763:
424:
31:
468:
It is thought that many Hsp70s crowd around an unfolded substrate, stabilizing it and preventing aggregation until the unfolded molecule folds properly, at which time the Hsp70s lose affinity for the molecule and diffuse away. Hsp70 also acts as a mitochondrial and chloroplastic molecular chaperone
682:
in 1987 to describe proteins that mediated the post-translational assembly of protein complexes. In 1988, it was realised that similar proteins mediated this process in both prokaryotes and eukaryotes. The details of this process were determined in 1989, when the ATP-dependent protein folding was
632:
rather than being incorporated themselves into the phage structure. These gps were gp26, gp31, gp38, gp51, gp28, and gp4 . The first four of these six gene products have since been recognized as being chaperone proteins. Additionally, gp40, gp57A, gp63 and gpwac have also now been identified as
101:
and functioning of chaperones. Bulk biochemical measurements have informed us on the protein folding efficiency, and prevention of aggregation when chaperones are present during protein folding. Recent advances in single-molecule analysis have brought insights into structural heterogeneity of
490:) may be the least understood chaperone. Its molecular weight is about 90 kDa, and it is necessary for viability in eukaryotes (possibly for prokaryotes as well). Heat shock protein 90 (Hsp90) is a molecular chaperone essential for activating many signaling proteins in the eukaryotic cell.
649:
protein gp23. Chaperone gp40 participates in the assembly of gp20, thus aiding in the formation of the connector complex that initiates head procapsid assembly. Gp4(50)(65), although not specifically listed as a chaperone, acts catalytically as a nuclease that appears to be essential for
368:; such names are commonly used for eukaryotes such as yeast. The bacterial names have more varied forms, and refer directly to their apparent function at discovery. For example, "GroEL" originally stands for "phage growth defect, overcome by mutation in phage gene E, large subunit".
2321:
Snustad DP. Dominance interactions in
Escherichia coli cells mixedly infected with bacteriophage T4D wild-type and amber mutants and their possible implications as to type of gene-product function: catalytic vs. stoichiometric. Virology. 1968;35(4):550-563.
661:
of gp34 and gp37, the major structural proteins of the tail fibers. The chaperone protein gp38 is also required for the proper folding of gp37. Chaperone proteins gp63 and gpwac are employed in attachment of the long tail fibers to the tail baseplate.
628:. Most of these proteins proved to be either major or minor structural components of the completed phage particle. However among the gene products (gps) necessary for phage assembly, Snustad identified a group of gps that act
640:
is divided into three independent pathways: the head, the tail and the long tail fiber pathways as detailed by Yap and
Rossman. With regard to head morphogenesis, chaperone gp31 interacts with the bacterial host chaperone
405:(Hsp10) is a single-ring heptamer that binds to GroEL in the presence of ATP or ADP. GroEL/GroES may not be able to undo previous aggregation, but it does compete in the pathway of misfolding and aggregation. Also acts in
58:
that assist the conformational folding or unfolding of large proteins or macromolecular protein complexes. There are a number of classes of molecular chaperones, all of which function to assist large proteins in proper
200:, which could counteract this reduction in folding efficiency. Some highly specific 'steric chaperones' convey unique structural information onto proteins, which cannot be folded spontaneously. Such proteins violate
653:
During overall tail assembly, chaperone proteins gp26 and gp51 are necessary for baseplate hub assembly. Gp57A is required for correct folding of gp12, a structural component of the baseplate short tail fibers.
261:
activity, induction of aggregation towards non-amyloid aggregates, suppression of toxic protein oligomers via their clustering, and in responding to diseases linked to protein aggregation and cancer maintenance.
2038:
Yochem, J; Uchida, H; Sunshine, M; Saito, H; Georgopoulos, CP; Feiss, M (4 August 1978). "Genetic analysis of two genes, dnaJ and dnaK, necessary for
Escherichia coli and bacteriophage lambda DNA replication".
191:
can accelerate the folding process, since a compact folded protein will occupy less volume than an unfolded protein chain. However, crowding can reduce the yield of correctly folded protein by increasing
2590:
Goloubinoff P, Christeller JT, Gatenby AA, Lorimer GH (1989). "Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP".
361:, many of these proteins are highly expressed under conditions of high stress, for example, when the bacterium is placed in high temperatures, thus heat shock protein chaperones are the most extensive.
2361:
Benler S, Hung SH, Vander Griend JA, Peters GA, Rohwer F, Segall AM. Gp4 is a nuclease required for morphogenesis of T4-like bacteriophages. Virology. 2020;543:7-12. doi:10.1016/j.virol.2020.01.008
1617:
Mannini B, Cascella R, Zampagni M, van Waarde-Verhagen M, Meehan S, Roodveldt C, Campioni S, Boninsegna M, Penco A, Relini A, Kampinga HH, Dobson CM, Wilson MR, Cecchi C, Chiti F (31 July 2012).
2539:
Hemmingsen SM, Woolford C, van der Vies SM, Tilly K, Dennis DT, Georgopoulos CP, et al. (May 1988). "Homologous plant and bacterial proteins chaperone oligomeric protein assembly".
2702:
2955:
1361:. Advances in Experimental Medicine and Biology. Vol. 594. New York, N.Y.: Sprinter Science+Business Media, LLC ; Austin, Tex.: Landes Bioscience/Eurekah.com. pp.
572:
structures with unfoldase activity in the presence of ATP. These proteins are thought to function as chaperones by processively threading client proteins through a small 20 Γ
(2
446:), which increase the ATP consumption rate and activity of the Hsp70s. The two protein are named "Dna" in bacteria because they were initially identified as being required for
1676:
Sadigh-Eteghad S, Majdi A, Talebi M, Mahmoudi J, Babri S (May 2015). "Regulation of nicotinic acetylcholine receptors in
AlzheimerΧ³s disease: a possible role of chaperones".
364:
A variety of nomenclatures are in use for chaperones. As heat shock proteins, the names are classically formed by "Hsp" followed by the approximate molecular mass in
457:. Although a precise mechanistic understanding has yet to be determined, it is known that Hsp70s have a high-affinity bound state to unfolded proteins when bound to
118:
in response to elevated temperatures or other cellular stresses. Heat shock protein chaperones are classified based on their observed molecular weights into Hsp60,
501:
domain. Originally thought to clamp onto their substrate protein (also known as a client protein) upon binding ATP, the recently published structures by
Vaughan
97:. The specific mode of function of chaperones differs based on their target proteins and location. Various approaches have been applied to study the structure,
93:
information for protein folding, and instead assist in protein folding by binding to and stabilizing folding intermediates until the polypeptide chain is fully
2377:
Leiman PG, Arisaka F, van Raaij MJ, et al. Morphogenesis of the T4 tail and tail fibers. Virol J. 2010;7:355. Published 2010 Dec 3. doi:10.1186/1743-422X-7-355
270:
In human cell lines, chaperone proteins were found to compose ~10% of the gross proteome mass, and are ubiquitously and highly expressed across human tissues.
153:
system). Although most newly synthesized proteins can fold in absence of chaperones, a minority strictly requires them for the same. Other chaperones work as
2695:
586:
ClpP; instead of catalyzing the refolding of client proteins, these complexes are responsible for the targeted destruction of tagged and misfolded proteins.
2437:
Laskey RA, Honda BM, Mills AD, Finch JT (October 1978). "Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA".
165:. Chaperones can also work as disaggregases, which interact with aberrant protein assemblies and revert them to monomers. Some chaperones can assist in
2688:
3300:
670:
The investigation of chaperones has a long history. The term "molecular chaperone" appeared first in the literature in 1978, and was invented by
82:. One major function of molecular chaperones is to prevent the aggregation of misfolded proteins, thus many chaperone proteins are classified as
1378:
126:, and are characterized by a stacked double-ring structure and are found in prokaryotes, in the cytosol of eukaryotes, and in mitochondria.
3518:
285:
In the endoplasmic reticulum (ER) there are general, lectin- and non-classical molecular chaperones that moderate protein folding.
1875:
678:
to prevent the aggregation of folded histone proteins with DNA during the assembly of nucleosomes. The term was later extended by
2711:
2386:
Hyman P, van Raaij M. Bacteriophage T4 long tail fiber domains. Biophys Rev. 2018;10(2):463-471. doi:10.1007/s12551-017-0348-5
2338:
Yap ML, Rossmann MG. Structure and function of bacteriophage T4. Future
Microbiol. 2014;9(12):1319-1327. doi:10.2217/fmb.14.91
355:
There are many different families of chaperones; each family acts to aid protein folding in a different way. In bacteria like
2911:
2352:
Marusich EI, Kurochkina LP, Mesyanzhinov VV. Chaperones in bacteriophage T4 assembly. Biochemistry (Mosc). 1998;63(4):399-406
290:
63:
during or after synthesis, and after partial denaturation. Chaperones are also involved in the translocation of proteins for
1403:
3548:
3543:
767:
3124:
1460:
3069:
2312:
Edgar RS, Epstein RH. The genetics of a bacterial virus. Sci Am. 1965;212:70-78. doi:10.1038/scientificamerican0265-70
1829:"Mutations in domain a' of protein disulfide isomerase affect the folding pathway of bovine pancreatic ribonuclease A"
853:"Analysis of gene expression profiles in HeLa cells in response to overexpression or siRNA-mediated depletion of NASP"
739:
327:
247:
174:
2642:
Taylor JP (August 2015). "Multisystem proteinopathy: intersecting genetics in muscle, bone, and brain degeneration".
696:
453:
It has been noted that increased expression of Hsp70 proteins in the cell results in a decreased tendency toward
398:
812:"Nuclear autoantigenic sperm protein (NASP), a linker histone chaperone that is required for cell proliferation"
3009:
593:
232:
1521:"Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae"
102:
chaperones, folding intermediates and affinity of chaperones for unstructured and structured protein chains.
70:
The first molecular chaperones discovered were a type of assembly chaperones which assist in the assembly of
3334:
184:
3506:
3375:
1100:
Balchin D, Hayer-Hartl M, Hartl FU (July 2016). "In vivo aspects of protein folding and quality control".
462:
2756:
1995:
Fenton WA, Horwich AL (May 2003). "Chaperonin-mediated protein folding: fate of substrate polypeptide".
458:
220:
94:
1155:"Macromolecular crowding perturbs protein refolding kinetics: implications for folding inside the cell"
509:
indicate that client proteins may bind externally to both the N-terminal and middle domains of Hsp90.
2600:
2548:
2497:
2446:
2193:
1900:
1780:"Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis"
1732:
1630:
1307:
1056:
617:
580:
569:
2278:
Pearl LH, Prodromou C (2006). "Structure and mechanism of the Hsp90 molecular chaperone machinery".
810:
Richardson RT, Alekseev OM, Grossman G, Widgren EE, Thresher R, Wagner EJ, et al. (July 2006).
1461:"The structural view of bacterial translocation-specific chaperone SecB: implications for function"
1043:
Nillegoda NB, Kirstein J, Szlachcic A, Berynskyy M, Stank A, Stengel F, et al. (August 2015).
724:
212:
201:
193:
166:
3365:
2733:
2667:
2624:
2572:
2521:
2470:
2064:
2020:
1977:
1701:
1501:
1434:
1276:
1135:
729:
111:
83:
657:
Synthesis of the long tail fibers depends on the chaperone protein gp57A that is needed for the
3035:
2659:
2616:
2564:
2513:
2462:
2419:
2295:
2260:
2219:
2162:
2113:
2056:
2012:
1969:
1928:
1858:
1809:
1760:
1693:
1658:
1619:"Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers"
1599:
1550:
1493:
1426:
1384:
1374:
1335:
1268:
1233:
1184:
1127:
1082:
1025:
976:
925:
884:
833:
709:
274:
258:
243:
239:
236:
47:
2291:
3295:
3254:
3249:
3224:
3214:
3209:
3199:
2999:
2651:
2608:
2556:
2505:
2454:
2409:
2287:
2250:
2209:
2201:
2152:
2144:
2131:
Vaughan CK, Gohlke U, Sobott F, Good VM, Ali MM, Prodromou C, et al. (September 2006).
2103:
2095:
2048:
2004:
1959:
1918:
1908:
1848:
1840:
1827:
Ruoppolo M, OrrΓΉ S, Talamo F, Ljung J, Pirneskoski A, Kivirikko KI, et al. (May 2003).
1799:
1791:
1750:
1740:
1685:
1648:
1638:
1589:
1581:
1540:
1532:
1483:
1475:
1418:
1366:
1362:
1355:
1325:
1315:
1260:
1223:
1215:
1174:
1166:
1117:
1109:
1072:
1064:
1015:
1007:
966:
956:
917:
874:
864:
823:
754:
406:
357:
337:
205:
98:
3270:
3204:
525:
3501:
2724:
1122:
583:
115:
60:
2604:
2552:
2501:
2450:
2197:
1904:
1736:
1634:
1311:
1060:
921:
181:. Chaperone proteins participate in the folding of over half of all mammalian proteins.
3048:
3043:
2214:
2181:
2157:
2132:
2108:
2083:
1853:
1828:
1804:
1779:
1755:
1720:
1653:
1618:
1594:
1569:
1545:
1520:
1228:
1203:
1077:
1044:
1020:
995:
971:
944:
879:
852:
744:
658:
624:
with a role in determining phage T4 structure were identified using conditional lethal
494:
2414:
2397:
2180:
Ali MM, Roe SM, Vaughan CK, Meyer P, Panaretou B, Piper PW, et al. (April 2006).
1923:
1889:"TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain"
1888:
1179:
1154:
695:
There are many disorders associated with mutations in genes encoding chaperones (i.e.
579:
Some of these Hsp100 chaperones, like ClpA and ClpX, associate with the double-ringed
3537:
1887:
Frickel EM, Riek R, Jelesarov I, Helenius A, Wuthrich K, Ellgaard L (February 2002).
1479:
1422:
1330:
1295:
679:
675:
637:
498:
2671:
2068:
2024:
1705:
1505:
600:. Deletion of the HSP104 gene results in cells that are unable to propagate certain
133:: they support the folding of proteins in an ATP-dependent manner (for example, the
17:
3404:
3386:
2628:
2576:
2525:
2474:
1981:
1438:
1280:
1139:
597:
517:
513:
309:
216:
122:, Hsp90, Hsp104, and small Hsps. The Hsp60 family of protein chaperones are termed
2680:
2655:
2148:
1745:
1689:
397:
patch at its opening; it is so large it can accommodate native folding of 54-kDa
196:. Crowding may also increase the effectiveness of the chaperone proteins such as
3480:
3348:
1721:"Inhibiting heat shock factor 1 in human cancer cells with a potent RNA aptamer"
1442:
1370:
650:
morphogenesis by cleaving packaged DNA to enable the joining of heads to tails.
394:
64:
1893:
Proceedings of the
National Academy of Sciences of the United States of America
1300:
Proceedings of the
National Academy of Sciences of the United States of America
1251:
Ellis RJ, Minton AP (May 2006). "Protein aggregation in crowded environments".
1219:
1170:
3310:
2738:
2099:
2008:
1795:
1296:"The effect of macromolecular crowding on chaperonin-mediated protein folding"
749:
719:
671:
365:
251:
178:
123:
71:
30:
1011:
3058:
3004:
2182:"Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex"
1643:
1357:
Molecular
Aspects of the Stress Response: Chaperones, Membranes and Networks
1113:
1045:"Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation"
714:
629:
573:
454:
228:
224:
157:: they bind folding intermediates to prevent their aggregation, for example
2663:
2620:
2299:
2264:
2223:
2166:
2117:
2016:
1973:
1932:
1913:
1862:
1813:
1764:
1697:
1662:
1603:
1554:
1497:
1430:
1388:
1320:
1272:
1237:
1188:
1131:
1086:
1029:
980:
888:
869:
837:
828:
811:
2568:
2517:
2423:
1536:
1339:
929:
762:
273:
Chaperones are found extensively in the endoplasmic reticulum (ER), since
3338:
2971:
2963:
2466:
2060:
1585:
1570:"Sequestration of toxic oligomers by HspB1 as a cytoprotective mechanism"
1488:
961:
561:
305:
170:
2255:
2238:
2205:
1264:
1068:
423:
3089:
2976:
2936:
2867:
2862:
2857:
2852:
2847:
2802:
2052:
1844:
1204:"Effects of macromolecular crowding on protein folding and aggregation"
621:
555:
188:
187:
may be important in chaperone function. The crowded environment of the
154:
130:
86:, as the tendency for protein aggregation is increased by heat stress.
75:
55:
1876:
Soluble complexes of target proteins and peptidyl prolyl isomerase ...
945:"A History of Molecular Chaperone Structures in the Protein Data Bank"
565:
for their ability to target and unfold tagged and misfolded proteins.
3305:
3280:
3275:
3265:
3229:
3219:
3194:
3179:
3174:
3169:
3164:
3159:
3154:
3149:
3144:
3109:
3094:
2941:
2906:
2891:
2886:
2881:
2842:
2837:
2832:
2827:
2822:
2817:
2812:
2807:
2797:
2792:
2787:
2782:
2777:
2612:
2560:
2509:
2458:
1568:
Ojha J, Masilamoni G, Dunlap D, Udoff RA, Cashikar AG (August 2011).
646:
625:
601:
589:
541:
298:
90:
576:) pore, thereby giving each client protein a second chance to fold.
438:) is perhaps the best characterized small (~ 70 kDa) chaperone. The
3496:
3486:
3476:
3461:
3443:
3438:
3433:
3428:
3360:
3320:
3285:
3259:
3244:
3239:
3234:
3189:
3184:
3139:
3134:
3129:
3099:
3084:
2981:
2950:
2931:
2926:
2921:
2916:
2901:
2896:
2876:
2772:
2765:
2761:
2751:
2746:
1964:
1947:
699:) that can affect muscle, bone and/or the central nervous system.
642:
521:
478:
439:
422:
418:
402:
390:
377:
342:
319:
315:
294:
197:
162:
138:
134:
119:
39:
35:
29:
3511:
3491:
3471:
3466:
3416:
3399:
3355:
3343:
3325:
3315:
3114:
3104:
3079:
3074:
3019:
3014:
994:
Hoffmann JH, Linke K, Graf PC, Lilie H, Jakob U (January 2004).
734:
613:
529:
257:
New functions for chaperones continue to be discovered, such as
158:
150:
146:
142:
2684:
389:) is the best characterized large (~ 1 MDa) chaperone complex.
2084:"Hsp70 chaperones: cellular functions and molecular mechanism"
1402:
Pauwels K, Van Molle I, Tommassen J, Van Gelder P (May 2007).
851:
Alekseev OM, Richardson RT, Alekseev O, O'Rand MG (May 2009).
790:
Hsp83 homologue. Name stands for "high temperature protein G".
79:
1719:
Salamanca HH, Antonyak MA, Cerione RA, Shi H, Lis JT (2014).
1153:
van den Berg B, Wain R, Dobson CM, Ellis RJ (August 2000).
211:
Other types of chaperones are involved in transport across
908:
Ellis RJ, van der Vies SM (1991). "Molecular chaperones".
1519:
Specht S, Miller SB, Mogk A, Bukau B (14 November 2011).
996:"Identification of a redox-regulated chaperone network"
532:, and also cooperates with the Hsp70 chaperone system.
89:
The majority of molecular chaperones do not convey any
1202:
van den Berg B, Ellis RJ, Dobson CM (December 1999).
2488:
Ellis J (1987). "Proteins as molecular chaperones".
674:
to describe the ability of a nuclear protein called
3454:
3385:
3374:
3057:
3034:
2992:
2732:
2718:
1354:
2348:
2346:
2344:
493:Each Hsp90 has an ATP-binding domain, a middle
351:Nomenclature and examples of chaperone families
442:proteins are aided by Hsp40 proteins (DnaJ in
2696:
2373:
2371:
2369:
2367:
2237:Terasawa K, Minami M, Minami Y (April 2005).
568:Proteins in the Hsp100/Clp family form large
8:
645:to promote proper folding of the major head
1404:"Chaperoning Anfinsen: the steric foldases"
949:International Journal of Molecular Sciences
596:, is essential for the propagation of many
3382:
2729:
2703:
2689:
2681:
2334:
2332:
2330:
2328:
2133:"Structure of an Hsp90-Cdc37-Cdk4 complex"
2413:
2254:
2213:
2156:
2107:
1963:
1922:
1912:
1852:
1803:
1778:Finka A, Goloubinoff P (September 2013).
1754:
1744:
1652:
1642:
1593:
1544:
1487:
1329:
1319:
1227:
1178:
1121:
1076:
1019:
970:
960:
878:
868:
827:
461:, and a low-affinity state when bound to
2292:10.1146/annurev.biochem.75.103004.142738
1353:Ellis RJ (2007). "Protein Misassembly".
2239:"Constantly updated knowledge of Hsp90"
802:
779:
943:Bascos NA, Landry SJ (December 2019).
857:Reproductive Biology and Endocrinology
393:(Hsp60) is a double-ring 14mer with a
27:Proteins assisting in protein folding
7:
2088:Cellular and Molecular Life Sciences
1294:Martin J, Hartl FU (February 1997).
314:Non-classical molecular chaperones:
2398:"Discovery of molecular chaperones"
922:10.1146/annurev.bi.60.070191.001541
816:The Journal of Biological Chemistry
334:Peptidyl prolyl cis-trans isomerase
3519:Prokaryotic ubiquitin-like protein
427:hsp70 pocket for substrate binding
25:
231:translocation-specific chaperone
106:Functions of molecular chaperones
42:bacterial chaperone complex model
2322:doi:10.1016/0042-6822(68)90285-7
2082:Mayer MP, Bukau B (March 2005).
2041:Molecular & General Genetics
1946:Smith, Tracy (1 December 1999).
1678:European Journal of Pharmacology
1480:10.1111/j.1365-2958.2005.04842.x
1423:10.1111/j.1365-2958.2007.05718.x
761:
1997:Quarterly Reviews of Biophysics
250:) state and guides them to the
215:, for example membranes of the
129:Some chaperone systems work as
3049:Mitochondrial targeting signal
2712:Posttranslational modification
1948:"The discovery of chaperonins"
1123:11858/00-001M-0000-002B-0856-C
1:
2280:Annual Review of Biochemistry
1459:Zhou J, Xu Z (October 2005).
910:Annual Review of Biochemistry
553:) proteins have been studied
3125:Ubiquitin-conjugating enzyme
2656:10.1212/WNL.0000000000001862
2402:Cell Stress & Chaperones
2149:10.1016/j.molcel.2006.07.016
1784:Cell Stress & Chaperones
1746:10.1371/journal.pone.0096330
1690:10.1016/j.ejphar.2015.02.047
235:maintains newly synthesized
3413:E2 SUMO-conjugating enzyme
3070:Ubiquitin-activating enzyme
2396:Ellis RJ (September 1996).
1371:10.1007/978-0-387-39975-1_1
740:Molecular chaperone therapy
328:Protein disulfide isomerase
277:often occurs in this area.
175:ubiquitin-proteasome system
3565:
3396:E1 SUMO-activating enzyme
1623:Proc. Natl. Acad. Sci. USA
539:
476:
416:
375:
2100:10.1007/s00018-004-4464-6
2009:10.1017/S0033583503003883
1952:Nature Structural Biology
1796:10.1007/s12192-013-0413-3
697:multisystem proteinopathy
3010:Survival of motor neuron
1220:10.1093/emboj/18.24.6927
1171:10.1093/emboj/19.15.3870
1012:10.1038/sj.emboj.7600016
786:Initially identified as
618:bacteriophage (phage) T4
594:Saccharomyces cerevisiae
409:as molecular chaperone.
385:(GroEL/GroES complex in
266:Human chaperone proteins
3376:Ubiquitin-like proteins
3335:Deubiquitinating enzyme
2243:Journal of Biochemistry
1644:10.1073/pnas.1117799109
1114:10.1126/science.aac4354
512:Hsp90 may also require
185:Macromolecular crowding
1914:10.1073/pnas.042699099
1468:Molecular Microbiology
1411:Molecular Microbiology
1321:10.1073/pnas.94.4.1107
870:10.1186/1477-7827-7-45
829:10.1074/jbc.M603816200
428:
169:, leading proteins to
43:
1537:10.1083/jcb.201106037
770:at Wikimedia Commons
691:Clinical significance
426:
281:Endoplasmic reticulum
221:endoplasmic reticulum
173:systems, such as the
33:
3549:Protein biosynthesis
3544:Molecular chaperones
1586:10.1128/MCB.01187-10
1253:Biological Chemistry
962:10.3390/ijms20246195
407:mitochondrial matrix
324:Folding chaperones:
289:General chaperones:
114:, that is, proteins
110:Many chaperones are
52:molecular chaperones
18:Molecular chaperones
2734:Heat shock proteins
2605:1989Natur.342..884G
2553:1988Natur.333..330H
2502:1987Natur.328..378E
2451:1978Natur.275..416L
2206:10.1038/nature04716
2198:2006Natur.440.1013A
1905:2002PNAS...99.1954F
1737:2014PLoSO...996330S
1635:2012PNAS..10912479M
1312:1997PNAS...94.1107M
1265:10.1515/BC.2006.064
1069:10.1038/nature14884
1061:2015Natur.524..247N
735:Heat shock factor 1
725:Chemical chaperones
710:Biological machines
304:Lectin chaperones:
208:to fold correctly.
194:protein aggregation
167:protein degradation
112:heat shock proteins
84:heat shock proteins
2053:10.1007/BF00267593
1845:10.1110/ps.0242803
768:Chaperone proteins
730:Heat shock protein
429:
248:generally unfolded
240:polypeptide chains
44:
34:A top-view of the
3531:
3530:
3527:
3526:
3036:Protein targeting
3030:
3029:
2256:10.1093/jb/mvi056
1380:978-0-387-39974-4
1108:(6294): aac4354.
766:Media related to
450:DNA replication.
275:protein synthesis
259:bacterial adhesin
48:molecular biology
16:(Redirected from
3556:
3383:
3296:Ubiquitin ligase
3062:(ubiquitylation)
3000:Alpha crystallin
2730:
2705:
2698:
2691:
2682:
2676:
2675:
2639:
2633:
2632:
2613:10.1038/342884a0
2587:
2581:
2580:
2561:10.1038/333330a0
2536:
2530:
2529:
2510:10.1038/328378a0
2485:
2479:
2478:
2459:10.1038/275416a0
2445:(5679): 416β20.
2434:
2428:
2427:
2417:
2393:
2387:
2384:
2378:
2375:
2362:
2359:
2353:
2350:
2339:
2336:
2323:
2319:
2313:
2310:
2304:
2303:
2275:
2269:
2268:
2258:
2234:
2228:
2227:
2217:
2192:(7087): 1013β7.
2177:
2171:
2170:
2160:
2128:
2122:
2121:
2111:
2079:
2073:
2072:
2035:
2029:
2028:
1992:
1986:
1985:
1967:
1943:
1937:
1936:
1926:
1916:
1884:
1878:
1873:
1867:
1866:
1856:
1824:
1818:
1817:
1807:
1775:
1769:
1768:
1758:
1748:
1716:
1710:
1709:
1673:
1667:
1666:
1656:
1646:
1629:(31): 12479β84.
1614:
1608:
1607:
1597:
1565:
1559:
1558:
1548:
1516:
1510:
1509:
1491:
1465:
1456:
1450:
1449:
1447:
1441:. Archived from
1408:
1399:
1393:
1392:
1360:
1350:
1344:
1343:
1333:
1323:
1291:
1285:
1284:
1248:
1242:
1241:
1231:
1208:The EMBO Journal
1199:
1193:
1192:
1182:
1159:The EMBO Journal
1150:
1144:
1143:
1125:
1097:
1091:
1090:
1080:
1055:(7564): 247β51.
1040:
1034:
1033:
1023:
1000:The EMBO Journal
991:
985:
984:
974:
964:
940:
934:
933:
905:
899:
893:
892:
882:
872:
848:
842:
841:
831:
822:(30): 21526β34.
807:
791:
784:
765:
755:Protein dynamics
592:, the Hsp100 of
338:Prolyl isomerase
206:protein dynamics
202:Anfinsen's dogma
21:
3564:
3563:
3559:
3558:
3557:
3555:
3554:
3553:
3534:
3533:
3532:
3523:
3450:
3425:E3 SUMO ligase
3389:
3378:
3370:
3061:
3053:
3026:
2988:
2967:
2959:
2737:
2725:protein folding
2723:
2714:
2709:
2679:
2641:
2640:
2636:
2599:(6252): 884β9.
2589:
2588:
2584:
2547:(6171): 330β4.
2538:
2537:
2533:
2496:(6129): 378β9.
2487:
2486:
2482:
2436:
2435:
2431:
2395:
2394:
2390:
2385:
2381:
2376:
2365:
2360:
2356:
2351:
2342:
2337:
2326:
2320:
2316:
2311:
2307:
2277:
2276:
2272:
2236:
2235:
2231:
2179:
2178:
2174:
2130:
2129:
2125:
2081:
2080:
2076:
2037:
2036:
2032:
1994:
1993:
1989:
1945:
1944:
1940:
1886:
1885:
1881:
1874:
1870:
1833:Protein Science
1826:
1825:
1821:
1777:
1776:
1772:
1718:
1717:
1713:
1675:
1674:
1670:
1616:
1615:
1611:
1580:(15): 3146β57.
1574:Mol. Cell. Biol
1567:
1566:
1562:
1518:
1517:
1513:
1463:
1458:
1457:
1453:
1445:
1406:
1401:
1400:
1396:
1381:
1352:
1351:
1347:
1293:
1292:
1288:
1250:
1249:
1245:
1214:(24): 6927β33.
1201:
1200:
1196:
1152:
1151:
1147:
1099:
1098:
1094:
1042:
1041:
1037:
993:
992:
988:
942:
941:
937:
907:
906:
902:
896:
850:
849:
845:
809:
808:
804:
800:
795:
794:
785:
781:
776:
759:
705:
693:
668:
610:
584:serine protease
549:(Clp family in
544:
538:
481:
475:
469:in eukaryotes.
421:
415:
413:Hsp70 and Hsp40
380:
374:
372:Hsp10 and Hsp60
353:
283:
268:
108:
61:protein folding
28:
23:
22:
15:
12:
11:
5:
3562:
3560:
3552:
3551:
3546:
3536:
3535:
3529:
3528:
3525:
3524:
3522:
3521:
3515:
3514:
3509:
3504:
3499:
3494:
3489:
3484:
3474:
3469:
3464:
3458:
3456:
3452:
3451:
3449:
3448:
3447:
3446:
3441:
3436:
3431:
3422:
3421:
3420:
3419:
3410:
3409:
3408:
3407:
3402:
3393:
3391:
3380:
3372:
3371:
3369:
3368:
3363:
3358:
3352:
3351:
3346:
3341:
3331:
3330:
3329:
3328:
3323:
3318:
3313:
3308:
3303:
3291:
3290:
3289:
3288:
3283:
3278:
3273:
3268:
3263:
3257:
3252:
3247:
3242:
3237:
3232:
3227:
3222:
3217:
3212:
3207:
3202:
3197:
3192:
3187:
3182:
3177:
3172:
3167:
3162:
3157:
3152:
3147:
3142:
3137:
3132:
3120:
3119:
3118:
3117:
3112:
3107:
3102:
3097:
3092:
3087:
3082:
3077:
3065:
3063:
3055:
3054:
3052:
3051:
3046:
3044:Signal peptide
3040:
3038:
3032:
3031:
3028:
3027:
3025:
3024:
3023:
3022:
3017:
3007:
3002:
2996:
2994:
2990:
2989:
2987:
2986:
2985:
2984:
2979:
2974:
2969:
2965:
2961:
2957:
2947:
2946:
2945:
2944:
2939:
2934:
2929:
2924:
2919:
2914:
2909:
2904:
2899:
2894:
2889:
2884:
2873:
2872:
2871:
2870:
2865:
2860:
2855:
2850:
2845:
2840:
2835:
2830:
2825:
2820:
2815:
2810:
2805:
2800:
2795:
2790:
2785:
2780:
2769:
2768:
2759:
2754:
2749:
2743:
2741:
2727:
2716:
2715:
2710:
2708:
2707:
2700:
2693:
2685:
2678:
2677:
2634:
2582:
2531:
2480:
2429:
2388:
2379:
2363:
2354:
2340:
2324:
2314:
2305:
2270:
2229:
2172:
2143:(5): 697β707.
2137:Molecular Cell
2123:
2074:
2030:
1987:
1938:
1879:
1868:
1819:
1790:(5): 591β605.
1770:
1711:
1668:
1609:
1560:
1511:
1451:
1448:on 2012-05-23.
1394:
1379:
1345:
1306:(4): 1107β12.
1286:
1243:
1194:
1165:(15): 3870β5.
1145:
1092:
1035:
986:
935:
900:
894:
843:
801:
799:
796:
793:
792:
778:
777:
775:
772:
758:
757:
752:
747:
745:Pharmacoperone
742:
737:
732:
727:
722:
717:
712:
706:
704:
701:
692:
689:
667:
664:
609:
606:
581:tetradecameric
540:Main article:
537:
534:
477:Main article:
474:
471:
417:Main article:
414:
411:
401:in its lumen.
376:Main article:
373:
370:
352:
349:
348:
347:
346:
345:
340:
331:
322:
312:
302:
282:
279:
267:
264:
107:
104:
26:
24:
14:
13:
10:
9:
6:
4:
3:
2:
3561:
3550:
3547:
3545:
3542:
3541:
3539:
3520:
3517:
3516:
3513:
3510:
3508:
3505:
3503:
3500:
3498:
3495:
3493:
3490:
3488:
3485:
3482:
3478:
3475:
3473:
3470:
3468:
3465:
3463:
3460:
3459:
3457:
3453:
3445:
3442:
3440:
3437:
3435:
3432:
3430:
3427:
3426:
3424:
3423:
3418:
3415:
3414:
3412:
3411:
3406:
3403:
3401:
3398:
3397:
3395:
3394:
3392:
3390:(SUMOylation)
3388:
3384:
3381:
3377:
3373:
3367:
3364:
3362:
3359:
3357:
3354:
3353:
3350:
3347:
3345:
3342:
3340:
3336:
3333:
3332:
3327:
3324:
3322:
3319:
3317:
3314:
3312:
3309:
3307:
3304:
3302:
3299:
3298:
3297:
3293:
3292:
3287:
3284:
3282:
3279:
3277:
3274:
3272:
3269:
3267:
3264:
3261:
3258:
3256:
3253:
3251:
3248:
3246:
3243:
3241:
3238:
3236:
3233:
3231:
3228:
3226:
3223:
3221:
3218:
3216:
3213:
3211:
3208:
3206:
3203:
3201:
3198:
3196:
3193:
3191:
3188:
3186:
3183:
3181:
3178:
3176:
3173:
3171:
3168:
3166:
3163:
3161:
3158:
3156:
3153:
3151:
3148:
3146:
3143:
3141:
3138:
3136:
3133:
3131:
3128:
3127:
3126:
3122:
3121:
3116:
3113:
3111:
3108:
3106:
3103:
3101:
3098:
3096:
3093:
3091:
3088:
3086:
3083:
3081:
3078:
3076:
3073:
3072:
3071:
3067:
3066:
3064:
3060:
3056:
3050:
3047:
3045:
3042:
3041:
3039:
3037:
3033:
3021:
3018:
3016:
3013:
3012:
3011:
3008:
3006:
3003:
3001:
2998:
2997:
2995:
2991:
2983:
2980:
2978:
2975:
2973:
2970:
2968:
2962:
2960:
2954:
2953:
2952:
2949:
2948:
2943:
2940:
2938:
2935:
2933:
2930:
2928:
2925:
2923:
2920:
2918:
2915:
2913:
2910:
2908:
2905:
2903:
2900:
2898:
2895:
2893:
2890:
2888:
2885:
2883:
2880:
2879:
2878:
2875:
2874:
2869:
2866:
2864:
2861:
2859:
2856:
2854:
2851:
2849:
2846:
2844:
2841:
2839:
2836:
2834:
2831:
2829:
2826:
2824:
2821:
2819:
2816:
2814:
2811:
2809:
2806:
2804:
2801:
2799:
2796:
2794:
2791:
2789:
2786:
2784:
2781:
2779:
2776:
2775:
2774:
2771:
2770:
2767:
2763:
2760:
2758:
2755:
2753:
2750:
2748:
2745:
2744:
2742:
2740:
2735:
2731:
2728:
2726:
2721:
2717:
2713:
2706:
2701:
2699:
2694:
2692:
2687:
2686:
2683:
2673:
2669:
2665:
2661:
2657:
2653:
2650:(8): 658β60.
2649:
2645:
2638:
2635:
2630:
2626:
2622:
2618:
2614:
2610:
2606:
2602:
2598:
2594:
2586:
2583:
2578:
2574:
2570:
2566:
2562:
2558:
2554:
2550:
2546:
2542:
2535:
2532:
2527:
2523:
2519:
2515:
2511:
2507:
2503:
2499:
2495:
2491:
2484:
2481:
2476:
2472:
2468:
2464:
2460:
2456:
2452:
2448:
2444:
2440:
2433:
2430:
2425:
2421:
2416:
2411:
2408:(3): 155β60.
2407:
2403:
2399:
2392:
2389:
2383:
2380:
2374:
2372:
2370:
2368:
2364:
2358:
2355:
2349:
2347:
2345:
2341:
2335:
2333:
2331:
2329:
2325:
2318:
2315:
2309:
2306:
2301:
2297:
2293:
2289:
2285:
2281:
2274:
2271:
2266:
2262:
2257:
2252:
2248:
2244:
2240:
2233:
2230:
2225:
2221:
2216:
2211:
2207:
2203:
2199:
2195:
2191:
2187:
2183:
2176:
2173:
2168:
2164:
2159:
2154:
2150:
2146:
2142:
2138:
2134:
2127:
2124:
2119:
2115:
2110:
2105:
2101:
2097:
2094:(6): 670β84.
2093:
2089:
2085:
2078:
2075:
2070:
2066:
2062:
2058:
2054:
2050:
2046:
2042:
2034:
2031:
2026:
2022:
2018:
2014:
2010:
2006:
2003:(2): 229β56.
2002:
1998:
1991:
1988:
1983:
1979:
1975:
1971:
1966:
1965:10.1038/70015
1961:
1957:
1953:
1949:
1942:
1939:
1934:
1930:
1925:
1920:
1915:
1910:
1906:
1902:
1899:(4): 1954β9.
1898:
1894:
1890:
1883:
1880:
1877:
1872:
1869:
1864:
1860:
1855:
1850:
1846:
1842:
1839:(5): 939β52.
1838:
1834:
1830:
1823:
1820:
1815:
1811:
1806:
1801:
1797:
1793:
1789:
1785:
1781:
1774:
1771:
1766:
1762:
1757:
1752:
1747:
1742:
1738:
1734:
1731:(5): e96330.
1730:
1726:
1722:
1715:
1712:
1707:
1703:
1699:
1695:
1691:
1687:
1683:
1679:
1672:
1669:
1664:
1660:
1655:
1650:
1645:
1640:
1636:
1632:
1628:
1624:
1620:
1613:
1610:
1605:
1601:
1596:
1591:
1587:
1583:
1579:
1575:
1571:
1564:
1561:
1556:
1552:
1547:
1542:
1538:
1534:
1531:(4): 617β29.
1530:
1526:
1522:
1515:
1512:
1507:
1503:
1499:
1495:
1490:
1489:2027.42/74325
1485:
1481:
1477:
1474:(2): 349β57.
1473:
1469:
1462:
1455:
1452:
1444:
1440:
1436:
1432:
1428:
1424:
1420:
1417:(4): 917β22.
1416:
1412:
1405:
1398:
1395:
1390:
1386:
1382:
1376:
1372:
1368:
1364:
1359:
1358:
1349:
1346:
1341:
1337:
1332:
1327:
1322:
1317:
1313:
1309:
1305:
1301:
1297:
1290:
1287:
1282:
1278:
1274:
1270:
1266:
1262:
1259:(5): 485β97.
1258:
1254:
1247:
1244:
1239:
1235:
1230:
1225:
1221:
1217:
1213:
1209:
1205:
1198:
1195:
1190:
1186:
1181:
1176:
1172:
1168:
1164:
1160:
1156:
1149:
1146:
1141:
1137:
1133:
1129:
1124:
1119:
1115:
1111:
1107:
1103:
1096:
1093:
1088:
1084:
1079:
1074:
1070:
1066:
1062:
1058:
1054:
1050:
1046:
1039:
1036:
1031:
1027:
1022:
1017:
1013:
1009:
1005:
1001:
997:
990:
987:
982:
978:
973:
968:
963:
958:
954:
950:
946:
939:
936:
931:
927:
923:
919:
915:
911:
904:
901:
898:
895:
890:
886:
881:
876:
871:
866:
862:
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854:
847:
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839:
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830:
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821:
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806:
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789:
783:
780:
773:
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769:
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728:
726:
723:
721:
718:
716:
713:
711:
708:
707:
702:
700:
698:
690:
688:
686:
683:demonstrated
681:
680:R. John Ellis
677:
676:nucleoplasmin
673:
665:
663:
660:
659:trimerization
655:
651:
648:
644:
639:
638:morphogenesis
634:
631:
630:catalytically
627:
623:
619:
615:
608:Bacteriophage
607:
605:
603:
599:
595:
591:
587:
585:
582:
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571:
566:
564:
563:
558:
557:
552:
548:
543:
535:
533:
531:
527:
523:
519:
518:immunophilins
515:
514:co-chaperones
510:
508:
504:
500:
496:
491:
489:
485:
480:
472:
470:
466:
464:
460:
456:
451:
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296:
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288:
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280:
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271:
265:
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253:
249:
245:
244:translocation
241:
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230:
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156:
152:
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144:
140:
136:
132:
127:
125:
121:
117:
113:
105:
103:
100:
96:
92:
87:
85:
81:
77:
73:
68:
66:
62:
57:
53:
49:
41:
37:
32:
19:
3387:SUMO protein
2719:
2647:
2643:
2637:
2596:
2592:
2585:
2544:
2540:
2534:
2493:
2489:
2483:
2442:
2438:
2432:
2405:
2401:
2391:
2382:
2357:
2317:
2308:
2283:
2279:
2273:
2249:(4): 443β7.
2246:
2242:
2232:
2189:
2185:
2175:
2140:
2136:
2126:
2091:
2087:
2077:
2044:
2040:
2033:
2000:
1996:
1990:
1958:(12): 1090.
1955:
1951:
1941:
1896:
1892:
1882:
1871:
1836:
1832:
1822:
1787:
1783:
1773:
1728:
1724:
1714:
1681:
1677:
1671:
1626:
1622:
1612:
1577:
1573:
1563:
1528:
1525:J. Cell Biol
1524:
1514:
1471:
1467:
1454:
1443:the original
1414:
1410:
1397:
1356:
1348:
1303:
1299:
1289:
1256:
1252:
1246:
1211:
1207:
1197:
1162:
1158:
1148:
1105:
1101:
1095:
1052:
1048:
1038:
1006:(1): 160β8.
1003:
999:
989:
955:(24): 6195.
952:
948:
938:
913:
909:
903:
897:
860:
856:
846:
819:
815:
805:
787:
782:
760:
694:
684:
669:
656:
652:
635:
633:chaperones.
620:that encode
611:
598:yeast prions
588:
578:
567:
560:
554:
550:
546:
545:
511:
506:
502:
499:dimerization
492:
487:
483:
482:
467:
452:
447:
443:
435:
431:
430:
386:
382:
381:
363:
356:
354:
333:
310:calreticulin
284:
272:
269:
256:
246:-competent (
217:mitochondria
210:
204:, requiring
183:
128:
109:
88:
74:from folded
69:
51:
45:
3481:neddylation
2747:Hsp10/GroES
2739:Chaperonins
2047:(1): 9β14.
916:: 321β347.
788:Drosophilia
395:hydrophobic
366:kilodaltons
124:chaperonins
72:nucleosomes
65:proteolysis
3538:Categories
2773:Hsp40/DnaJ
2720:Chaperones
2286:: 271β94.
798:References
750:Proteasome
720:Chaperonin
672:Ron Laskey
252:translocon
225:eukaryotes
179:eukaryotes
95:translated
3059:Ubiquitin
3005:Clusterin
2644:Neurology
1684:: 34β41.
715:Chaperome
636:Phage T4
570:hexameric
486:(HtpG in
455:apoptosis
434:(DnaK in
291:GRP78/BiP
237:precursor
229:bacterial
213:membranes
116:expressed
3339:Ataxin 3
2672:42203997
2664:26208960
2621:10532860
2300:16756493
2265:15858167
2224:16625188
2167:16949366
2118:15770419
2069:28144214
2025:10328521
2017:14686103
1974:10581544
1933:11842220
1863:12717017
1814:23430704
1765:24800749
1725:PLOS ONE
1706:31929001
1698:25771456
1663:22802614
1604:21670152
1555:22065637
1506:33227532
1498:16194224
1431:17501917
1389:17205670
1273:16740119
1238:10601015
1189:10921869
1132:27365453
1087:26245380
1030:14685279
981:31817979
889:19439102
838:16728391
703:See also
685:in vitro
622:proteins
562:in vitro
505:and Ali
497:, and a
383:Hsp10/60
306:calnexin
223:(ER) in
171:protease
155:holdases
131:foldases
99:dynamics
76:histones
56:proteins
3262:(CDC34)
2629:4319510
2601:Bibcode
2577:4325057
2569:2897629
2549:Bibcode
2526:4337273
2518:3112578
2498:Bibcode
2475:2535641
2447:Bibcode
2424:9222600
2215:5703407
2194:Bibcode
2158:5704897
2109:2773841
1982:6158370
1901:Bibcode
1854:2323865
1805:3745260
1756:4011729
1733:Bibcode
1654:3411936
1631:Bibcode
1595:3147607
1546:3257523
1439:6435829
1340:9037014
1308:Bibcode
1281:7336464
1229:1171756
1140:5174431
1102:Science
1078:4830470
1057:Bibcode
1021:1271656
972:6940948
930:1679318
880:2686705
666:History
626:mutants
556:in vivo
551:E. coli
528:), and
524:, p50 (
488:E. coli
448:E. coli
444:E. coli
436:E. coli
387:E. coli
358:E. coli
336:(PPI),
189:cytosol
141:or the
3306:Cullin
2670:
2662:
2627:
2619:
2593:Nature
2575:
2567:
2541:Nature
2524:
2516:
2490:Nature
2473:
2467:692721
2465:
2439:Nature
2422:
2415:248474
2412:
2298:
2263:
2222:
2212:
2186:Nature
2165:
2155:
2116:
2106:
2067:
2061:360041
2059:
2023:
2015:
1980:
1972:
1931:
1924:122301
1921:
1861:
1851:
1812:
1802:
1763:
1753:
1704:
1696:
1661:
1651:
1602:
1592:
1553:
1543:
1504:
1496:
1437:
1429:
1387:
1377:
1338:
1328:
1279:
1271:
1236:
1226:
1187:
1180:306593
1177:
1138:
1130:
1085:
1075:
1049:Nature
1028:
1018:
979:
969:
928:
887:
877:
863:: 45.
836:
647:capsid
602:prions
590:Hsp104
547:Hsp100
542:HSP100
536:Hsp100
516:-like
507:et al.
503:et al.
495:domain
330:(PDI),
299:GRP170
91:steric
3497:ATG12
3487:FAT10
3477:NEDD8
3462:ISG15
3455:Other
3444:PIAS4
3439:PIAS3
3434:PIAS2
3429:PIAS1
3379:(UBL)
3361:BIRC6
3321:FANCL
2993:Other
2982:TRAP1
2951:Hsp90
2877:Hsp70
2766:GroEL
2762:HSP60
2757:Hsp47
2752:Hsp27
2668:S2CID
2625:S2CID
2573:S2CID
2522:S2CID
2471:S2CID
2065:S2CID
2021:S2CID
1978:S2CID
1702:S2CID
1502:S2CID
1464:(PDF)
1446:(PDF)
1435:S2CID
1407:(PDF)
1331:19752
1277:S2CID
1136:S2CID
774:Notes
643:GroEL
614:genes
526:Cdc37
484:Hsp90
479:Hsp90
473:Hsp90
440:Hsp70
432:Hsp70
419:Hsp70
403:GroES
391:GroEL
378:HSP60
343:ERp57
320:ERp29
316:HSP47
295:GRP94
242:in a
198:GroEL
163:Hsp33
139:GroES
135:GroEL
120:Hsp70
40:GroEL
36:GroES
3512:UBL5
3502:FUB1
3492:ATG8
3472:UFM1
3467:URM1
3417:UBC9
3405:SAE2
3400:SAE1
3366:UFC1
3356:ATG3
3349:CYLD
3344:USP6
3326:UBR1
3316:MDM2
3115:SAE1
3110:NAE1
3105:ATG7
3100:UBA7
3095:UBA6
3090:UBA5
3085:UBA3
3080:UBA2
3075:UBA1
3020:SMN2
3015:SMN1
2660:PMID
2617:PMID
2565:PMID
2514:PMID
2463:PMID
2420:PMID
2296:PMID
2261:PMID
2220:PMID
2163:PMID
2114:PMID
2057:PMID
2013:PMID
1970:PMID
1929:PMID
1859:PMID
1810:PMID
1761:PMID
1694:PMID
1659:PMID
1600:PMID
1551:PMID
1494:PMID
1427:PMID
1385:PMID
1375:ISBN
1363:1β13
1336:PMID
1269:PMID
1234:PMID
1185:PMID
1128:PMID
1083:PMID
1026:PMID
977:PMID
926:PMID
885:PMID
834:PMID
612:The
559:and
530:Aha1
522:Sti1
318:and
308:and
233:SecB
227:. A
219:and
159:DnaJ
151:GrpE
147:DnaJ
143:DnaK
78:and
54:are
3507:MUB
3311:CBL
3301:VHL
3294:E3
3123:E2
3068:E1
2937:12A
2868:C19
2863:C14
2858:C13
2853:C11
2848:C10
2803:B11
2652:doi
2609:doi
2597:342
2557:doi
2545:333
2506:doi
2494:328
2455:doi
2443:275
2410:PMC
2288:doi
2251:doi
2247:137
2210:PMC
2202:doi
2190:440
2153:PMC
2145:doi
2104:PMC
2096:doi
2049:doi
2045:164
2005:doi
1960:doi
1919:PMC
1909:doi
1849:PMC
1841:doi
1800:PMC
1792:doi
1751:PMC
1741:doi
1686:doi
1682:755
1649:PMC
1639:doi
1627:109
1590:PMC
1582:doi
1541:PMC
1533:doi
1529:195
1484:hdl
1476:doi
1419:doi
1367:doi
1326:PMC
1316:doi
1261:doi
1257:387
1224:PMC
1216:doi
1175:PMC
1167:doi
1118:hdl
1110:doi
1106:353
1073:PMC
1065:doi
1053:524
1016:PMC
1008:doi
967:PMC
957:doi
918:doi
875:PMC
865:doi
824:doi
820:281
616:of
463:ATP
459:ADP
399:GFP
177:in
161:or
80:DNA
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3281:V2
3276:V1
3266:R2
3260:R1
3255:Q2
3250:Q1
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3220:L3
3215:L2
3210:L1
3200:J2
3195:J1
3180:G2
3175:G1
3170:E3
3165:E2
3160:E1
3155:D3
3150:D2
3145:D1
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