Chaperone Proteins: Guardians of Protein Folding and Function

By Dr. Zubair Khalid, DVM, MS, PhD · 2026-08-11

Introduction to Chaperone Proteins

Proteins must fold into precise three-dimensional structures to function. The information for this folding is encoded in the amino acid sequence itself, yet the cellular environment presents formidable obstacles to spontaneous folding. Chaperone proteins are a diverse class of molecular assistants that bind to non-native proteins, stabilize them, and facilitate their progression to the native state—without becoming part of the final functional structure. They do not dictate the fold; they create the conditions under which the polypeptide can find it.

The term "chaperone" was coined in 1978 by Ron Laskey and colleagues studying nucleoplasmin, a protein that assists nucleosome assembly in Xenopus oocytes. They observed that nucleoplasmin was required for correct DNA–histone interactions but was absent from the final assembled nucleosome. The analogy to a human chaperone—present to ensure proper behavior but not part of the event itself—was apt and has persisted.

Historical context: from heat shock proteins to chaperones

The foundational discovery came earlier, in 1962, when Ferruccio Ritossa observed that heat shock induced a characteristic puffing pattern in Drosophila salivary gland chromosomes, indicating active transcription of specific genes. The protein products of these heat shock genes—the heat shock proteins (Hsps)—were later found to be induced by elevated temperature and other stresses. For years, their function remained obscure.

The connection between heat shock proteins and protein folding emerged in the 1980s. Work by Hugh Pelham suggested that Hsps might repair denatured proteins. John Ellis then proposed that these proteins, which he called "molecular chaperones," assist protein folding generally, not just under stress. The realization that Hsp70 and Hsp60 families are constitutively expressed and participate in normal protein biogenesis transformed the field. Today, "chaperone" is the functional term; "heat shock protein" refers to the historical discovery context and the inducible expression of many family members.

Chaperones vs. chaperonins: what's the difference?

The terms are often confused. Chaperones is the broad category: any protein that assists others in folding, assembly, transport, or degradation without being part of the final complex. Chaperonins are a specific subclass—large, barrel-shaped complexes that provide an enclosed chamber for a single polypeptide to fold in isolation. The bacterial chaperonin GroEL with its lid GroES is the paradigm. All chaperonins are chaperones, but not all chaperones are chaperonins. Hsp70 and Hsp90, for example, are chaperones that bind their substrates directly without enclosing them.

Why Cells Need Chaperone Proteins

The protein folding problem

Anfinsen's classic experiments in the 1960s demonstrated that ribonuclease A could refold spontaneously in vitro after denaturation, establishing the thermodynamic hypothesis: the amino acid sequence contains all information needed for the native structure. However, this experiment was performed at micromolar protein concentrations in dilute buffer. The cellular reality is starkly different.

The protein folding problem has two dimensions. First, the conformational search problem: a protein of 100 amino acids has an astronomically large number of possible conformations. Levinthal estimated that if a protein sampled conformations at the rate of 10¹³ per second, finding the native state by random search would take longer than the age of the universe. Proteins solve this through funneled energy landscapes—the native state is a deep minimum, and partially folded intermediates guide the search—but the landscape is rugged, with kinetic traps.

Second, the timescale problem: many proteins fold in milliseconds to seconds in vitro, which is fast enough, but they must do so in a crowded, viscous cellular environment while still attached to the ribosome. The Ribosome Make Protein process produces polypeptides vectorially from N-terminus to C-terminus, meaning folding begins co-translationally, before the entire sequence is available. This creates a strong risk of misfolding.

Cellular crowding and the danger of aggregation

The cytoplasm contains 200–400 mg/mL of macromolecules—proteins, nucleic acids, polysaccharides. This macromolecular crowding has two consequences. First, it dramatically increases the effective concentration of any given protein, favoring intermolecular interactions. Second, it reduces the volume available for a polypeptide to explore conformational space. Both effects promote aggregation.

The danger is real: misfolded proteins expose hydrophobic patches that are normally buried in the native structure. These patches drive non-specific association, producing amorphous aggregates or ordered amyloid fibrils. Aggregation is concentration-dependent and often irreversible. Once a protein aggregates, it is not merely non-functional—it can sequester other proteins, including essential chaperones, and in the case of amyloid, disrupt membranes and cause cell death. The cell therefore invests heavily in preventing aggregation from the moment a nascent chain emerges from the ribosome.

Mechanisms of Chaperone Action

Binding and release cycles

The unifying principle of chaperone action is the regulated binding and release of hydrophobic surfaces. Chaperones recognize features common to non-native states: exposed hydrophobic patches, unstructured regions, and unpaired β-strands. These features are absent in the native state, giving chaperones specificity for unfolded or misfolded conformers.

The binding itself serves two purposes. First, it shields hydrophobic surfaces from the solvent and from other proteins, preventing aggregation. Second, it can actively unfold misfolded intermediates, giving the polypeptide another chance to fold correctly. This "iterative annealing" mechanism is best characterized for Hsp70: binding of the chaperone to a misfolded state destabilizes it, promoting unfolding, and release allows refolding to attempt again.

Binding and release must be regulated. If a chaperone bound too tightly, the substrate would never be released; if too weakly, aggregation would proceed. The solution is an ATP-driven cycle that alternates between high-affinity and low-affinity states.

ATP hydrolysis as an energy source

ATP hydrolysis provides the energy for conformational changes in the chaperone, not for the folding of the substrate itself. The folding reaction is thermodynamically downhill; the chaperone's job is to prevent off-pathway reactions. ATP binding and hydrolysis act as a timer and a switch.

For Hsp70, the cycle is as follows:

1. ATP-bound state: The substrate-binding domain has low affinity and fast exchange rates for substrate. The lid is open.
2. Substrate binding: A non-native protein binds to the open substrate-binding domain.
3. ATP hydrolysis: Stimulated by the substrate and by a co-chaperone (J-protein), ATP is hydrolyzed to ADP. This induces a conformational change that closes the lid, trapping the substrate with high affinity.
4. ADP-bound state: The substrate is held tightly for seconds, allowing it to fold or be transferred to another chaperone.
5. Nucleotide exchange: A nucleotide exchange factor (NEF) displaces ADP, allowing ATP to bind again. The lid opens, and the substrate is released.

The cycle repeats. Each round costs one ATP. The chaperone does not "know" whether the substrate has folded; it simply releases and, if the substrate is still non-native, rebinds.

The Anfinsen cage model

Chaperonins operate on a different principle. GroEL is a tetradecamer: two heptameric rings stacked back-to-back, forming a barrel with a central cavity. Each ring has an ATP-binding site. The co-chaperone GroES is a heptameric dome that binds to the opening of the ring.

The mechanism is as follows:

1. A non-native protein binds to hydrophobic patches lining the cavity rim of the open ring.
2. ATP binds to the ring, inducing a conformational change that displaces the substrate into the central cavity.
3. GroES binds, capping the cavity and displacing the hydrophobic patches. The cavity interior becomes hydrophilic.
4. The substrate is now enclosed in a cage of ~60 Å diameter, isolated from the cellular environment. It folds in solitude.
5. ATP hydrolysis in the opposite ring triggers release of GroES and the substrate—folded or not.

The cage serves multiple functions: it provides a confined space that prevents aggregation, it removes the substrate from the crowded cytoplasm, and the hydrophilic walls may promote folding by favoring burial of hydrophobic residues. The term "Anfinsen cage" honors Christian Anfinsen, whose work established that folding is spontaneous given the right conditions. The chaperonin provides those conditions.

Major Families of Chaperone Proteins

Hsp70: the ATP-dependent binding protein

Hsp70 (DnaK in E. coli, BiP in the ER, Hsc70 in the cytosol) is the most abundant chaperone family. It consists of two domains: an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD), connected by a flexible linker. The SBD contains a β-sandwich pocket that binds extended stretches of 5–7 hydrophobic residues, typically flanked by basic residues. Such sequences occur, on average, every 40 amino acids in proteins, making Hsp70 a generalist that can bind almost any non-native protein.

Hsp70 functions in multiple contexts: co-translational folding (binding nascent chains emerging from the ribosome), translocation of proteins across membranes (holding them in an unfolded state), disassembly of protein complexes, and delivery of substrates to other chaperones. Its binding specificity for extended, hydrophobic stretches means it recognizes early folding intermediates and prevents their aggregation.

The J-protein co-chaperones (Hsp40/DnaJ) deliver substrates to Hsp70 and stimulate ATP hydrolysis. There are dozens of J-proteins in eukaryotic cells, each with distinct localization and substrate specificity, allowing Hsp70 to be directed to specific tasks. Nucleotide exchange factors (GrpE in bacteria, BAG family and Hsp110 in eukaryotes) complete the cycle.

Hsp90: the maturation of signaling proteins

Hsp90 is a dimeric chaperone that functions as a dimer of dimers, with each monomer containing an N-terminal ATP-binding domain, a middle domain, and a C-terminal dimerization domain. Unlike Hsp70, Hsp90 does not bind extended hydrophobic stretches; it recognizes partially folded, "near-native" states of specific client proteins.

The clientele of Hsp90 is remarkably specific: steroid hormone receptors, kinases (including many oncogenes), telomerase, and other signaling proteins. Hsp90 is required for the final maturation of these clients—the last step in their folding, often involving ligand binding or assembly into complexes. Hsp90 works with a large cohort of co-chaperones (more than 20 in humans) that modulate its ATPase activity and recruit specific clients.

The ATPase cycle of Hsp90 involves large conformational changes: ATP binding induces dimerization of the N-terminal domains, closing the chaperone into a molecular clamp around the client. Hydrolysis and ADP release reopen the clamp. The cycle is slow (minutes), reflecting the fact that Hsp90 clients fold slowly and require prolonged chaperone association.

Hsp90 is of particular interest in cancer biology because many of its clients are oncoproteins. Inhibitors of Hsp90 (geldanamycin, 17-AAG) are being investigated as anti-cancer drugs; they work by preventing the maturation of multiple oncogenic kinases simultaneously.

Chaperonins: the barrel-shaped folding chambers

Chaperonins are divided into two groups. Group I includes bacterial GroEL, mitochondrial Hsp60, and chloroplast Cpn60. These require a co-chaperonin lid (GroES, Hsp10, Cpn10). Group II includes archaeal thermosomes and eukaryotic TRiC/CCT (TCP-1 ring complex). Group II chaperonins have a built-in lid and do not require a separate co-chaperonin.

TRiC/CCT is particularly important in eukaryotes: it is the only chaperonin in the cytosol and is obligate for the folding of actin and tubulin, which cannot fold spontaneously even in dilute solution. TRiC is a hetero-oligomer of eight different subunits, each with distinct substrate-binding properties, allowing it to recognize a broader range of substrates than the homo-oligomeric GroEL.

The chaperonin mechanism is ATP-driven, but the timing differs between groups. GroEL/GroES uses a two-stroke motor: ATP binding to one ring drives the folding cycle in that ring while the opposite ring is in the ADP state. TRiC uses a sequential mechanism in which ATP hydrolysis in individual subunits occurs in a defined order, producing a progressive conformational change.

Small heat shock proteins: ATP-independent holdases

Small heat shock proteins (sHsps) are the simplest chaperones: they are ATP-independent and bind non-native proteins to prevent aggregation, but they do not actively refold them. They are "holdases" rather than "foldases." sHsps form large oligomeric complexes (12–40 subunits) that bind denatured proteins on their surface, sequestering them until ATP-dependent chaperones (Hsp70/Hsp100) can extract and refold them.

sHsps are strongly induced by stress and are particularly abundant in muscle and lens tissue. Mutations in human sHsps (HSPB1, HSPB8) cause inherited neuropathies and myopathies, demonstrating their physiological importance. Their ATP-independence makes them effective under conditions of energy depletion, when ATP-dependent chaperones would be inactive.

The following table summarizes the major chaperone families:

Chaperones in Protein Quality Control

Triaging: refolding vs. degradation

Chaperones do not work alone. They are integrated into a protein quality control network that decides the fate of every polypeptide: fold, hold, or degrade. The decision depends on the persistence of the non-native state. If a protein fails to fold after multiple chaperone cycles, it must be eliminated to prevent aggregation.

The connection between chaperones and degradation is direct. Hsp70 and Hsp90 can deliver misfolded proteins to the ubiquitin-proteasome system. In the cytosol, the E3 ubiquitin ligase CHIP (C-terminus of Hsp70-interacting protein) binds to both Hsp70 and Hsp90. When a client remains bound to the chaperone for too long, CHIP ubiquitinates it, targeting it for degradation by the proteasome. This is a classic example of chaperone-mediated triage: the chaperone holds the substrate, and the duration of holding determines whether it is refolded or destroyed.

The Targeted Protein Degradation pathway and the Proteasome Protein Degradation machinery are the executioners. The Two Phases of Protein Degradation—ubiquitination followed by proteasomal processing—are both influenced by chaperone activity. In the endoplasmic reticulum, a parallel system called ER-associated degradation (ERAD) uses BiP (Hsp70) to recognize misfolded proteins and retrotranslocate them to the cytosol for degradation. The Forms of Protein Degradation thus include both chaperone-dependent and chaperone-independent routes, but the chaperone-dependent route is the primary quality control mechanism.

Co-chaperones and the chaperone network

Chaperones function as networks, not isolated actors. Co-chaperones are proteins that regulate chaperone activity without being chaperones themselves. They include:

• J-proteins (Hsp40): Stimulate Hsp70 ATPase activity and deliver substrates.
• Nucleotide exchange factors: Promote ADP release from Hsp70.
• HOP (Hsp70-Hsp90 organizing protein): Transfers clients from Hsp70 to Hsp90.
• CHIP: Ubiquitinates chaperone-bound clients, committing them to degradation.
• p23: Stabilizes the Hsp90-client complex.
• Immunophilins: Link Hsp90 complexes to steroid hormone receptors.

The sequential action of chaperones is well illustrated by the folding of steroid hormone receptors. The receptor is first bound by Hsp70, transferred to Hsp90 via HOP, and then matured in an Hsp90 complex containing p23 and an immunophilin. This ordered pathway ensures that the receptor reaches a ligand-binding-competent state.

Chaperones and Disease

Protein aggregation diseases

Neurodegenerative diseases are characterized by the accumulation of misfolded protein aggregates. Alzheimer's disease features amyloid-β plaques and tau tangles; Parkinson's disease features α-synuclein Lewy bodies; Huntington's disease features polyglutamine aggregates of huntingtin. In each case, the aggregating protein is normally soluble but adopts an aberrant conformation that seeds aggregation.

Chaperones are the first line of defense against these aggregates. Overexpression of Hsp70 or Hsp40 suppresses polyglutamine toxicity in animal models of Huntington's disease. Hsp70 and Hsp90 can bind α-synuclein and inhibit its fibrillization. Small heat shock proteins are found in Lewy bodies and amyloid plaques, suggesting they are recruited to contain the damage.

However, chaperone capacity is finite. Under chronic stress or with aging, chaperone expression declines, and the proteostasis network becomes overwhelmed. The Protein Misfolding that results is both a cause and a consequence of chaperone dysfunction. The aggregates themselves can sequester chaperones, reducing their availability for other clients and creating a vicious cycle.

Chaperones as drug targets

Chaperones are attractive drug targets for two opposing reasons. In cancer, Hsp90 inhibitors (17-AAG, ganetespib) are being developed because they simultaneously destabilize multiple oncogenic clients. The rationale is that cancer cells are particularly dependent on Hsp90 to maintain the activity of mutated, unstable oncoproteins. Inhibiting Hsp90 causes these clients to be degraded, killing the cancer cell.

In neurodegeneration, the goal is the opposite: to enhance chaperone activity. Pharmacological upregulation of Hsp70 and Hsp90 has been shown to reduce aggregation and toxicity in models of Huntington's and Parkinson's diseases. Compounds that activate the heat shock response, such as geldanamycin (ironically also an Hsp90 inhibitor), induce Hsp70 expression and are protective.

The therapeutic window is narrow. Too much chaperone activity could interfere with normal protein turnover, while too little accelerates aggregation. The challenge is to modulate specific chaperone-client interactions without disrupting global proteostasis.

Methods to Study Chaperone Proteins

In vitro reconstitution

The classic approach is to purify a chaperone and its substrate, then assay folding in a test tube. A typical experiment uses a model substrate such as firefly luciferase or malate dehydrogenase, which are easily denatured and whose activity can be measured. The substrate is denatured with urea or guanidinium chloride, then diluted into a refolding buffer containing the chaperone, ATP, and an ATP-regenerating system (creatine phosphate/creatine kinase or phosphoenolpyruvate/pyruvate kinase). Refolding is monitored by measuring enzyme activity over time.

Control experiments are essential: the substrate alone (to show spontaneous refolding), the chaperone without ATP (to show the energy requirement), and the chaperone with a non-hydrolyzable ATP analog such as AMP-PNP (to show that hydrolysis, not just binding, is required). Typical buffer conditions are 25 mM HEPES pH 7.5, 50 mM KCl, 5 mM MgCl₂, 2 mM ATP, at 25–30°C.

ATPase activity is measured using a coupled assay: pyruvate kinase converts ADP and phosphoenolpyruvate to ATP and pyruvate; lactate dehydrogenase then converts pyruvate and NADH to lactate and NAD⁺, and the decrease in NADH absorbance at 340 nm is monitored. This allows real-time measurement of ATP hydrolysis rates.

Structural biology approaches

X-ray crystallography has provided high-resolution structures of GroEL, Hsp70, Hsp90, and their complexes. The GroEL-GroES-ADP structure, solved in the 1990s, revealed the Anfinsen cage in atomic detail. However, crystallography requires stable, homogeneous samples and captures a single conformation.

Cryo-electron microscopy (cryo-EM) has revolutionized the field by allowing structures of chaperone complexes in multiple conformations to be determined. Single-particle cryo-EM has captured GroEL-GroES in different nucleotide states, TRiC with bound actin, and Hsp90 with client proteins. The ability to sort particles into conformational classes provides a movie of the chaperone cycle.

Single-molecule studies

Single-molecule fluorescence techniques—Förster resonance energy transfer (FRET), fluorescence correlation spectroscopy, and optical tweezers—allow observation of individual chaperone-substrate interactions in real time. These methods reveal heterogeneity that is hidden in ensemble measurements: some substrate molecules fold rapidly, others slowly, and the chaperone interacts with each differently.

Single-molecule FRET has been used to show that GroEL actively unfolds misfolded substrates, that Hsp70 binds and releases substrates stochastically, and that the Hsp90 ATPase cycle is highly irregular, with dwell times varying from milliseconds to minutes. Optical tweezers have measured the mechanical force exerted by chaperones on their substrates, showing that ClpB (a bacterial disaggregase) can unfold proteins by translocating them through its central pore.

Common Pitfalls and Misconceptions

Chaperones do not determine the final fold

The most persistent misconception is that chaperones "tell" proteins how to fold or that they contribute steric information to the final structure. They do not. The native structure is determined entirely by the amino acid sequence. Chaperones increase the efficiency of folding by preventing aggregation and giving the polypeptide multiple attempts. A protein that folds correctly without a chaperone has exactly the same structure as one that required chaperone assistance. Chaperones are catalysts of folding efficiency, not determinants of folding outcome.

Constitutive vs. stress-induced expression

Students often assume chaperones are only present under stress. In reality, many chaperones are constitutively expressed and essential for normal growth. E. coli cells with GroEL deleted cannot survive even at optimal temperatures. Eukaryotic cells express Hsp70, Hsp90, and TRiC at high levels under normal conditions. Heat shock increases expression, but the baseline is substantial. The distinction matters: chaperones are not emergency responders; they are integral components of the protein biogenesis machinery.

ATP requirement is not universal

Not all chaperones require ATP. Small heat shock proteins function without ATP. Some chaperones in the ER and mitochondria use ATP, but others use different energy sources or none at all. The ATP requirement is a property of specific families, not a defining feature of chaperones. Students should also note that ATP hydrolysis powers conformational changes in the chaperone, not the folding of the substrate. The folding reaction itself is spontaneous; the chaperone merely creates conditions that make it more likely.

Chaperones are not enzymes in the classical sense

Chaperones are often called "folding catalysts," but they differ from enzymes in an important way: they do not lower the activation energy of the folding reaction. They do not stabilize the transition state. Instead, they prevent off-pathway reactions (aggregation) and, in some cases, actively unfold misfolded states. The distinction is subtle but important. Protein disulfide isomerase and peptidyl-prolyl isomerase are true folding enzymes because they catalyze specific covalent reactions. Chaperones are not.

Frequently Asked Questions

What is a chaperone protein?

A chaperone protein is a protein that assists other proteins in folding, assembly, transport, or degradation without being part of the final functional structure. Chaperones bind to non-native proteins, stabilize them, and facilitate their progression to the native state. They are found in all organisms and in all cellular compartments where proteins fold.

What is the purpose of chaperone proteins?

The primary purpose is to prevent protein misfolding and aggregation. Chaperones bind to exposed hydrophobic surfaces on non-native proteins, shielding them from inappropriate interactions. They also provide an isolated environment for folding (chaperonins), promote unfolding of misfolded states (Hsp70), and deliver clients to degradation systems when folding fails. Chaperones are essential for co-translational folding, protein translocation across membranes, and the assembly of multi-subunit complexes.

How do chaperone proteins work?

Chaperones work through regulated binding and release cycles. Most use ATP hydrolysis to drive conformational changes that alternate between high-affinity and low-affinity substrate-binding states. Hsp70 binds extended hydrophobic stretches, Hsp90 binds near-native states of specific clients, and chaperonins enclose substrates in a cage. Small heat shock proteins bind denatured proteins without ATP and hold them for other chaperones. The common theme is shielding hydrophobic surfaces and giving the polypeptide multiple opportunities to fold.

What are examples of chaperone proteins?

Major examples include Hsp70 (DnaK in bacteria, BiP in the ER), Hsp90, the chaperonins GroEL/GroES (bacteria) and TRiC/CCT (eukaryotes), and small heat shock proteins such as Hsp27 and αB-crystallin. Co-chaperones such as Hsp40 (J-proteins), GrpE, HOP, and CHIP regulate chaperone activity. Each family has distinct structures, substrate specificities, and mechanisms.

Are chaperone proteins enzymes?

Not in the classical sense. Enzymes lower the activation energy of a reaction and are unchanged by it. Chaperones do not lower the activation energy of folding; they prevent off-pathway reactions and, in some cases, actively unfold misfolded states. They are often called "folding catalysts" but the mechanism is fundamentally different from enzymatic catalysis. Some chaperones do have ATPase activity, but this powers their own conformational changes, not the folding reaction.

Do chaperone proteins determine the final structure of a protein?

No. The final three-dimensional structure is determined entirely by the amino acid sequence. Chaperones increase the efficiency and fidelity of folding by preventing aggregation and giving the polypeptide multiple attempts to reach the native state. A protein folded with chaperone assistance has the same structure as one folded spontaneously. Chaperones do not contribute steric information to the final fold.

Are chaperone proteins only produced under stress?

No. Many chaperones are constitutively expressed and essential for normal growth. GroEL, Hsp70, Hsp90, and TRiC are abundant in unstressed cells. Heat shock and other stresses increase their expression, but the baseline is substantial. The heat shock response is an amplification of an existing system, not the activation of a dormant one.

What happens if chaperone proteins fail?

Chaperone failure leads to protein misfolding and aggregation. In the short term, misfolded proteins are degraded by the ubiquitin-proteasome system. If the capacity of both chaperones and degradation systems is exceeded, aggregates form. Chronic aggregation is associated with neurodegenerative diseases such as Alzheimer's, Parkinson's, and Huntington's diseases. Chaperone dysfunction also contributes to aging and to the pathology of many other diseases.

Key Takeaways

• Chaperone proteins assist protein folding by binding non-native proteins and preventing aggregation, without becoming part of the final structure.
• The protein folding problem arises from the crowded cellular environment and the risk of off-pathway aggregation, not from the intrinsic difficulty of folding.
• Chaperones use ATP-driven binding and release cycles to shield hydrophobic surfaces and give substrates multiple folding attempts; chaperonins provide an isolated Anfinsen cage.
• Major chaperone families include Hsp70, Hsp90, chaperonins (GroEL/TRiC), and small heat shock proteins, each with distinct mechanisms and substrate specificities.
• Chaperones are integrated into protein quality control networks that decide between refolding and degradation via the ubiquitin-proteasome system.
• Chaperone dysfunction underlies protein aggregation diseases, and chaperones are therapeutic targets in both cancer and neurodegeneration.
• Chaperones do not determine the final fold, are not always ATP-dependent, and are constitutively expressed—not merely stress-induced.

Further Reading

• Stricher F et al. HSPA8/HSC70 chaperone protein: structure, function, and chemical targeting. Autophagy. 2013. PubMed 24121476
• Bellani V et al. CALR-mutated myeloproliferative neoplasms. Leukemia & lymphoma. 2025. PubMed 39960832
• Jones SE, Jomary C. Clusterin. The international journal of biochemistry & cell biology. 2002. PubMed 1190681500155-8)
• Falini B. NPM1-mutated acute myeloid leukemia: New pathogenetic and therapeutic insights and open questions. American journal of hematology. 2023. PubMed 37317978
• Birbo B et al. Role of HSP90 in Cancer. International journal of molecular sciences. 2021. PubMed 34638658
• Li K, Nowak RA. The role of basigin in reproduction. Reproduction (Cambridge, England). 2020. PubMed 31600731

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