HSP90AA1 | ENSG00000080824 | NCBI 3320

Details for: HSP90AA1

Gene ID: 3320

Symbol: HSP90AA1

Ensembl ID: ENSG00000080824

Description: heat shock protein 90 alpha family class A member 1

Associated with

Aggrephagy
(R-HSA-9646399)
Anchoring of the basal body to the plasma membrane
(R-HSA-5620912)
Attenuation phase
(R-HSA-3371568)
Aurka activation by tpx2
(R-HSA-8854518)
Autophagy
(R-HSA-9612973)
Axon guidance
(R-HSA-422475)
Bacterial infection pathways
(R-HSA-9824439)
Binding and uptake of ligands by scavenger receptors
(R-HSA-2173782)
Cell cycle
(R-HSA-1640170)
Cell cycle, mitotic
(R-HSA-69278)
Cellular responses to stimuli
(R-HSA-8953897)
Cellular responses to stress
(R-HSA-2262752)
Cellular response to heat stress
(R-HSA-3371556)
Centrosome maturation
(R-HSA-380287)
Chaperone mediated autophagy
(R-HSA-9613829)
Cilium assembly
(R-HSA-5617833)
Constitutive signaling by egfrviii
(R-HSA-5637810)
Constitutive signaling by ligand-responsive egfr cancer variants
(R-HSA-1236382)
Constitutive signaling by overexpressed erbb2
(R-HSA-9634285)
Cytokine signaling in immune system
(R-HSA-1280215)
Ddx58/ifih1-mediated induction of interferon-alpha/beta
(R-HSA-168928)
Developmental biology
(R-HSA-1266738)
Disease
(R-HSA-1643685)
Diseases of signal transduction by growth factor receptors and second messengers
(R-HSA-5663202)
Downregulation of erbb2 signaling
(R-HSA-8863795)
Drug-mediated inhibition of erbb2 signaling
(R-HSA-9652282)
Drug resistance in erbb2 kd mutants
(R-HSA-9665230)
Drug resistance in erbb2 tmd/jmd mutants
(R-HSA-9665737)
Enos activation
(R-HSA-203615)
Esr-mediated signaling
(R-HSA-8939211)
Estrogen-dependent gene expression
(R-HSA-9018519)
Extra-nuclear estrogen signaling
(R-HSA-9009391)
Fcgamma receptor (fcgr) dependent phagocytosis
(R-HSA-2029480)
G2/m transition
(R-HSA-69275)
Gene expression (transcription)
(R-HSA-74160)
Gene silencing by rna
(R-HSA-211000)
Hsf1 activation
(R-HSA-3371511)
Hsf1-dependent transactivation
(R-HSA-3371571)
Hsp90 chaperone cycle for steroid hormone receptors (shr) in the presence of ligand
(R-HSA-3371497)
Immune system
(R-HSA-168256)
Infectious disease
(R-HSA-5663205)
Influenza infection
(R-HSA-168255)
Influenza viral rna transcription and replication
(R-HSA-168273)
Innate immune system
(R-HSA-168249)
Interleukin-4 and interleukin-13 signaling
(R-HSA-6785807)
Macroautophagy
(R-HSA-1632852)
Metabolism
(R-HSA-1430728)
Metabolism of cofactors
(R-HSA-8978934)
Metabolism of nitric oxide: nos3 activation and regulation
(R-HSA-202131)
Metabolism of vitamins and cofactors
(R-HSA-196854)
Mitotic g2-g2/m phases
(R-HSA-453274)
Mitotic prometaphase
(R-HSA-68877)
M phase
(R-HSA-68886)
Nervous system development
(R-HSA-9675108)
Neutrophil degranulation
(R-HSA-6798695)
Organelle biogenesis and maintenance
(R-HSA-1852241)
Piwi-interacting rna (pirna) biogenesis
(R-HSA-5601884)
Programmed cell death
(R-HSA-5357801)
Recruitment of numa to mitotic centrosomes
(R-HSA-380320)
Regulated necrosis
(R-HSA-5218859)
Regulation of actin dynamics for phagocytic cup formation
(R-HSA-2029482)
Regulation of necroptotic cell death
(R-HSA-5675482)
Regulation of plk1 activity at g2/m transition
(R-HSA-2565942)
Resistance of erbb2 kd mutants to afatinib
(R-HSA-9665249)
Resistance of erbb2 kd mutants to neratinib
(R-HSA-9665246)
Resistance of erbb2 kd mutants to osimertinib
(R-HSA-9665247)
Resistance of erbb2 kd mutants to sapitinib
(R-HSA-9665244)
Resistance of erbb2 kd mutants to tesevatinib
(R-HSA-9665245)
Resistance of erbb2 kd mutants to trastuzumab
(R-HSA-9665233)
Respiratory syncytial virus infection pathway
(R-HSA-9820952)
Rho gtpase cycle
(R-HSA-9012999)
Ripk1-mediated regulated necrosis
(R-HSA-5213460)
Sars-cov infections
(R-HSA-9679506)
Scavenging by class f receptors
(R-HSA-3000484)
Selective autophagy
(R-HSA-9663891)
Sema3a pak dependent axon repulsion
(R-HSA-399954)
Semaphorin interactions
(R-HSA-373755)
Signaling by egfr in cancer
(R-HSA-1643713)
Signaling by egfrviii in cancer
(R-HSA-5637812)
Signaling by erbb2
(R-HSA-1227986)
Signaling by erbb2 ecd mutants
(R-HSA-9665348)
Signaling by erbb2 in cancer
(R-HSA-1227990)
Signaling by erbb2 kd mutants
(R-HSA-9664565)
Signaling by erbb2 tmd/jmd mutants
(R-HSA-9665686)
Signaling by interleukins
(R-HSA-449147)
Signaling by ligand-responsive egfr variants in cancer
(R-HSA-5637815)
Signaling by nuclear receptors
(R-HSA-9006931)
Signaling by receptor tyrosine kinases
(R-HSA-9006934)
Signaling by rho gtpases
(R-HSA-194315)
Signaling by rho gtpases, miro gtpases and rhobtb3
(R-HSA-9716542)
Signaling by vegf
(R-HSA-194138)
Signal transduction
(R-HSA-162582)
Tetrahydrobiopterin (bh4) synthesis, recycling, salvage and regulation
(R-HSA-1474151)
The role of gtse1 in g2/m progression after g2 checkpoint
(R-HSA-8852276)
Uptake and actions of bacterial toxins
(R-HSA-5339562)
Uptake and function of diphtheria toxin
(R-HSA-5336415)
Vegfa-vegfr2 pathway
(R-HSA-4420097)
Vegfr2 mediated vascular permeability
(R-HSA-5218920)
Vesicle-mediated transport
(R-HSA-5653656)
Viral infection pathways
(R-HSA-9824446)

Cells (max top 100)

(Cell Significance Index and respective Thresholds are uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

Cell Name: polychromatophilic erythroblast (CL0000550)
Fold Change: 1520.0081
Cell Significance Index: -236.4300
Cell Name: hematopoietic oligopotent progenitor cell (CL0002032)
Fold Change: 977.8296
Cell Significance Index: -248.0200
Cell Name: embryonic stem cell (CL0002322)
Fold Change: 705.4295
Cell Significance Index: -290.6000
Cell Name: smooth muscle fiber of ileum (CL1000278)
Fold Change: 616.4288
Cell Significance Index: -291.0300
Cell Name: peripheral blood mononuclear cell (CL2000001)
Fold Change: 538.6819
Cell Significance Index: -277.0900
Cell Name: ileal goblet cell (CL1000326)
Fold Change: 435.0527
Cell Significance Index: -291.9300
Cell Name: orthochromatic erythroblast (CL0000552)
Fold Change: 228.6213
Cell Significance Index: -281.8800
Cell Name: CD8-alpha-beta-positive, alpha-beta intraepithelial T cell (CL0000796)
Fold Change: 82.4362
Cell Significance Index: -220.8400
Cell Name: CD8-positive, alpha-beta regulatory T cell (CL0000795)
Fold Change: 78.8779
Cell Significance Index: -242.2700
Cell Name: stromal cell of bone marrow (CL0010001)
Fold Change: 74.6798
Cell Significance Index: -294.6900
Cell Name: epidermal Langerhans cell (CL0002457)
Fold Change: 41.0402
Cell Significance Index: -89.8200
Cell Name: thyroid follicular cell (CL0002258)
Fold Change: 17.1927
Cell Significance Index: 182.6700
Cell Name: glycinergic neuron (CL1001509)
Fold Change: 10.0132
Cell Significance Index: 525.7300
Cell Name: fibroblast of mammary gland (CL0002555)
Fold Change: 9.8299
Cell Significance Index: 281.7800
Cell Name: odontoblast (CL0000060)
Fold Change: 8.9261
Cell Significance Index: 1144.2800
Cell Name: cone retinal bipolar cell (CL0000752)
Fold Change: 8.6094
Cell Significance Index: 66.3600
Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
Fold Change: 8.5378
Cell Significance Index: 401.2700
Cell Name: mesonephric nephron tubule epithelial cell (CL1000022)
Fold Change: 7.3054
Cell Significance Index: 253.8600
Cell Name: intermediate cell of urothelium (CL4030055)
Fold Change: 6.2367
Cell Significance Index: 1124.2800
Cell Name: basal cell of urothelium (CL1000486)
Fold Change: 6.0719
Cell Significance Index: 746.5900
Cell Name: stromal cell of ovary (CL0002132)
Fold Change: 5.7229
Cell Significance Index: 785.9200
Cell Name: cell in vitro (CL0001034)
Fold Change: 5.4136
Cell Significance Index: 2956.5000
Cell Name: granulosa cell (CL0000501)
Fold Change: 4.9238
Cell Significance Index: 129.4700
Cell Name: hair follicular keratinocyte (CL2000092)
Fold Change: 4.3923
Cell Significance Index: 1941.9400
Cell Name: early pro-B cell (CL0002046)
Fold Change: 4.3593
Cell Significance Index: 281.2400
Cell Name: acinar cell of salivary gland (CL0002623)
Fold Change: 4.3228
Cell Significance Index: 201.5500
Cell Name: tonsil germinal center B cell (CL2000006)
Fold Change: 4.2424
Cell Significance Index: 500.3100
Cell Name: basal cell of prostate epithelium (CL0002341)
Fold Change: 3.7323
Cell Significance Index: 101.5900
Cell Name: lactocyte (CL0002325)
Fold Change: 3.6887
Cell Significance Index: 476.5600
Cell Name: placental villous trophoblast (CL2000060)
Fold Change: 3.5934
Cell Significance Index: 95.9500
Cell Name: neoplastic cell (CL0001063)
Fold Change: 3.5530
Cell Significance Index: 705.1000
Cell Name: peg cell (CL4033014)
Fold Change: 3.5384
Cell Significance Index: 81.7500
Cell Name: sebum secreting cell (CL0000317)
Fold Change: 2.8259
Cell Significance Index: 199.8600
Cell Name: umbrella cell of urothelium (CL4030056)
Fold Change: 2.6323
Cell Significance Index: 24.2400
Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
Fold Change: 2.3960
Cell Significance Index: 178.5700
Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
Fold Change: 2.1404
Cell Significance Index: 429.3700
Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
Fold Change: 1.9809
Cell Significance Index: 710.5200
Cell Name: enterocyte of epithelium of small intestine (CL1000334)
Fold Change: 1.7913
Cell Significance Index: 51.6100
Cell Name: retinal progenitor cell (CL0002672)
Fold Change: 1.7525
Cell Significance Index: 98.3400
Cell Name: pancreatic acinar cell (CL0002064)
Fold Change: 1.5332
Cell Significance Index: 261.8100
Cell Name: colon goblet cell (CL0009039)
Fold Change: 0.7566
Cell Significance Index: 74.8400
Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
Fold Change: 0.7565
Cell Significance Index: 554.6600
Cell Name: pulmonary alveolar epithelial cell (CL0000322)
Fold Change: 0.5060
Cell Significance Index: 383.0200
Cell Name: small intestine goblet cell (CL1000495)
Fold Change: 0.2169
Cell Significance Index: 7.6200
Cell Name: epithelial cell of small intestine (CL0002254)
Fold Change: 0.1781
Cell Significance Index: 28.9600
Cell Name: pigmented epithelial cell (CL0000529)
Fold Change: 0.0960
Cell Significance Index: 180.6800
Cell Name: secondary lens fiber (CL0002225)
Fold Change: -0.0747
Cell Significance Index: -101.6100
Cell Name: abnormal cell (CL0001061)
Fold Change: -0.1126
Cell Significance Index: -11.5000
Cell Name: anterior lens cell (CL0002223)
Fold Change: -0.1315
Cell Significance Index: -242.5400
Cell Name: fibroblast of dermis (CL0002551)
Fold Change: -0.1319
Cell Significance Index: -2.7600
Cell Name: lens epithelial cell (CL0002224)
Fold Change: -0.1446
Cell Significance Index: -222.5400
Cell Name: pancreatic A cell (CL0000171)
Fold Change: -0.1503
Cell Significance Index: -111.3600
Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
Fold Change: -0.1895
Cell Significance Index: -120.3500
Cell Name: pancreatic PP cell (CL0002275)
Fold Change: -0.2713
Cell Significance Index: -169.4300
Cell Name: eye photoreceptor cell (CL0000287)
Fold Change: -0.3019
Cell Significance Index: -19.0300
Cell Name: bladder urothelial cell (CL1001428)
Fold Change: -0.3338
Cell Significance Index: -17.3400
Cell Name: type B pancreatic cell (CL0000169)
Fold Change: -0.3902
Cell Significance Index: -220.0400
Cell Name: forebrain neuroblast (CL1000042)
Fold Change: -0.3908
Cell Significance Index: -24.0200
Cell Name: GABAergic interneuron (CL0011005)
Fold Change: -0.4021
Cell Significance Index: -278.1300
Cell Name: ciliary muscle cell (CL1000443)
Fold Change: -0.4256
Cell Significance Index: -193.1600
Cell Name: enteroendocrine cell of colon (CL0009042)
Fold Change: -0.4619
Cell Significance Index: -87.9100
Cell Name: pancreatic endocrine cell (CL0008024)
Fold Change: -0.4905
Cell Significance Index: -56.0000
Cell Name: pancreatic D cell (CL0000173)
Fold Change: -0.6882
Cell Significance Index: -144.9600
Cell Name: CD4-positive, alpha-beta memory T cell, CD45RO-positive (CL0001204)
Fold Change: -0.6919
Cell Significance Index: -20.3200
Cell Name: mesenchymal cell (CL0008019)
Fold Change: -0.7338
Cell Significance Index: -12.2800
Cell Name: dopaminergic neuron (CL0000700)
Fold Change: -0.8933
Cell Significance Index: -257.0300
Cell Name: vascular lymphangioblast (CL0005022)
Fold Change: -0.9747
Cell Significance Index: -17.2300
Cell Name: intestinal crypt stem cell of colon (CL0009043)
Fold Change: -1.0339
Cell Significance Index: -112.4600
Cell Name: pigmented ciliary epithelial cell (CL0002303)
Fold Change: -1.4373
Cell Significance Index: -208.9400
Cell Name: pancreatic ductal cell (CL0002079)
Fold Change: -1.4626
Cell Significance Index: -167.5700
Cell Name: epithelial cell of stomach (CL0002178)
Fold Change: -1.6335
Cell Significance Index: -190.3700
Cell Name: kidney loop of Henle descending limb epithelial cell (CL1001021)
Fold Change: -1.6431
Cell Significance Index: -130.1300
Cell Name: kidney cell (CL1000497)
Fold Change: -1.7040
Cell Significance Index: -13.6100
Cell Name: hippocampal granule cell (CL0001033)
Fold Change: -1.7736
Cell Significance Index: -119.2600
Cell Name: retinal rod cell (CL0000604)
Fold Change: -2.0112
Cell Significance Index: -23.9800
Cell Name: CD14-positive, CD16-negative classical monocyte (CL0002057)
Fold Change: -2.1214
Cell Significance Index: -39.2100
Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
Fold Change: -2.3323
Cell Significance Index: -65.1800
Cell Name: pro-T cell (CL0000827)
Fold Change: -2.4856
Cell Significance Index: -63.5000
Cell Name: cardiac muscle myoblast (CL0000513)
Fold Change: -2.7223
Cell Significance Index: -208.9100
Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
Fold Change: -2.7550
Cell Significance Index: -286.8600
Cell Name: enterocyte of epithelium of large intestine (CL0002071)
Fold Change: -3.0679
Cell Significance Index: -139.0600
Cell Name: cerebellar granule cell (CL0001031)
Fold Change: -3.1300
Cell Significance Index: -53.6400
Cell Name: paneth cell of epithelium of small intestine (CL1000343)
Fold Change: -3.3344
Cell Significance Index: -72.2400
Cell Name: microfold cell of epithelium of small intestine (CL1000353)
Fold Change: -3.4744
Cell Significance Index: -240.2700
Cell Name: gut absorptive cell (CL0000677)
Fold Change: -3.5718
Cell Significance Index: -214.4300
Cell Name: indirect pathway medium spiny neuron (CL4023029)
Fold Change: -3.6081
Cell Significance Index: -159.6000
Cell Name: interstitial cell of ovary (CL0002094)
Fold Change: -3.6758
Cell Significance Index: -47.0800
Cell Name: conjunctival epithelial cell (CL1000432)
Fold Change: -3.8714
Cell Significance Index: -52.8200
Cell Name: oral mucosa squamous cell (CL1001576)
Fold Change: -3.9160
Cell Significance Index: -33.6500
Cell Name: direct pathway medium spiny neuron (CL4023026)
Fold Change: -4.6201
Cell Significance Index: -174.9500
Cell Name: intestinal tuft cell (CL0019032)
Fold Change: -4.7154
Cell Significance Index: -289.1000
Cell Name: skeletal muscle myoblast (CL0000515)
Fold Change: -4.8237
Cell Significance Index: -52.4400
Cell Name: neutrophil progenitor cell (CL0000834)
Fold Change: -4.8949
Cell Significance Index: -130.9400
Cell Name: hippocampal pyramidal neuron (CL1001571)
Fold Change: -4.9101
Cell Significance Index: -140.1200
Cell Name: transit amplifying cell of colon (CL0009011)
Fold Change: -5.2497
Cell Significance Index: -168.1400
Cell Name: endothelial cell of venule (CL1000414)
Fold Change: -5.4531
Cell Significance Index: -61.9500
Cell Name: kidney epithelial cell (CL0002518)
Fold Change: -5.5540
Cell Significance Index: -163.5900
Cell Name: enteroendocrine cell of small intestine (CL0009006)
Fold Change: -5.6754
Cell Significance Index: -141.8700
Cell Name: stratified epithelial cell (CL0000079)
Fold Change: -6.4845
Cell Significance Index: -238.0400
Cell Name: L6b glutamatergic cortical neuron (CL4023038)
Fold Change: -6.8630
Cell Significance Index: -224.7000

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

**Key Characteristics** HSP90AA1 is a 90-kDa protein that is constitutively expressed in most cell types. It is a member of the HSP90 family, which is characterized by its ability to bind to and stabilize the folding of client proteins. HSP90AA1 has been shown to interact with a wide range of client proteins, including kinases, phosphatases, and other chaperones. It is also known to be involved in various signaling pathways, including the EGFR and ER signaling pathways. **Pathways and Functions** HSP90AA1 is involved in a wide range of cellular processes, including: * Cell cycle regulation: HSP90AA1 is involved in the regulation of the cell cycle, particularly at the G2/M phase. * Apoptosis: HSP90AA1 has been shown to inhibit apoptosis by stabilizing the folding of pro-apoptotic proteins. * Immune response: HSP90AA1 is involved in the regulation of immune responses, particularly in the activation of natural killer cells. * Signaling pathways: HSP90AA1 is involved in the signaling pathways of various growth factor receptors, including the EGFR and ER. * Protein folding: HSP90AA1 is involved in the folding of client proteins, particularly those that are prone to misfolding or aggregation. **Clinical Significance** HSP90AA1 has been implicated in various diseases, including: * Cancer: HSP90AA1 is overexpressed in many types of cancer, including breast, lung, and colon cancer. Its dysregulation has been shown to contribute to cancer progression and resistance to therapy. * Neurodegenerative diseases: HSP90AA1 has been implicated in the pathogenesis of neurodegenerative diseases, including Alzheimer's disease and Parkinson's disease. * Inflammatory diseases: HSP90AA1 has been shown to contribute to the development of inflammatory diseases, including rheumatoid arthritis and multiple sclerosis. * Infectious diseases: HSP90AA1 has been implicated in the pathogenesis of infectious diseases, including HIV and tuberculosis. In conclusion, HSP90AA1 is a multifunctional protein that plays a crucial role in various cellular processes, including cell cycle regulation, apoptosis, and immune response. Its dysregulation has been implicated in various diseases, including cancer, neurodegenerative diseases, inflammatory diseases, and infectious diseases. Further research is needed to fully understand the mechanisms by which HSP90AA1 contributes to disease and to develop therapeutic strategies to target its dysregulation.

Disclaimer: This summary is generated by an AI language model and may contain inaccuracies or hallucinations. However, it is cross-referenced with curated gene expression data from major biological sources. Please verify the information before use.

Heat shock 86 kDa
Q86SX1_HUMAN

Genular Protein ID: 2723957671

Symbol: HS90A_HUMAN

Name: Heat shock 86 kDa

UniProtKB Accession Codes:

P07900 A8K500 B3KPJ9 Q2PP14 Q5CAQ6 Q5CAQ7 Q9BVQ5

Database IDs:

Citations:

PubMed ID: 2780322

Title: Nucleotide sequence of a full-length cDNA for 90 kDa heat-shock protein from human peripheral blood lymphocytes.

PubMed ID: 2780322

DOI: 10.1093/nar/17.17.7108

PubMed ID: 1368637

Title: Molecular cloning of cDNA encoding a human heat-shock protein whose expression is induced by adenovirus type 12 E1A in HeLa cells.

PubMed ID: 1368637

DOI: 10.1271/bbb1961.54.3163

PubMed ID: 2527334

Title: Sequence and regulation of a gene encoding a human 89-kilodalton heat shock protein.

PubMed ID: 2527334

DOI: 10.1128/mcb.9.6.2615-2626.1989

PubMed ID: 16269234

Title: The HSP90 family of genes in the human genome: insights into their divergence and evolution.

PubMed ID: 16269234

DOI: 10.1016/j.ygeno.2005.08.012

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 12508121

Title: The DNA sequence and analysis of human chromosome 14.

PubMed ID: 12508121

DOI: 10.1038/nature01348

PubMed ID: 2469626

Title: Heat-shock proteins, Hsp84 and Hsp86, of mice and men: two related genes encode formerly identified tumour-specific transplantation antigens.

PubMed ID: 2469626

DOI: 10.1016/0378-1119(88)90182-5

PubMed ID: 2591742

Title: Cloning and analysis of a human 86-kDa heat-shock-protein-encoding gene.

PubMed ID: 2591742

DOI: 10.1016/0378-1119(89)90408-3

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 2492519

Title: Two human 90-kDa heat shock proteins are phosphorylated in vivo at conserved serines that are phosphorylated in vitro by casein kinase II.

PubMed ID: 2492519

DOI: 10.1016/s0021-9258(19)81631-9

PubMed ID: 10409742

Title: Kinase suppressor of Ras forms a multiprotein signaling complex and modulates MEK localization.

PubMed ID: 10409742

DOI: 10.1128/mcb.19.8.5523

PubMed ID: 15937123

Title: S-nitrosylation of Hsp90 promotes the inhibition of its ATPase and endothelial nitric oxide synthase regulatory activities.

PubMed ID: 15937123

DOI: 10.1073/pnas.0407294102

PubMed ID: 2507541

Title: The human double-stranded DNA-activated protein kinase phosphorylates the 90-kDa heat-shock protein, hsp90 alpha at two NH2-terminal threonine residues.

PubMed ID: 2507541

DOI: 10.1016/s0021-9258(18)71488-9

PubMed ID: 8289821

Title: The carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivo.

PubMed ID: 8289821

DOI: 10.1128/mcb.14.2.1459-1464.1994

PubMed ID: 7588731

Title: Mechanism of dimer formation of the 90-kDa heat-shock protein.

PubMed ID: 7588731

DOI: 10.1111/j.1432-1033.1995.001_1.x

PubMed ID: 9195923

Title: Protein phosphatase 5 is a major component of glucocorticoid receptor.hsp90 complexes with properties of an FK506-binding immunophilin.

PubMed ID: 9195923

DOI: 10.1074/jbc.272.26.16224

PubMed ID: 9660753

Title: Specific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of hsp90.

PubMed ID: 9660753

DOI: 10.1074/jbc.273.29.18007

PubMed ID: 10508479

Title: Antigens recognized by autologous antibody in patients with renal-cell carcinoma.

PubMed ID: 10508479

DOI: 10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5

PubMed ID: 11274138

Title: Stable association of hsp90 and p23, but Not hsp70, with active human telomerase.

PubMed ID: 11274138

DOI: 10.1074/jbc.c100055200

PubMed ID: 11583998

Title: Evidence for a mechanism of repression of heat shock factor 1 transcriptional activity by a multichaperone complex.

PubMed ID: 11583998

DOI: 10.1074/jbc.m105931200

PubMed ID: 11276205

Title: A CD14-independent LPS receptor cluster.

PubMed ID: 11276205

DOI: 10.1038/86342

PubMed ID: 12526792

Title: Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70.

PubMed ID: 12526792

DOI: 10.1016/s0092-8674(02)01250-3

PubMed ID: 12853476

Title: Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system.

PubMed ID: 12853476

DOI: 10.1093/emboj/cdg362

PubMed ID: 12604615

Title: Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone.

PubMed ID: 12604615

DOI: 10.1074/jbc.m212761200

PubMed ID: 14654843

Title: Proteomic characterization of the human centrosome by protein correlation profiling.

PubMed ID: 14654843

DOI: 10.1038/nature02166

PubMed ID: 15235609

Title: SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells.

PubMed ID: 15235609

DOI: 10.1038/ncb1151

PubMed ID: 15708368

Title: Small glutamine-rich tetratricopeptide repeat-containing protein is composed of three structural units with distinct functions.

PubMed ID: 15708368

DOI: 10.1016/j.abb.2004.12.020

PubMed ID: 15383005

Title: Human protein phosphatase 5 dissociates from heat-shock proteins and is proteolytically activated in response to arachidonic acid and the microtubule-depolymerizing drug nocodazole.

PubMed ID: 15383005

DOI: 10.1042/bj20040690

PubMed ID: 15577939

Title: Molecular basis for TPR domain-mediated regulation of protein phosphatase 5.

PubMed ID: 15577939

DOI: 10.1038/sj.emboj.7600496

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 16807684

Title: Phosphoproteomic analysis of the human pituitary.

PubMed ID: 16807684

DOI: 10.1007/s11102-006-8916-x

PubMed ID: 16531226

Title: Conformational diversity in the TPR domain-mediated interaction of protein phosphatase 5 with Hsp90.

PubMed ID: 16531226

DOI: 10.1016/j.str.2005.12.009

PubMed ID: 17947705

Title: Heat shock protein 90 associates with monarch-1 and regulates its ability to promote degradation of NF-kappaB-inducing kinase.

PubMed ID: 17947705

DOI: 10.4049/jimmunol.179.9.6291

PubMed ID: 18400751

Title: Conserved conformational changes in the ATPase cycle of human Hsp90.

PubMed ID: 18400751

DOI: 10.1074/jbc.m800540200

PubMed ID: 19367720

Title: Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment.

PubMed ID: 19367720

DOI: 10.1021/pr800500r

PubMed ID: 18088087

Title: Phosphoproteome of resting human platelets.

PubMed ID: 18088087

DOI: 10.1021/pr0704130

PubMed ID: 18691976

Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.

PubMed ID: 18691976

DOI: 10.1016/j.molcel.2008.07.007

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 18318008

Title: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography.

PubMed ID: 18318008

DOI: 10.1002/pmic.200700884

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 19875381

Title: A proteomic investigation of ligand-dependent HSP90 complexes reveals CHORDC1 as a novel ADP-dependent HSP90-interacting protein.

PubMed ID: 19875381

DOI: 10.1074/mcp.m900261-mcp200

PubMed ID: 16139798

Title: Proteomic identification of proteins conjugated to ISG15 in mouse and human cells.

PubMed ID: 16139798

DOI: 10.1016/j.bbrc.2005.08.132

PubMed ID: 17081065

Title: Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes.

PubMed ID: 17081065

DOI: 10.1021/pr060363j

PubMed ID: 17028174

Title: Folliculin encoded by the BHD gene interacts with a binding protein, FNIP1, and AMPK, and is involved in AMPK and mTOR signaling.

PubMed ID: 17028174

DOI: 10.1073/pnas.0603781103

PubMed ID: 18256191

Title: The ATPase-dependent chaperoning activity of Hsp90a regulates thick filament formation and integration during skeletal muscle myofibrillogenesis.

PubMed ID: 18256191

DOI: 10.1242/dev.018150

PubMed ID: 19696785

Title: Hsp90 is regulated by a switch point in the C-terminal domain.

PubMed ID: 19696785

DOI: 10.1038/embor.2009.153

PubMed ID: 20628368

Title: Tom70 mediates activation of interferon regulatory factor 3 on mitochondria.

PubMed ID: 20628368

DOI: 10.1038/cr.2010.103

PubMed ID: 20353823

Title: Stat1 mediates an auto-regulation of hsp90beta gene in heat shock response.

PubMed ID: 20353823

DOI: 10.1016/j.cellsig.2010.03.012

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22066472

Title: Human heat shock protein (Hsp) 90 interferes with Neisseria meningitidis adhesin A (NadA)-mediated adhesion and invasion.

PubMed ID: 22066472

DOI: 10.1111/j.1462-5822.2011.01722.x

PubMed ID: 23569206

Title: Cdc37 (cell division cycle 37) restricts Hsp90 (heat shock protein 90) motility by interaction with N-terminal and middle domain binding sites.

PubMed ID: 23569206

DOI: 10.1074/jbc.m112.439257

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24613385

Title: Hsp70 and Hsp90 oppositely regulate TGF-beta signaling through CHIP/Stub1.

PubMed ID: 24613385

DOI: 10.1016/j.bbrc.2014.02.124

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 24681825

Title: The NLR-related protein NWD1 is associated with prostate cancer and modulates androgen receptor signaling.

PubMed ID: 24681825

DOI: 10.18632/oncotarget.1850

PubMed ID: 25973397

Title: Hsp90, the concertmaster: tuning transcription.

PubMed ID: 25973397

DOI: 10.3389/fonc.2015.00100

PubMed ID: 25609812

Title: Tom70 mediates Sendai virus-induced apoptosis on mitochondria.

PubMed ID: 25609812

DOI: 10.1128/jvi.02959-14

PubMed ID: 25738358

Title: C-terminal domain of SMYD3 serves as a unique HSP90-regulated motif in oncogenesis.

PubMed ID: 25738358

DOI: 10.18632/oncotarget.2970

PubMed ID: 26517842

Title: Client proteins and small molecule inhibitors display distinct binding preferences for constitutive and stress-induced HSP90 isoforms and their conformationally restricted mutants.

PubMed ID: 26517842

DOI: 10.1371/journal.pone.0141786

PubMed ID: 25944712

Title: N-terminome analysis of the human mitochondrial proteome.

PubMed ID: 25944712

DOI: 10.1002/pmic.201400617

PubMed ID: 27295069

Title: Hsp90: Friends, clients and natural foes.

PubMed ID: 27295069

DOI: 10.1016/j.biochi.2016.05.018

PubMed ID: 26991466

Title: Review: The HSP90 molecular chaperone-an enigmatic ATPase.

PubMed ID: 26991466

DOI: 10.1002/bip.22835

PubMed ID: 27353360

Title: The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding.

PubMed ID: 27353360

DOI: 10.1038/ncomms12037

PubMed ID: 26754925

Title: IER5 generates a novel hypo-phosphorylated active form of HSF1 and contributes to tumorigenesis.

PubMed ID: 26754925

DOI: 10.1038/srep19174

PubMed ID: 29127155

Title: Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facilitates folding of kinase and non-kinase clients.

PubMed ID: 29127155

DOI: 10.15252/embj.201796700

PubMed ID: 30559449

Title: Proteasomal degradation of NOD2 by NLRP12 in monocytes promotes bacterial tolerance and colonization by enteropathogens.

PubMed ID: 30559449

DOI: 10.1038/s41467-018-07750-5

PubMed ID: 29743370

Title: Herpes Simplex Virus 1 Inhibits TANK-Binding Kinase 1 through Formation of the Us11-Hsp90 Complex.

PubMed ID: 29743370

DOI: 10.1128/jvi.00402-18

PubMed ID: 9108479

Title: Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent.

PubMed ID: 9108479

DOI: 10.1016/s0092-8674(00)80203-2

PubMed ID: 9817749

Title: In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis.

PubMed ID: 9817749

DOI: 10.1083/jcb.143.4.901

PubMed ID: 16307917

Title: Chaperoned ubiquitylation -- crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex.

PubMed ID: 16307917

DOI: 10.1016/j.molcel.2005.09.023

Sequence Information:

Length: 732
Mass: 84660
Checksum: 969F65FCC0BC86FD
Sequence:

MPEETQTQDQ PMEEEEVETF AFQAEIAQLM SLIINTFYSN KEIFLRELIS NSSDALDKIR 
YESLTDPSKL DSGKELHINL IPNKQDRTLT IVDTGIGMTK ADLINNLGTI AKSGTKAFME 
ALQAGADISM IGQFGVGFYS AYLVAEKVTV ITKHNDDEQY AWESSAGGSF TVRTDTGEPM 
GRGTKVILHL KEDQTEYLEE RRIKEIVKKH SQFIGYPITL FVEKERDKEV SDDEAEEKED 
KEEEKEKEEK ESEDKPEIED VGSDEEEEKK DGDKKKKKKI KEKYIDQEEL NKTKPIWTRN 
PDDITNEEYG EFYKSLTNDW EDHLAVKHFS VEGQLEFRAL LFVPRRAPFD LFENRKKKNN 
IKLYVRRVFI MDNCEELIPE YLNFIRGVVD SEDLPLNISR EMLQQSKILK VIRKNLVKKC 
LELFTELAED KENYKKFYEQ FSKNIKLGIH EDSQNRKKLS ELLRYYTSAS GDEMVSLKDY 
CTRMKENQKH IYYITGETKD QVANSAFVER LRKHGLEVIY MIEPIDEYCV QQLKEFEGKT 
LVSVTKEGLE LPEDEEEKKK QEEKKTKFEN LCKIMKDILE KKVEKVVVSN RLVTSPCCIV 
TSTYGWTANM ERIMKAQALR DNSTMGYMAA KKHLEINPDH SIIETLRQKA EADKNDKSVK 
DLVILLYETA LLSSGFSLED PQTHANRIYR MIKLGLGIDE DDPTADDTSA AVTEEMPPLE 
GDDDTSRMEE VD

Genular Protein ID: 2236158157

Symbol: Q86SX1_HUMAN

Name: N/A

UniProtKB Accession Codes:

Q86SX1

Database IDs:

Sequence Information:

Length: 262
Mass: 29031
Checksum: 886BBF5DEE3BFF29
Sequence:

MPPCSGGDGS TPPGPSLRDR DCPAQSAEYP RDRLDPRPGS PSEASSPPFL RSRAPVNWYQ 
EKAQVFLWHL MVSGSTTLLC LWKQPFHVSA FPVTASLAFR QSQGAGQHLY KDLQPFILLR 
LLMPEETQTQ DQPMEEEEVE TFAFQAEIAQ LMSLIINTFY SNKEIFLREL ISNSSDALDK 
IRYESLTDPS KLDSGKELHI NLIPNKQDRT LTIVDTGIGM TKADLINNLG TIAKSGTKAF 
MEALQAGADI SMIGQFGVGF YS

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: HSP90AA1

Associated with

Cells (max top 100)

Other Information

Nucleotide sequence of a full-length cDNA for 90 kDa heat-shock protein from human peripheral blood lymphocytes. PubMed ID: 2780322

Molecular cloning of cDNA encoding a human heat-shock protein whose expression is induced by adenovirus type 12 E1A in HeLa cells. PubMed ID: 1368637

Sequence and regulation of a gene encoding a human 89-kilodalton heat shock protein. PubMed ID: 2527334

The HSP90 family of genes in the human genome: insights into their divergence and evolution. PubMed ID: 16269234

Complete sequencing and characterization of 21,243 full-length human cDNAs. PubMed ID: 14702039

The DNA sequence and analysis of human chromosome 14. PubMed ID: 12508121

Heat-shock proteins, Hsp84 and Hsp86, of mice and men: two related genes encode formerly identified tumour-specific transplantation antigens. PubMed ID: 2469626

Cloning and analysis of a human 86-kDa heat-shock-protein-encoding gene. PubMed ID: 2591742

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Two human 90-kDa heat shock proteins are phosphorylated in vivo at conserved serines that are phosphorylated in vitro by casein kinase II. PubMed ID: 2492519

Kinase suppressor of Ras forms a multiprotein signaling complex and modulates MEK localization. PubMed ID: 10409742

S-nitrosylation of Hsp90 promotes the inhibition of its ATPase and endothelial nitric oxide synthase regulatory activities. PubMed ID: 15937123

The human double-stranded DNA-activated protein kinase phosphorylates the 90-kDa heat-shock protein, hsp90 alpha at two NH2-terminal threonine residues. PubMed ID: 2507541

The carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivo. PubMed ID: 8289821

Mechanism of dimer formation of the 90-kDa heat-shock protein. PubMed ID: 7588731

Protein phosphatase 5 is a major component of glucocorticoid receptor.hsp90 complexes with properties of an FK506-binding immunophilin. PubMed ID: 9195923

Specific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of hsp90. PubMed ID: 9660753

Antigens recognized by autologous antibody in patients with renal-cell carcinoma. PubMed ID: 10508479

Stable association of hsp90 and p23, but Not hsp70, with active human telomerase. PubMed ID: 11274138

Evidence for a mechanism of repression of heat shock factor 1 transcriptional activity by a multichaperone complex. PubMed ID: 11583998

A CD14-independent LPS receptor cluster. PubMed ID: 11276205

Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70. PubMed ID: 12526792

Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system. PubMed ID: 12853476

Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone. PubMed ID: 12604615

Proteomic characterization of the human centrosome by protein correlation profiling. PubMed ID: 14654843

SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells. PubMed ID: 15235609

Small glutamine-rich tetratricopeptide repeat-containing protein is composed of three structural units with distinct functions. PubMed ID: 15708368

Human protein phosphatase 5 dissociates from heat-shock proteins and is proteolytically activated in response to arachidonic acid and the microtubule-depolymerizing drug nocodazole. PubMed ID: 15383005

Molecular basis for TPR domain-mediated regulation of protein phosphatase 5. PubMed ID: 15577939

Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. PubMed ID: 17081983

Phosphoproteomic analysis of the human pituitary. PubMed ID: 16807684

Conformational diversity in the TPR domain-mediated interaction of protein phosphatase 5 with Hsp90. PubMed ID: 16531226

Heat shock protein 90 associates with monarch-1 and regulates its ability to promote degradation of NF-kappaB-inducing kinase. PubMed ID: 17947705

Conserved conformational changes in the ATPase cycle of human Hsp90. PubMed ID: 18400751

Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment. PubMed ID: 19367720

Phosphoproteome of resting human platelets. PubMed ID: 18088087

Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. PubMed ID: 18691976

A quantitative atlas of mitotic phosphorylation. PubMed ID: 18669648

Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography. PubMed ID: 18318008

Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. PubMed ID: 19413330

Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. PubMed ID: 19690332

Lysine acetylation targets protein complexes and co-regulates major cellular functions. PubMed ID: 19608861

A proteomic investigation of ligand-dependent HSP90 complexes reveals CHORDC1 as a novel ADP-dependent HSP90-interacting protein. PubMed ID: 19875381

Proteomic identification of proteins conjugated to ISG15 in mouse and human cells. PubMed ID: 16139798

Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. PubMed ID: 17081065

Folliculin encoded by the BHD gene interacts with a binding protein, FNIP1, and AMPK, and is involved in AMPK and mTOR signaling. PubMed ID: 17028174

The ATPase-dependent chaperoning activity of Hsp90a regulates thick filament formation and integration during skeletal muscle myofibrillogenesis. PubMed ID: 18256191

Hsp90 is regulated by a switch point in the C-terminal domain. PubMed ID: 19696785

Tom70 mediates activation of interferon regulatory factor 3 on mitochondria. PubMed ID: 20628368

Stat1 mediates an auto-regulation of hsp90beta gene in heat shock response. PubMed ID: 20353823

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PubMed ID: 20068231

Initial characterization of the human central proteome. PubMed ID: 21269460

System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. PubMed ID: 21406692

Human heat shock protein (Hsp) 90 interferes with Neisseria meningitidis adhesin A (NadA)-mediated adhesion and invasion. PubMed ID: 22066472

Cdc37 (cell division cycle 37) restricts Hsp90 (heat shock protein 90) motility by interaction with N-terminal and middle domain binding sites. PubMed ID: 23569206

Toward a comprehensive characterization of a human cancer cell phosphoproteome. PubMed ID: 23186163

Hsp70 and Hsp90 oppositely regulate TGF-beta signaling through CHIP/Stub1. PubMed ID: 24613385

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

The NLR-related protein NWD1 is associated with prostate cancer and modulates androgen receptor signaling. PubMed ID: 24681825

Hsp90, the concertmaster: tuning transcription. PubMed ID: 25973397

Tom70 mediates Sendai virus-induced apoptosis on mitochondria. PubMed ID: 25609812

C-terminal domain of SMYD3 serves as a unique HSP90-regulated motif in oncogenesis. PubMed ID: 25738358

Client proteins and small molecule inhibitors display distinct binding preferences for constitutive and stress-induced HSP90 isoforms and their conformationally restricted mutants. PubMed ID: 26517842

N-terminome analysis of the human mitochondrial proteome. PubMed ID: 25944712

Hsp90: Friends, clients and natural foes. PubMed ID: 27295069

Review: The HSP90 molecular chaperone-an enigmatic ATPase. PubMed ID: 26991466

The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding. PubMed ID: 27353360

IER5 generates a novel hypo-phosphorylated active form of HSF1 and contributes to tumorigenesis. PubMed ID: 26754925

Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facilitates folding of kinase and non-kinase clients. PubMed ID: 29127155

Proteasomal degradation of NOD2 by NLRP12 in monocytes promotes bacterial tolerance and colonization by enteropathogens. PubMed ID: 30559449

Herpes Simplex Virus 1 Inhibits TANK-Binding Kinase 1 through Formation of the Us11-Hsp90 Complex. PubMed ID: 29743370

Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent. PubMed ID: 9108479

In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis. PubMed ID: 9817749

Chaperoned ubiquitylation -- crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex. PubMed ID: 16307917