Gene Research Report: HSCB (DNAJC20) – Human Iron–Sulfur Cluster Co-Chaperone OpenAI o3-deep-research-2025-06-26 97 citations 2025-12-27T20:16:35.899317

Gene Research Report: HSCB (DNAJC20) – Human Iron–Sulfur Cluster Co-Chaperone

Overview and Key Concepts

HSCB (DNAJC20/HSC20) is a human gene encoding a DnaJ-type co-chaperone belonging to the heat shock cognate B family (www.ncbi.nlm.nih.gov). Its protein product is a specialized co-chaperone that plays a crucial role in the biogenesis of iron–sulfur (Fe–S) clusters, which are inorganic cofactors essential for numerous cellular enzymes and processes. Fe–S clusters consist of iron and sulfide ions coordinated by cysteine residues in proteins, commonly forming [2Fe-2S] or [4Fe-4S] structures (pmc.ncbi.nlm.nih.gov). These clusters enable redox reactions and stabilizing functions in proteins involved in mitochondrial respiration, metabolic pathways, and DNA maintenance (pubmed.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). The final step of Fe–S protein assembly involves transferring a newly synthesized cluster from a scaffold protein to a target apoprotein – a process facilitated by a dedicated chaperone system comprising an Hsp70-family chaperone and a J-domain co-chaperone like HSCB (pmc.ncbi.nlm.nih.gov). In bacteria (e.g. E. coli), this role is fulfilled by the HscA/HscB chaperone pair, while in yeast it’s Ssq1/Jac1; human HSCB (also called HSC20) is the functional homolog in mitochondria, partnering with the Hsp70 chaperone HSPA9 (mortalin/Grp75) (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Together, HSCB and HSPA9 ensure that nascent Fe–S clusters are properly transferred and inserted into recipient Fe–S proteins. This co-chaperone activity is critical because Fe–S clusters can be unstable; dedicated factors like HSCB guide cluster delivery with specificity, preventing loss or misplacement of the cluster (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov).

Protein Features and Localization

HSCB protein is relatively small (≈235 amino acids) and is synthesized with an N-terminal mitochondrial targeting sequence. This leader sequence directs HSCB to the mitochondrial matrix, where it is cleaved off to produce the mature functional protein inside mitochondria (pmc.ncbi.nlm.nih.gov). As a result, HSCB localizes predominantly to the mitochondrial matrix, consistent with mitochondria being the site of Fe–S cluster assembly. A 2010 study confirmed HSCB is expressed in many human tissues and localizes mainly to mitochondria, though intriguingly, a small fraction was detected outside mitochondria in cells (pmc.ncbi.nlm.nih.gov). Subsequent research suggests alternative splicing of HSCB can produce an isoform lacking the targeting sequence, termed “C-HSC20”, which resides in the cytosol (www.ncbi.nlm.nih.gov). This cytosolic form appears to integrate with the cytosolic Fe–S cluster assembly machinery, hinting that HSCB’s function may not be strictly confined to mitochondria (pmc.ncbi.nlm.nih.gov).

Structurally, human HSCB contains the signature J-domain at its N-terminus, characterized by the HPD motif, which is crucial for stimulating the ATPase activity of its partner Hsp70 (HSPA9) (pmc.ncbi.nlm.nih.gov). Uniquely, human and other metazoan HSCB proteins possess an auxiliary tetracysteine metal-binding domain at the far N-terminus (motif: CWXCX9–13FCXXCXXXQ), not present in bacterial HscB (pmc.ncbi.nlm.nih.gov). The 3.0 Å crystal structure of human HSCB (solved in 2008) revealed an L-shaped molecule with this extra N-terminal domain coordinating a metal ion via four cysteines (pmc.ncbi.nlm.nih.gov). The metal-binding site is structurally reminiscent of a rubredoxin/zinc-finger motif, suggesting it likely binds a metal such as Zn²⁺ or perhaps an Fe–S fragment (pmc.ncbi.nlm.nih.gov). The exact function of this metal-binding domain remains under investigation, but its conservation in animals and plants (and even some bacteria) implies a regulatory or stability role unique to eukaryotic HSCB (pmc.ncbi.nlm.nih.gov). The C-terminal region of HSCB forms an oligomerization and client-binding domain (also called J-domain C-terminal domain) that is responsible for recognizing partner proteins like the Fe–S scaffold. Overall, HSCB’s architecture — J-domain plus specialized C-terminal domains — is optimized for bridging interactions between the Hsp70 chaperone, the Fe–S cluster scaffold, and the recipient apoprotein (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov).

Functional Role in Fe–S Cluster Assembly

HSCB’s primary function is as an iron–sulfur cluster co-chaperone, orchestrating the transfer of newly formed Fe–S clusters to target proteins. In the mitochondrial Fe–S cluster assembly (ISC) pathway, a transient [2Fe-2S] cluster is first built on a scaffold protein (human ISCU) with the help of a cysteine desulfurase (NFS1/ISD11) and other factors. HSCB intervenes at the cluster transfer step: it binds directly to the cluster-loaded ISCU scaffold and also to the recipient apo-protein that needs the cluster (pmc.ncbi.nlm.nih.gov). By simultaneously engaging the scaffold and the target, HSCB effectively guides the cluster delivery to the correct client protein (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). At the same time, HSCB recruits its partner Hsp70 chaperone (HSPA9) via the J-domain. Specifically, HSCB’s J-domain contacts the ATP-bound form of HSPA9, binding to HSPA9’s nucleotide-binding domain while the scaffold (ISCU) associates with HSPA9’s substrate-binding domain (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). This arrangement triggers HSPA9 to hydrolyze ATP – a reaction stimulated by HSCB’s J-domain – which induces a conformational change in HSPA9. The ATP hydrolysis causes HSPA9 to clamp down, an action thought to facilitate release of the Fe–S cluster from ISCU and its transfer onto the recipient protein (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). In essence, HSCB acts as a matchmaker and activator: it brings together the cluster donor and acceptor, and activates HSPA9’s chaperone activity at just the right time to ensure the cluster is handed off efficiently (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). After transfer, a nucleotide exchange on HSPA9 allows the chaperone to reset, and the cycle can repeat for additional cluster delivery events (pmc.ncbi.nlm.nih.gov).

Crucially, HSCB imparts specificity to the cluster transfer process. Not all client proteins randomly receive clusters; many require the HSCB–HSPA9 system to be present. Studies indicate HSCB recognizes a particular sequence motif (LYR) in many Fe–S target proteins (pmc.ncbi.nlm.nih.gov). This motif, usually a tripeptide Leu-Tyr-Arg or a closely related sequence (hydrophobic–aromatic–basic), has been identified in various Fe–S enzymes and in components of the cytosolic Fe–S assembly machinery (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). HSCB binding to a target’s LYR motif recruits the HSCB–HSPA9 complex to that apo-protein, thus acting as a docking signal for cluster delivery (pmc.ncbi.nlm.nih.gov). For example, the human heme-biosynthetic enzyme ferrochelatase (FECH) contains an LYR-like motif; although FECH’s [2Fe-2S] cluster was only discovered in mammals, HSCB’s involvement via this motif helps explain how the cluster is inserted into FECH (pmc.ncbi.nlm.nih.gov). Likewise, an LYR motif in the CIAO1 protein (a key factor of the cytosolic Fe–S insertion apparatus) is bound by HSCB, indicating HSCB may hand off clusters to the CIAO1 complex for final delivery to cytosolic/nuclear Fe–S proteins (pmc.ncbi.nlm.nih.gov). This motif-driven targeting underscores HSCB’s role in ensuring that Fe–S clusters are delivered to the correct subset of recipient proteins, rather than diffusing indiscriminately. It also highlights a elegant convergence: the same co-chaperone system that works in mitochondria can recognize signals in cytosolic assembly factors, thereby linking mitochondrial Fe–S production to cytosolic Fe–S protein maturation (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov).

Molecular Interactions and Pathways

HSCB does not work in isolation; it is embedded in the larger Fe–S cluster biogenesis network and interacts with multiple partners. Its principal binding partners in mitochondria are: (1) HSPA9, the Hsp70 family chaperone that actually provides the ATP-driven conformational work; (2) ISCU, the scaffold protein that initially holds the nascent Fe–S cluster; and (3) the Fe–S recipient proteins (which often present the LYR motif for HSCB binding). Biochemical assays and yeast-two-hybrid screens have confirmed HSCB’s direct interaction with ISCU and HSPA9 (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). In fact, human HSCB can functionally replace its yeast counterpart (Jac1) in S. cerevisiae, indicating conservation of these interactions (pmc.ncbi.nlm.nih.gov). Beyond these core partners, HSCB also associates with other components of the Fe–S assembly machinery. Notably, a 2011 study demonstrated that HSCB physically interacts with frataxin (FXN) (pmc.ncbi.nlm.nih.gov), the mitochondrial iron-binding protein deficient in Friedreich’s ataxia. Frataxin is thought to deliver or regulate iron for cluster synthesis, and the HSCB–frataxin interaction suggests a coordination between HSCB and iron supply. Perturbing HSCB levels had reciprocal effects on frataxin levels and altered cellular iron homeostasis, consistent with two proteins operating in the same pathway (pmc.ncbi.nlm.nih.gov). When HSCB was knocked down, cells showed misregulation of iron (increased transferrin receptor and IRP2 expression), indicating iron was not properly utilized – a hallmark of defective Fe–S assembly (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). This supports the idea that HSCB’s role in cluster transfer is critical not only for Fe–S enzyme maturation but also for maintaining overall iron balance in mitochondria.

Another emerging facet of HSCB’s role is its involvement in the cytosolic iron–sulfur protein assembly (CIA) pathway. While the de novo cluster synthesis occurs in mitochondria, many Fe–S proteins reside in the cytosol or nucleus and require a CIA machinery to receive their clusters. HSCB (or specifically a cytosolic form of it) has been found to form a bridge between these two cellular pathways. Mass spectrometry analysis in 2018 showed that a portion of HSCB (termed C-HSC20) can form a large complex containing both mitochondrial ISC components (HSPA9, ISCU) and CIA factors (CIAO1, MMS19, FAM96B) (pmc.ncbi.nlm.nih.gov). This suggests HSCB may travel or act at the interface, picking up a cluster in the mitochondrion and handing it to the CIA targeting complex in the cytosol. Indeed, HSCB’s binding to the CIAO1 protein (which has an LYR motif) provides a direct physical link: HSCB can dock onto CIAO1 and potentially transfer a cluster to it (pmc.ncbi.nlm.nih.gov). Two models have been proposed for cytosolic cluster delivery: in one, the HSPA9–HSCB system itself directly delivers clusters to certain cytosolic apoproteins (especially those that also have LYR motifs, e.g. CIAPIN1 or NUBP1/2) (pmc.ncbi.nlm.nih.gov). In the other model, HSCB primarily hands the cluster to the CIAO1/MMS19 complex (the CIA “targeting complex”), which then inserts it into various client proteins involved in DNA replication and repair (pmc.ncbi.nlm.nih.gov). Current evidence suggests both routes may exist – HSCB/HSPA9 might directly service a subset of Fe–S proteins, while also collaborating with CIA machinery for others (pmc.ncbi.nlm.nih.gov). This integrative role highlights HSCB as a central player ensuring that Fe–S clusters synthesized in mitochondria are efficiently distributed to all parts of the cell where they are needed.

Finally, HSCB’s importance is underscored by its participation in critical metabolic pathways. Fe–S cluster-dependent enzymes supported by HSCB include components of the tricarboxylic acid (TCA) cycle (e.g. aconitase in both mitochondria and cytosol), electron transport chain complexes (which contain Fe–S subunits, such as in Complex I and II), and enzymes like ferrochelatase (in heme biosynthesis) (pmc.ncbi.nlm.nih.gov). HSCB-driven cluster insertion is even indirectly necessary for mitochondrial lipoic acid synthesis, because the enzyme that synthesizes lipoate (lipoic acid synthase) itself requires an Fe–S cofactor (pmc.ncbi.nlm.nih.gov). Consistent with these roles, knocking down HSCB causes broad defects in Fe–S enzymes: cells with HSCB depletion show significantly reduced activities of Fe–S dependent enzymes such as succinate dehydrogenase (Complex II) and aconitase (pmc.ncbi.nlm.nih.gov). In one experiment, partial HSCB silencing to ~30% of normal levels led to total aconitase activity dropping to about 60% of control, and succinate dehydrogenase activity to about 85% of control (pmc.ncbi.nlm.nih.gov). With more complete HSCB knockdown, the impairment deepens – both mitochondrial and cytosolic aconitase activities decline, reflecting failure to insert clusters into these enzymes (pmc.ncbi.nlm.nih.gov). HSCB-deficient cells also fail to properly lipoylate the E2 subunits of pyruvate dehydrogenase and α-ketoglutarate dehydrogenase (which require lipoyl cofactors made by a Fe–S enzyme), linking HSCB to energy metabolism (pmc.ncbi.nlm.nih.gov). These molecular phenotypes translate into cellular fitness effects: HSCB knockdown causes slowed growth and heightened sensitivity to oxidative stress, while conversely HSCB overexpression can protect cells from oxidative damage (pmc.ncbi.nlm.nih.gov). Researchers observed that cells overexpressing HSCB recovered aconitase activity faster and survived better after peroxide or paraquat exposure, suggesting HSCB boosts the robustness of Fe–S cluster maintenance under stress (pmc.ncbi.nlm.nih.gov). This is logical, as oxidative stress tends to damage Fe–S clusters, and a strong HSCB–HSPA9 system would aid rapid repair or replacement of those clusters.

Recent Developments (2020–2024)

Recent research has further illuminated HSCB’s role and clinical significance. In 2020, a breakthrough genetics study identified mutations in HSCB as a cause of a human disease, solidifying HSCB’s importance. Specifically, Crispín et al. (JCI, 2020) reported that loss-of-function mutations in HSCB lead to congenital sideroblastic anemia (CSA), a rare inherited anemia characterized by iron-loaded immature red blood cells (pmc.ncbi.nlm.nih.gov) (www.jci.org). CSA had previously been linked to defects in mitochondrial Fe–S assembly (for example, mutations in GLRX5 and HSPA9 can cause similar anemias) (pmc.ncbi.nlm.nih.gov). The 2020 study found a patient with CSA who carried biallelic HSCB variants (including a frameshift and a promoter mutation) that reduced HSCB expression (www.jci.org). Functional tests confirmed that the patient’s cells had impaired Fe–S cluster-dependent enzymes and activated iron-starvation responses – essentially recapitulating what HSCB knockdown does in lab models. Morpholino knockdowns of HSCB in zebrafish likewise produced anemic phenotypes (diminished hemoglobinization), supporting that these mutations were indeed pathogenic (pmc.ncbi.nlm.nih.gov). Thanks to this finding, HSCB joins the list of critical Fe–S assembly genes whose disruption causes sideroblastic anemia, emphasizing that proper Fe–S cluster delivery is indispensable for red blood cell iron utilization and heme synthesis (pmc.ncbi.nlm.nih.gov). Clinically, this means HSCB genetic testing is now considered in work-ups of unexplained sideroblastic anemia – an example of how fundamental research on HSCB translated into a diagnostic insight (www.jci.org).

On the mechanistic front, late-2010s and 2020s studies have provided new insights into HSCB’s network of interactions. A 2018 study by Maio et al. delineated how cytosolic HSCB (C-HSC20) forms a multi-protein complex bridging mitochondrial and cytosolic Fe–S assembly systems (pmc.ncbi.nlm.nih.gov). This work used proteomics to show HSCB pulling together the ISC and CIA machineries, and it identified CIAO1’s LYR motif as the docking site for HSCB (pmc.ncbi.nlm.nih.gov). Their findings propose that HSCB not only works inside mitochondria, but also may escort Fe–S clusters out (or at least to the mitochondrial surface) and hand them to CIAO1 for further delivery in the cytosol (pmc.ncbi.nlm.nih.gov). This concept has prompted a refinement of the classical view of compartmentalized Fe–S assembly, suggesting a more integrated “Fe–S transfer pipeline” with HSCB as a critical link. Additionally, high-throughput interaction studies (yeast two-hybrid and proteomic screens) in 2021–2022 catalogued many new potential HSCB client proteins, thanks to the conserved LYR motif. Some notable targets include components of DNA repair (e.g. XPD, which contains Fe–S) and cytosolic enzymes, hinting that HSCB’s client repertoire might be broader than initially appreciated (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Structural biology also advanced: while the core structure of HSCB was known, recent analyses have focused on the dynamics of HSCB’s two-domain “L-shape” and its binding interfaces. The goal is to understand how HSCB distinguishes a scaffold protein like ISCU from a multitude of client proteins – research that has benefitted from NMR solution structures and mutational mapping of the HSCB–ISCU interface (pmc.ncbi.nlm.nih.gov). These studies confirm that a patch on HSCB’s C-terminal domain specifically recognizes ISCU’s amino acids, explaining the tight binding between HSCB and the cluster scaffold (pmc.ncbi.nlm.nih.gov). Together, such developments have enriched our understanding of HSCB as an adaptable adaptor protein that secures Fe–S cluster transfer in multiple contexts.

Another emerging area of interest is the role of HSCB in infectious disease and other conditions. Discoveries in 2022–2023 revealed that some viruses exploit host Fe–S assembly: for instance, the SARS-CoV-2 coronavirus encodes replication enzymes that contain Fe–S clusters. Recent work showed that the SARS-CoV-2 helicase and polymerase (RdRp) require Fe–S clusters for their activity and that these viral proteins can interact with human HSCB during infection (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Pull-down experiments with the coronavirus helicase found it could bind HSCB, presumably recruiting the host’s Fe–S insertion machinery to assemble the viral enzyme’s Fe–S center (pmc.ncbi.nlm.nih.gov). The Fe–S clusters in SARS-CoV-2 RdRp are essential for viral genome replication, so there is speculation that inhibiting HSCB or its partner HSPA9 could interfere with viral replication by preventing proper assembly of the viral polymerase (pmc.ncbi.nlm.nih.gov). While targeting such a fundamental host factor comes with risks (since HSCB is vital for the host as well), this line of research highlights HSCB as a potential host-targeted antiviral leverage point under investigation. More broadly, it underscores how deeply Fe–S biology is woven into cell function – even viruses must tap into HSCB’s machinery to build their required Fe–S proteins.

Expert Perspectives and Analysis

Scientific experts consider HSCB (DNAJC20) to be an integral component of the Fe–S cluster biogenesis pathway, with a role that is both specific and indispensable. A 2022 review in IUBMB Life summarizing mammalian Fe–S assembly referred to HSCB/HSC20 as “the dedicated co-chaperone that initiates the transfer of the Fe–S cluster from ISCU to recipient proteins” (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). The same review highlighted the unique evolutionary adaptation of HSCB: the presence of the tetracysteine domain in higher eukaryotes may allow dimerization or regulatory control, potentially tuning the chaperone’s activity (though its exact role “remains to be elucidated” (pmc.ncbi.nlm.nih.gov)). Dr. Tracey Rouault, a leading researcher in the field, and colleagues noted in 2010 that HSCB is an integral part of human ISC biosynthesis, given that its depletion alone was enough to impair multiple Fe–S enzymes and sensitize cells to oxidative damage (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). They pointed out that boosting HSCB levels could mitigate oxidative stress, suggesting HSCB is a limiting factor in how cells cope with Fe–S cluster damage (pmc.ncbi.nlm.nih.gov). Another expert, Gino Cortopassi, who studied HSCB’s connection to frataxin, emphasized that HSCB and frataxin “operate in the same pathway” and that altering one affects the other (pmc.ncbi.nlm.nih.gov). This insight ties HSCB to the broader context of mitochondrial iron management and disease (e.g. Friedreich’s ataxia).

From a clinical genetics standpoint, Dr. Mark Fleming’s group (authors of the 2020 CSA study) remarked that HSCB, HSPA9, and GLRX5 form a trio of factors necessary for Fe–S delivery in erythroid cells, and loss of any of them can cause sideroblastic anemia (pmc.ncbi.nlm.nih.gov). They noted that the discovery of HSCB mutations in anemia patients “further validates the paradigm that congenital anemias can result from defective mitochondrial Fe–S assembly”, an idea that was not obvious a decade ago. Importantly, these researchers underscore that such anemia is due not to lack of heme synthesis enzymes per se, but to a failure in the Fe–S cofactor assembly that indirectly cripples heme synthesis (ferrochelatase being Fe–S-dependent) (pmc.ncbi.nlm.nih.gov). This nuanced understanding, drawn from HSCB’s case, is shaping how physicians think about sideroblastic anemia and iron dysregulation disorders. In summary, expert analyses concur that HSCB is a key facilitator of Fe–S cluster trafficking, whose activity is finely tuned and connected to both cellular metabolic health and disease. There is a growing appreciation that studying HSCB can yield insights not just into a single chaperone, but into the entire network of iron–sulfur biology, oxidative stress response, and even pathogen–host interactions.

Conclusion

HSCB (DNAJC20) emerges as a pivotal co-chaperone in human cells dedicated to the biogenesis of iron–sulfur cluster proteins. It defines a specialized pathway in mitochondria that ensures newly synthesized Fe–S clusters are efficiently and specifically transferred to a broad array of recipient proteins, underlining its importance in fundamental processes from energy production to genome maintenance. Current understanding portrays HSCB as a molecular linchpin connecting mitochondrial Fe–S assembly with cytosolic Fe–S utilization, safeguarding iron homeostasis in the process. Recent research (2018–2024) has expanded HSCB’s known roles – revealing alternative isoforms in the cytosol, identifying client-binding motifs, linking HSCB mutations to human disease, and even implicating HSCB in the life cycle of viruses. The study of HSCB thus sits at the intersection of basic biochemistry and medicine. Ongoing investigations continue to uncover how HSCB’s unique structural features regulate its function and how this co-chaperone can be modulated, potentially offering new strategies to address diseases of iron mismanagement or to inhibit pathogens. In sum, HSCB is an excellent example of a highly conserved molecular assistant – one that, despite its diminutive size, plays an outsized role in maintaining the functional metalloproteome of the cell. Its precise action in Fe–S cluster delivery is essential for cellular viability, and disturbances in HSCB’s function reverberate through critical metabolic and genetic pathways, manifesting in observable clinical outcomes. As research progresses, HSCB remains a focal point for understanding the delicate choreography of metallochaperones that sustain life.

References (Selected):

Citations

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  18. AnnotationURLCitation(end_index=6105, start_index=5981, title='Structure of Human J-type Co-chaperone HscB Reveals a Tetracysteine Metal-binding Domain - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2573069/#:~:text=homologs%20is%20the%20presence%20of,like')
  19. AnnotationURLCitation(end_index=6682, start_index=6508, title='Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co-chaperone proteins - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10118776/#:~:text=transfer%20machinery.%5E%7B106%7D%20HSC20%20shares%2034,of%20bacterial%20and%20human%20co')
  20. AnnotationURLCitation(end_index=6853, start_index=6683, title='Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co-chaperone proteins - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10118776/#:~:text=residues%20being%20of%20crucial%20importance,it%20contains%2C%20downstream%20of%20the')
  21. AnnotationURLCitation(end_index=7559, start_index=7437, title='Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co-chaperone proteins - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10118776/#:~:text=Fe,SBD%20of%20the%20HSP70%20chaperone')
  22. AnnotationURLCitation(end_index=7818, start_index=7696, title='Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co-chaperone proteins - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10118776/#:~:text=Fe,SBD%20of%20the%20HSP70%20chaperone')
  23. AnnotationURLCitation(end_index=7968, start_index=7819, title='Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co-chaperone proteins - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10118776/#:~:text=HSC20%20is%20the%20component%20of,bound%20by%20HSC20%20as%20well')
  24. AnnotationURLCitation(end_index=8370, start_index=8248, title='Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co-chaperone proteins - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10118776/#:~:text=Fe,SBD%20of%20the%20HSP70%20chaperone')
  25. AnnotationURLCitation(end_index=8492, start_index=8371, title='Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co-chaperone proteins - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10118776/#:~:text=,association%20of%20ISCU%20and%20the')
  26. AnnotationURLCitation(end_index=8926, start_index=8805, title='Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co-chaperone proteins - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10118776/#:~:text=,association%20of%20ISCU%20and%20the')
  27. AnnotationURLCitation(end_index=9070, start_index=8927, title='Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co-chaperone proteins - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10118776/#:~:text=interaction%20of%20the%20NBD%20of,%284%29%20A%20nucleotide')
  28. AnnotationURLCitation(end_index=9410, start_index=9288, title='Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co-chaperone proteins - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10118776/#:~:text=Fe,SBD%20of%20the%20HSP70%20chaperone')
  29. AnnotationURLCitation(end_index=9554, start_index=9411, title='Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co-chaperone proteins - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10118776/#:~:text=interaction%20of%20the%20NBD%20of,%284%29%20A%20nucleotide')
  30. AnnotationURLCitation(end_index=9841, start_index=9698, title='Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co-chaperone proteins - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10118776/#:~:text=interaction%20of%20the%20NBD%20of,%284%29%20A%20nucleotide')
  31. AnnotationURLCitation(end_index=10274, start_index=10119, title='Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co-chaperone proteins - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10118776/#:~:text=recruitment%20of%20the%20HSC20%2FHSPA9,or%20lysine%20in%20position%203')
  32. AnnotationURLCitation(end_index=10643, start_index=10488, title='Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co-chaperone proteins - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10118776/#:~:text=recruitment%20of%20the%20HSC20%2FHSPA9,or%20lysine%20in%20position%203')
  33. AnnotationURLCitation(end_index=10818, start_index=10644, title='Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co-chaperone proteins - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10118776/#:~:text=HSC20%20to%20the%20LYR%20motif,targeting%20complex.%5E%7B128%7D%20Adopted%20from%5E%7B139')
  34. AnnotationURLCitation(end_index=11122, start_index=10967, title='Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co-chaperone proteins - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10118776/#:~:text=recruitment%20of%20the%20HSC20%2FHSPA9,or%20lysine%20in%20position%203')
  35. AnnotationURLCitation(end_index=11517, start_index=11377, title='HSC20 interacts with frataxin and is involved in iron–sulfur cluster biogenesis and iron homeostasis - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3298274/#:~:text=mitochondrial%20ISC%20assembly%20machinery,20%20%2C%2020')
  36. AnnotationURLCitation(end_index=11911, start_index=11755, title='Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co-chaperone proteins - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10118776/#:~:text=dedicated%20chaperone%2Fco,metabolism%20through%20direct%20binding%20of')
  37. AnnotationURLCitation(end_index=12493, start_index=12337, title='Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co-chaperone proteins - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10118776/#:~:text=dedicated%20chaperone%2Fco,metabolism%20through%20direct%20binding%20of')
  38. AnnotationURLCitation(end_index=12668, start_index=12494, title='Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co-chaperone proteins - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10118776/#:~:text=HSC20%20to%20the%20LYR%20motif,targeting%20complex.%5E%7B128%7D%20Adopted%20from%5E%7B139')
  39. AnnotationURLCitation(end_index=13453, start_index=13287, title='Characterization of the human HSC20, an unusual DnaJ type III protein, involved in iron–sulfur cluster biogenesis - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2935859/#:~:text=specialized%20DnaJ%20type%20co,deficient%20cells.%20Conversely%2C%20overexpression')
  40. AnnotationURLCitation(end_index=13576, start_index=13454, title='Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co-chaperone proteins - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10118776/#:~:text=Fe,SBD%20of%20the%20HSP70%20chaperone')
  41. AnnotationURLCitation(end_index=13904, start_index=13718, title='Characterization of the human HSC20, an unusual DnaJ type III protein, involved in iron–sulfur cluster biogenesis - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2935859/#:~:text=The%20importance%20of%20mitochondrial%20iron%E2%80%93sulfur,However%2C%20small%20amounts%20were%20also')
  42. AnnotationURLCitation(end_index=14278, start_index=14099, title='HSC20 interacts with frataxin and is involved in iron–sulfur cluster biogenesis and iron homeostasis - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3298274/#:~:text=suggesting%20a%20potential%20therapeutic%20strategy,studies%20of%20mammalian%20ISC%20biogenesis')
  43. AnnotationURLCitation(end_index=14822, start_index=14679, title='HSC20 interacts with frataxin and is involved in iron–sulfur cluster biogenesis and iron homeostasis - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3298274/#:~:text=and%20also%20defects%20in%20ISC,may%20act%20late%20in%20the')
  44. AnnotationURLCitation(end_index=15199, start_index=15027, title='HSC20 interacts with frataxin and is involved in iron–sulfur cluster biogenesis and iron homeostasis - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3298274/#:~:text=expected%20of%20two%20cooperating%20proteins,studies%20of%20mammalian%20ISC%20biogenesis')
  45. AnnotationURLCitation(end_index=15374, start_index=15200, title='HSC20 interacts with frataxin and is involved in iron–sulfur cluster biogenesis and iron homeostasis - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3298274/#:~:text=altered%20cytosolic%20and%20mitochondrial%20iron,apoproteins%20and%20that%20HSC20%20should')
  46. AnnotationURLCitation(end_index=16330, start_index=16174, title='Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co-chaperone proteins - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10118776/#:~:text=the%20components%20of%20the%20de,the%20interaction%20with%20the%20viral')
  47. AnnotationURLCitation(end_index=16817, start_index=16661, title='Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co-chaperone proteins - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10118776/#:~:text=dedicated%20chaperone%2Fco,metabolism%20through%20direct%20binding%20of')
  48. AnnotationURLCitation(end_index=17204, start_index=17048, title='Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co-chaperone proteins - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10118776/#:~:text=dedicated%20chaperone%2Fco,metabolism%20through%20direct%20binding%20of')
  49. AnnotationURLCitation(end_index=17563, start_index=17407, title='Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co-chaperone proteins - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10118776/#:~:text=dedicated%20chaperone%2Fco,metabolism%20through%20direct%20binding%20of')
  50. AnnotationURLCitation(end_index=17891, start_index=17735, title='Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co-chaperone proteins - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10118776/#:~:text=dedicated%20chaperone%2Fco,metabolism%20through%20direct%20binding%20of')
  51. AnnotationURLCitation(end_index=18671, start_index=18503, title='Mutations in the iron-sulfur cluster biogenesis protein HSCB cause congenital sideroblastic anemia - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7524500/#:~:text=clusters%2C%20such%20as%20FECH%20and,complexes%2C%20likely%20because%20lipoic%20acid')
  52. AnnotationURLCitation(end_index=19045, start_index=18877, title='Mutations in the iron-sulfur cluster biogenesis protein HSCB cause congenital sideroblastic anemia - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7524500/#:~:text=clusters%2C%20such%20as%20FECH%20and,complexes%2C%20likely%20because%20lipoic%20acid')
  53. AnnotationURLCitation(end_index=19440, start_index=19286, title='Characterization of the human HSC20, an unusual DnaJ type III protein, involved in iron–sulfur cluster biogenesis - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2935859/#:~:text=match%20at%20L511%20oligo1%20and,was%20affected%20earlier%20and%20more')
  54. AnnotationURLCitation(end_index=19798, start_index=19644, title='Characterization of the human HSC20, an unusual DnaJ type III protein, involved in iron–sulfur cluster biogenesis - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2935859/#:~:text=match%20at%20L511%20oligo1%20and,was%20affected%20earlier%20and%20more')
  55. AnnotationURLCitation(end_index=20130, start_index=19984, title='Characterization of the human HSC20, an unusual DnaJ type III protein, involved in iron–sulfur cluster biogenesis - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2935859/#:~:text=specifically%20reduced%20the%20activities%20of,These%20results')
  56. AnnotationURLCitation(end_index=20526, start_index=20351, title='Mutations in the iron-sulfur cluster biogenesis protein HSCB cause congenital sideroblastic anemia - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7524500/#:~:text=HSCB%20knockdown%20also%20impaired%20the,RC%20proteins%2C%20Seahorse%20extracellular%20flux')
  57. AnnotationURLCitation(end_index=20907, start_index=20761, title='Characterization of the human HSC20, an unusual DnaJ type III protein, involved in iron–sulfur cluster biogenesis - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2935859/#:~:text=specifically%20reduced%20the%20activities%20of,These%20results')
  58. AnnotationURLCitation(end_index=21279, start_index=21133, title='Characterization of the human HSC20, an unusual DnaJ type III protein, involved in iron–sulfur cluster biogenesis - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2935859/#:~:text=specifically%20reduced%20the%20activities%20of,These%20results')
  59. AnnotationURLCitation(end_index=22044, start_index=21912, title='Mutations in the iron-sulfur cluster biogenesis protein HSCB cause congenital sideroblastic anemia - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7524500/#:~:text=The%20congenital%20sideroblastic%20anemias%20,We')
  60. AnnotationURLCitation(end_index=22200, start_index=22045, title='JCI - Mutations in the iron-sulfur cluster biogenesis protein HSCB cause congenital sideroblastic anemia', type='url_citation', url='https://www.jci.org/articles/view/135479#:~:text=The%20congenital%20sideroblastic%20anemias%20,mitochondrial%20heat%20shock%20protein%20A9')
  61. AnnotationURLCitation(end_index=22485, start_index=22353, title='Mutations in the iron-sulfur cluster biogenesis protein HSCB cause congenital sideroblastic anemia - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7524500/#:~:text=The%20congenital%20sideroblastic%20anemias%20,We')
  62. AnnotationURLCitation(end_index=22718, start_index=22641, title='JCI - Mutations in the iron-sulfur cluster biogenesis protein HSCB cause congenital sideroblastic anemia', type='url_citation', url='https://www.jci.org/articles/view/135479#:~:text=CSA,derived')
  63. AnnotationURLCitation(end_index=23243, start_index=23091, title='Mutations in the iron-sulfur cluster biogenesis protein HSCB cause congenital sideroblastic anemia - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7524500/#:~:text=expression%20and%20the%20effect%20of,but%20a%20reduced%20number%20of')
  64. AnnotationURLCitation(end_index=23621, start_index=23489, title='Mutations in the iron-sulfur cluster biogenesis protein HSCB cause congenital sideroblastic anemia - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7524500/#:~:text=The%20congenital%20sideroblastic%20anemias%20,We')
  65. AnnotationURLCitation(end_index=23896, start_index=23819, title='JCI - Mutations in the iron-sulfur cluster biogenesis protein HSCB cause congenital sideroblastic anemia', type='url_citation', url='https://www.jci.org/articles/view/135479#:~:text=CSA,derived')
  66. AnnotationURLCitation(end_index=24340, start_index=24184, title='Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co-chaperone proteins - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10118776/#:~:text=the%20components%20of%20the%20de,the%20interaction%20with%20the%20viral')
  67. AnnotationURLCitation(end_index=24648, start_index=24492, title='Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co-chaperone proteins - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10118776/#:~:text=dedicated%20chaperone%2Fco,metabolism%20through%20direct%20binding%20of')
  68. AnnotationURLCitation(end_index=25023, start_index=24867, title='Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co-chaperone proteins - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10118776/#:~:text=dedicated%20chaperone%2Fco,metabolism%20through%20direct%20binding%20of')
  69. AnnotationURLCitation(end_index=25741, start_index=25592, title='Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co-chaperone proteins - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10118776/#:~:text=HSC20%20is%20the%20component%20of,bound%20by%20HSC20%20as%20well')
  70. AnnotationURLCitation(end_index=25916, start_index=25742, title='Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co-chaperone proteins - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10118776/#:~:text=HSC20%20to%20the%20LYR%20motif,targeting%20complex.%5E%7B128%7D%20Adopted%20from%5E%7B139')
  71. AnnotationURLCitation(end_index=26466, start_index=26328, title='Solution Structure of the Iron−Sulfur Cluster Cochaperone HscB and Its Binding Surface for the Iron−Sulfur Assembly Scaffold Protein IscU - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2627783/#:~:text=Solution%20Structure%20of%20the%20Iron%E2%88%92Sulfur,')
  72. AnnotationURLCitation(end_index=26780, start_index=26642, title='Solution Structure of the Iron−Sulfur Cluster Cochaperone HscB and Its Binding Surface for the Iron−Sulfur Assembly Scaffold Protein IscU - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2627783/#:~:text=Solution%20Structure%20of%20the%20Iron%E2%88%92Sulfur,')
  73. AnnotationURLCitation(end_index=27577, start_index=27412, title='An iron–sulfur cluster in the zinc-binding domain of the SARS-CoV-2 helicase modulates its RNA-binding and -unwinding activities - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10438387/#:~:text=An%20iron%E2%80%93sulfur%20cluster%20in%20the,nsp13%20proteins%20was%20performed')
  74. AnnotationURLCitation(end_index=27734, start_index=27578, title='Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co-chaperone proteins - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10118776/#:~:text=the%20components%20of%20the%20de,the%20interaction%20with%20the%20viral')
  75. AnnotationURLCitation(end_index=28080, start_index=27915, title='An iron–sulfur cluster in the zinc-binding domain of the SARS-CoV-2 helicase modulates its RNA-binding and -unwinding activities - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10438387/#:~:text=An%20iron%E2%80%93sulfur%20cluster%20in%20the,nsp13%20proteins%20was%20performed')
  76. AnnotationURLCitation(end_index=28482, start_index=28326, title='Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co-chaperone proteins - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10118776/#:~:text=the%20components%20of%20the%20de,the%20interaction%20with%20the%20viral')
  77. AnnotationURLCitation(end_index=29408, start_index=29286, title='Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co-chaperone proteins - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10118776/#:~:text=Fe,SBD%20of%20the%20HSP70%20chaperone')
  78. AnnotationURLCitation(end_index=29579, start_index=29409, title='Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co-chaperone proteins - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10118776/#:~:text=residues%20being%20of%20crucial%20importance,it%20contains%2C%20downstream%20of%20the')
  79. AnnotationURLCitation(end_index=30029, start_index=29859, title='Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co-chaperone proteins - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10118776/#:~:text=residues%20being%20of%20crucial%20importance,it%20contains%2C%20downstream%20of%20the')
  80. AnnotationURLCitation(end_index=30477, start_index=30291, title='Characterization of the human HSC20, an unusual DnaJ type III protein, involved in iron–sulfur cluster biogenesis - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2935859/#:~:text=The%20importance%20of%20mitochondrial%20iron%E2%80%93sulfur,However%2C%20small%20amounts%20were%20also')
  81. AnnotationURLCitation(end_index=30624, start_index=30478, title='Characterization of the human HSC20, an unusual DnaJ type III protein, involved in iron–sulfur cluster biogenesis - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2935859/#:~:text=specifically%20reduced%20the%20activities%20of,These%20results')
  82. AnnotationURLCitation(end_index=30932, start_index=30786, title='Characterization of the human HSC20, an unusual DnaJ type III protein, involved in iron–sulfur cluster biogenesis - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2935859/#:~:text=specifically%20reduced%20the%20activities%20of,These%20results')
  83. AnnotationURLCitation(end_index=31259, start_index=31116, title='HSC20 interacts with frataxin and is involved in iron–sulfur cluster biogenesis and iron homeostasis - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3298274/#:~:text=and%20also%20defects%20in%20ISC,may%20act%20late%20in%20the')
  84. AnnotationURLCitation(end_index=31775, start_index=31643, title='Mutations in the iron-sulfur cluster biogenesis protein HSCB cause congenital sideroblastic anemia - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7524500/#:~:text=The%20congenital%20sideroblastic%20anemias%20,We')
  85. AnnotationURLCitation(end_index=32370, start_index=32238, title='Mutations in the iron-sulfur cluster biogenesis protein HSCB cause congenital sideroblastic anemia - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7524500/#:~:text=The%20congenital%20sideroblastic%20anemias%20,We')
  86. AnnotationURLCitation(end_index=34997, start_index=34811, title='Characterization of the human HSC20, an unusual DnaJ type III protein, involved in iron–sulfur cluster biogenesis - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2935859/#:~:text=The%20importance%20of%20mitochondrial%20iron%E2%80%93sulfur,However%2C%20small%20amounts%20were%20also')
  87. AnnotationURLCitation(end_index=35164, start_index=34998, title='Characterization of the human HSC20, an unusual DnaJ type III protein, involved in iron–sulfur cluster biogenesis - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2935859/#:~:text=counterpart%20in%20yeast%2C%20Jac1p%2C%20and,of%20the%20human%20ISC%20biosynthetic')
  88. AnnotationURLCitation(end_index=35465, start_index=35286, title='HSC20 interacts with frataxin and is involved in iron–sulfur cluster biogenesis and iron homeostasis - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3298274/#:~:text=suggesting%20a%20potential%20therapeutic%20strategy,studies%20of%20mammalian%20ISC%20biogenesis')
  89. AnnotationURLCitation(end_index=35640, start_index=35466, title='HSC20 interacts with frataxin and is involved in iron–sulfur cluster biogenesis and iron homeostasis - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3298274/#:~:text=altered%20cytosolic%20and%20mitochondrial%20iron,apoproteins%20and%20that%20HSC20%20should')
  90. AnnotationURLCitation(end_index=35861, start_index=35755, title='Structure of Human J-type Co-chaperone HscB Reveals a Tetracysteine Metal-binding Domain - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2573069/#:~:text=mitochondrial%20J,like')
  91. AnnotationURLCitation(end_index=36136, start_index=35980, title='Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co-chaperone proteins - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10118776/#:~:text=the%20components%20of%20the%20de,the%20interaction%20with%20the%20viral')
  92. AnnotationURLCitation(end_index=36293, start_index=36137, title='Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co-chaperone proteins - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10118776/#:~:text=dedicated%20chaperone%2Fco,metabolism%20through%20direct%20binding%20of')
  93. AnnotationURLCitation(end_index=36530, start_index=36398, title='Mutations in the iron-sulfur cluster biogenesis protein HSCB cause congenital sideroblastic anemia - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7524500/#:~:text=The%20congenital%20sideroblastic%20anemias%20,We')
  94. AnnotationURLCitation(end_index=36608, start_index=36531, title='JCI - Mutations in the iron-sulfur cluster biogenesis protein HSCB cause congenital sideroblastic anemia', type='url_citation', url='https://www.jci.org/articles/view/135479#:~:text=CSA,derived')
  95. AnnotationURLCitation(end_index=36839, start_index=36717, title='Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co-chaperone proteins - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10118776/#:~:text=Fe,SBD%20of%20the%20HSP70%20chaperone')
  96. AnnotationURLCitation(end_index=36995, start_index=36840, title='Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co-chaperone proteins - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10118776/#:~:text=recruitment%20of%20the%20HSC20%2FHSPA9,or%20lysine%20in%20position%203')
  97. AnnotationURLCitation(end_index=37246, start_index=37091, title='HSCB HscB mitochondrial iron-sulfur cluster cochaperone [Homo sapiens (human)] - Gene - NCBI', type='url_citation', url='https://www.ncbi.nlm.nih.gov/gene/150274#:~:text=This%20gene%20encodes%20a%20DnaJ,results%20in%20multiple%20transcript%20variants')