-5). Immunofluorescence studies confirm co-localization of SIL1 with BiP in the ER lumen (pareja2018arolefor pages 31-36). Interestingly, disruption of the KELR retention signal does not cause Sil1 secretion, suggesting that ER retention may be primarily mediated by SIL1's strong interaction with the highly abundant BiP, which is approximately 1,000-fold more concentrated than SIL1 in the ER lumen (pareja2018arolefor pages 26-31, pareja2018arolefor pages 31-36). By inference, the S. pombe sil1 gene product is predicted to localize to the ER lumen.
SIL1/Sls1 contributes to co-translational protein import into the ER lumen by supporting the BiP/Kar2 ATPase cycle associated with the Sec61/Sec63 translocon complex. In S. cerevisiae, Sil1 forms nucleotide-dependent interactions with Kar2p and stimulates Sec63p-mediated activation of Kar2p in a conformation-dependent manner (david2019redoxsignalingthrough pages 29-33, ichhaporia2021roleofthe pages 18-19). In Y. lipolytica, the ortholog Sls1 co-localizes with Kar2 and the Sec61 translocon, consistent with a role in co-translational translocation (delic2013thesecretorypathway pages 10-13).
By regenerating ATP-bound BiP, SIL1 supports the iterative cycles of client binding and release that constitute chaperone-assisted protein folding in the ER lumen (ichhaporia2021roleofthe pages 1-3, bracher2015grpehsp110grp170hspbp1sil1 pages 19-21). Loss of SIL1 in mammalian systems leads to compromised BiP function, activation of the unfolded protein response (UPR), and ultimately to proteostasis collapse in sensitive tissues (ichhaporia2018theroleof pages 42-46).
SIL1 participates in ERAD pathways. In S. cerevisiae, Δsil1 mutants are primarily defective in ERAD; deletion of Sil1 reduces viability in ERAD-defective backgrounds and slows the degradation of ERAD substrates such as CPY* (pareja2018arolefor pages 26-31, delic2013thesecretorypathway pages 10-13).
SIL1 and Lhs1/GRP170 are the two known ER-luminal NEFs for BiP/Kar2. They are partially redundant: single deletions of either factor produce comparatively mild phenotypes and trigger UPR activation, but combined loss of both SIL1 and Lhs1 is synthetically lethal and causes complete translocation failure (bracher2015grpehsp110grp170hspbp1sil1 pages 19-21, ichhaporia2021roleofthe pages 4-5, verghese2012biologyofthe pages 24-25). Despite this redundancy, the two NEFs are mechanistically distinct—they bind BiP through different molecular contacts, and point mutations that disrupt SIL1 binding do not affect GRP170/Lhs1 interaction with BiP (ichhaporia2021roleofthe pages 4-5, ichhaporia2018theroleof pages 34-38). Under normal conditions, Sil1p is approximately one order of magnitude more abundant than Lhs1p, although both constitute less than 0.1% of BiP content (bracher2015grpehsp110grp170hspbp1sil1 pages 19-21).
A landmark discovery revealed that yeast Sil1 has an unexpected reductant function beyond its canonical NEF activity. During oxidative ER stress, a conserved cysteine in BiP's NBD (Cys63 in S. cerevisiae Kar2) becomes oxidized, converting BiP into an ATP-independent holdase that helps cells cope with stress. Sil1 can reverse this BiP cysteine oxidation through a redox-active cysteine pair (Cys52 and Cys57) located in its flexible N-terminal domain (siegenthaler2017anunexpectedrole pages 1-2). This reduction occurs via a dithiol-disulfide exchange mechanism, forming a transient BiP-Sil1 mixed-disulfide intermediate (siegenthaler2017anunexpectedrole pages 6-7). Sil1 is substantially more effective at reducing oxidized BiP than glutathione, requiring 100-fold less molar concentration to achieve comparable activity, owing to its high affinity for BiP (siegenthaler2017anunexpectedrole pages 5-6).
Critically, the N-terminal cysteines are not required for NEF activity itself—the C52A/C57A double mutant retains normal nucleotide exchange function but completely loses reductant capacity (siegenthaler2017anunexpectedrole pages 8-9). In cells, loss of Sil1 dramatically slows the removal of BiP cysteine adducts post-oxidative stress, extending the half-life from approximately 6 minutes to more than 45 minutes (siegenthaler2017anunexpectedrole pages 3-5). Additionally, Sil1 may serve as an electron bridge between protein disulfide isomerase (PDI) and BiP, facilitating BiP reduction through multiple mechanisms (david2019redoxsignalingthrough pages 121-125).
In S. cerevisiae, Sil1 is subject to Ost3-dependent N-glycosylation that is dynamically regulated by the ER redox environment. Under reductive ER stress, the Ost3 thioredoxin-like domain becomes reduced, which inhibits N-glycosylation of Sil1 at Asn181. This produces an unglycosylated form (uSil1) that is functionally active and can more effectively compensate for Lhs1 loss than the glycosylated form (stevens2017diminishedost3dependentnglycosylation pages 1-2, stevens2017diminishedost3dependentnglycosylation pages 2-3, stevens2017diminishedost3dependentnglycosylation pages 3-4). This represents a specific adaptive mechanism, distinct from general UPR activation, by which cells tailor SIL1 activity to the redox status of the ER lumen (stevens2017diminishedost3dependentnglycosylation pages 2-2). Importantly, unglycosylatable Sil1 (N181Q variant) remains functional, demonstrating that N-glycosylation is not essential for NEF activity but rather serves a regulatory role (stevens2017diminishedost3dependentnglycosylation pages 2-3).
Loss-of-function mutations in human SIL1 cause Marinesco-Sjögren syndrome (MSS), an autosomal recessive multisystem disorder characterized by cerebellar ataxia, early-onset cataracts, and progressive myopathy (ichhaporia2021roleofthe pages 1-3, ichhaporia2018theroleof pages 42-46). The pathological importance of SIL1 in human disease underscores the functional significance of this protein family across eukaryotes and supports the inference that the S. pombe ortholog performs an analogous essential role in ER proteostasis.
Based on the conserved domain architecture (ARM-like repeats, SIL1/FES1/HPBP1 family membership) and extensive evidence from ortholog studies, the S. pombe sil1 gene product (SPAC1071.03c, Q9UTR0) is most parsimoniously annotated as an ER-luminal nucleotide exchange factor for the Hsp70 chaperone BiP/Kar2. It is predicted to participate in protein translocation into the ER, chaperone-assisted protein folding, ERAD, and potentially ER redox homeostasis. It likely functions in partial redundancy with the S. pombe Lhs1/GRP170 ortholog. Direct experimental characterization in S. pombe remains to be performed, but the strong conservation of domain architecture and the essential nature of this function across eukaryotes provide high confidence in this functional assignment.
References
(ichhaporia2021roleofthe pages 4-5): Viraj P. Ichhaporia and Linda M. Hendershot. Role of the hsp70 co-chaperone sil1 in health and disease. International Journal of Molecular Sciences, 22:1564, Feb 2021. URL: https://doi.org/10.3390/ijms22041564, doi:10.3390/ijms22041564. This article has 33 citations.
(bracher2015grpehsp110grp170hspbp1sil1 pages 11-14): Andreas Bracher and Jacob Verghese. Grpe, hsp110/grp170, hspbp1/sil1 and bag domain proteins: nucleotide exchange factors for hsp70 molecular chaperones. Sub-cellular biochemistry, 78:1-33, Dec 2015. URL: https://doi.org/10.1007/978-3-319-11731-7_1, doi:10.1007/978-3-319-11731-7_1. This article has 88 citations.
(david2019redoxsignalingthrough pages 29-33): Kevin David Siegenthaler. Redox signaling through the endoplasmic reticulum chaperone bip. Text, Jan 2019. URL: https://doi.org/10.7298/9fam-y122, doi:10.7298/9fam-y122. This article has 2 citations and is from a peer-reviewed journal.
(ichhaporia2021roleofthe pages 1-3): Viraj P. Ichhaporia and Linda M. Hendershot. Role of the hsp70 co-chaperone sil1 in health and disease. International Journal of Molecular Sciences, 22:1564, Feb 2021. URL: https://doi.org/10.3390/ijms22041564, doi:10.3390/ijms22041564. This article has 33 citations.
(pareja2018arolefor pages 31-36): Kristeen Alcaide Pareja. A role for the n-terminal domain in modulating the activities of the nucleotide exchange factor sil1. Text, Jan 2018. URL: https://doi.org/10.7298/x4t43rc8, doi:10.7298/x4t43rc8. This article has 0 citations and is from a peer-reviewed journal.
(pareja2018arolefor pages 26-31): Kristeen Alcaide Pareja. A role for the n-terminal domain in modulating the activities of the nucleotide exchange factor sil1. Text, Jan 2018. URL: https://doi.org/10.7298/x4t43rc8, doi:10.7298/x4t43rc8. This article has 0 citations and is from a peer-reviewed journal.
(bracher2015grpehsp110grp170hspbp1sil1 pages 19-21): Andreas Bracher and Jacob Verghese. Grpe, hsp110/grp170, hspbp1/sil1 and bag domain proteins: nucleotide exchange factors for hsp70 molecular chaperones. Sub-cellular biochemistry, 78:1-33, Dec 2015. URL: https://doi.org/10.1007/978-3-319-11731-7_1, doi:10.1007/978-3-319-11731-7_1. This article has 88 citations.
(verghese2012biologyofthe pages 24-25): Jacob Verghese, Jennifer Abrams, Yanyu Wang, and Kevin A. Morano. Biology of the heat shock response and protein chaperones: budding yeast (saccharomyces cerevisiae) as a model system. Microbiology and Molecular Biology Reviews, 76:115-158, Jun 2012. URL: https://doi.org/10.1128/mmbr.05018-11, doi:10.1128/mmbr.05018-11. This article has 776 citations and is from a domain leading peer-reviewed journal.
(ichhaporia2018theroleof pages 42-46): V. P. Ichhaporia. The role of bip co-chaperone sil1 in marinesco-sjögren syndrome pathogenesis. ArXiv, 2018. URL: https://doi.org/10.21007/etd.cghs.2018.0470, doi:10.21007/etd.cghs.2018.0470. This article has 1 citations.
(delic2013thesecretorypathway pages 10-13): Marizela Delic, Minoska Valli, Alexandra B. Graf, Martin Pfeffer, Diethard Mattanovich, and Brigitte Gasser. The secretory pathway: exploring yeast diversity. FEMS microbiology reviews, 37 6:872-914, Nov 2013. URL: https://doi.org/10.1111/1574-6976.12020, doi:10.1111/1574-6976.12020. This article has 303 citations and is from a domain leading peer-reviewed journal.
(siegenthaler2017anunexpectedrole pages 1-2): Kevin D Siegenthaler, Kristeen A Pareja, Jie Wang, and Carolyn S Sevier. An unexpected role for the yeast nucleotide exchange factor sil1 as a reductant acting on the molecular chaperone bip. eLife, Mar 2017. URL: https://doi.org/10.7554/elife.24141, doi:10.7554/elife.24141. This article has 38 citations and is from a domain leading peer-reviewed journal.
(david2019redoxsignalingthrough pages 66-70): Kevin David Siegenthaler. Redox signaling through the endoplasmic reticulum chaperone bip. Text, Jan 2019. URL: https://doi.org/10.7298/9fam-y122, doi:10.7298/9fam-y122. This article has 2 citations and is from a peer-reviewed journal.
(siegenthaler2017anunexpectedrole pages 3-5): Kevin D Siegenthaler, Kristeen A Pareja, Jie Wang, and Carolyn S Sevier. An unexpected role for the yeast nucleotide exchange factor sil1 as a reductant acting on the molecular chaperone bip. eLife, Mar 2017. URL: https://doi.org/10.7554/elife.24141, doi:10.7554/elife.24141. This article has 38 citations and is from a domain leading peer-reviewed journal.
(siegenthaler2017anunexpectedrole pages 8-9): Kevin D Siegenthaler, Kristeen A Pareja, Jie Wang, and Carolyn S Sevier. An unexpected role for the yeast nucleotide exchange factor sil1 as a reductant acting on the molecular chaperone bip. eLife, Mar 2017. URL: https://doi.org/10.7554/elife.24141, doi:10.7554/elife.24141. This article has 38 citations and is from a domain leading peer-reviewed journal.
(siegenthaler2017anunexpectedrole pages 6-7): Kevin D Siegenthaler, Kristeen A Pareja, Jie Wang, and Carolyn S Sevier. An unexpected role for the yeast nucleotide exchange factor sil1 as a reductant acting on the molecular chaperone bip. eLife, Mar 2017. URL: https://doi.org/10.7554/elife.24141, doi:10.7554/elife.24141. This article has 38 citations and is from a domain leading peer-reviewed journal.
(stevens2017diminishedost3dependentnglycosylation pages 1-2): Kofi L. P. Stevens, Amy L. Black, Kelsi M. Wells, K. Y. Benjamin Yeo, Robert F. L. Steuart, Colin J. Stirling, Benjamin L. Schulz, and Carl J. Mousley. Diminished ost3-dependent n-glycosylation of the bip nucleotide exchange factor sil1 is an adaptive response to reductive er stress. Proceedings of the National Academy of Sciences, 114:12489-12494, Nov 2017. URL: https://doi.org/10.1073/pnas.1705641114, doi:10.1073/pnas.1705641114. This article has 17 citations and is from a highest quality peer-reviewed journal.
(stevens2017diminishedost3dependentnglycosylation pages 4-5): Kofi L. P. Stevens, Amy L. Black, Kelsi M. Wells, K. Y. Benjamin Yeo, Robert F. L. Steuart, Colin J. Stirling, Benjamin L. Schulz, and Carl J. Mousley. Diminished ost3-dependent n-glycosylation of the bip nucleotide exchange factor sil1 is an adaptive response to reductive er stress. Proceedings of the National Academy of Sciences, 114:12489-12494, Nov 2017. URL: https://doi.org/10.1073/pnas.1705641114, doi:10.1073/pnas.1705641114. This article has 17 citations and is from a highest quality peer-reviewed journal.
(stevens2017diminishedost3dependentnglycosylation pages 2-3): Kofi L. P. Stevens, Amy L. Black, Kelsi M. Wells, K. Y. Benjamin Yeo, Robert F. L. Steuart, Colin J. Stirling, Benjamin L. Schulz, and Carl J. Mousley. Diminished ost3-dependent n-glycosylation of the bip nucleotide exchange factor sil1 is an adaptive response to reductive er stress. Proceedings of the National Academy of Sciences, 114:12489-12494, Nov 2017. URL: https://doi.org/10.1073/pnas.1705641114, doi:10.1073/pnas.1705641114. This article has 17 citations and is from a highest quality peer-reviewed journal.
(stevens2017diminishedost3dependentnglycosylation pages 3-4): Kofi L. P. Stevens, Amy L. Black, Kelsi M. Wells, K. Y. Benjamin Yeo, Robert F. L. Steuart, Colin J. Stirling, Benjamin L. Schulz, and Carl J. Mousley. Diminished ost3-dependent n-glycosylation of the bip nucleotide exchange factor sil1 is an adaptive response to reductive er stress. Proceedings of the National Academy of Sciences, 114:12489-12494, Nov 2017. URL: https://doi.org/10.1073/pnas.1705641114, doi:10.1073/pnas.1705641114. This article has 17 citations and is from a highest quality peer-reviewed journal.
(ichhaporia2018theroleof pages 34-38): V. P. Ichhaporia. The role of bip co-chaperone sil1 in marinesco-sjögren syndrome pathogenesis. ArXiv, 2018. URL: https://doi.org/10.21007/etd.cghs.2018.0470, doi:10.21007/etd.cghs.2018.0470. This article has 1 citations.
(ichhaporia2021roleofthe pages 18-19): Viraj P. Ichhaporia and Linda M. Hendershot. Role of the hsp70 co-chaperone sil1 in health and disease. International Journal of Molecular Sciences, 22:1564, Feb 2021. URL: https://doi.org/10.3390/ijms22041564, doi:10.3390/ijms22041564. This article has 33 citations.
(siegenthaler2017anunexpectedrole pages 5-6): Kevin D Siegenthaler, Kristeen A Pareja, Jie Wang, and Carolyn S Sevier. An unexpected role for the yeast nucleotide exchange factor sil1 as a reductant acting on the molecular chaperone bip. eLife, Mar 2017. URL: https://doi.org/10.7554/elife.24141, doi:10.7554/elife.24141. This article has 38 citations and is from a domain leading peer-reviewed journal.
(david2019redoxsignalingthrough pages 121-125): Kevin David Siegenthaler. Redox signaling through the endoplasmic reticulum chaperone bip. Text, Jan 2019. URL: https://doi.org/10.7298/9fam-y122, doi:10.7298/9fam-y122. This article has 2 citations and is from a peer-reviewed journal.
(stevens2017diminishedost3dependentnglycosylation pages 2-2): Kofi L. P. Stevens, Amy L. Black, Kelsi M. Wells, K. Y. Benjamin Yeo, Robert F. L. Steuart, Colin J. Stirling, Benjamin L. Schulz, and Carl J. Mousley. Diminished ost3-dependent n-glycosylation of the bip nucleotide exchange factor sil1 is an adaptive response to reductive er stress. Proceedings of the National Academy of Sciences, 114:12489-12494, Nov 2017. URL: https://doi.org/10.1073/pnas.1705641114, doi:10.1073/pnas.1705641114. This article has 17 citations and is from a highest quality peer-reviewed journal.