Tag chaperonin [52 articles] Export

Recent papers classified by the tag chaperonin.

	Cooperativity in the Thermosome [My Copy] Journal of Molecular Biology, Vol. 348, No. 1. (April 2005), pp. 13-26. by M. Bigotti, A. Clarke posted to thermosome cooperativity chaperonin by yanjiang on 2009-11-14 00:10:48 as
	The Chaperonin ATPase Cycle: Mechanism of Allosteric Switching and Movements of Substrate-Binding Domains in GroEL [My Copy] Cell, Vol. 87, No. 2. (October 1996), pp. 241-251. by A. Roseman posted to chaperonin atpase allostery by yanjiang on 2009-11-02 22:37:57 as
	Chaperonin-mediated protein folding: using a central cavity to kinetically assist polypeptide chain folding [My Copy] Quarterly Reviews of Biophysics, Vol. 42, No. 02. (2009), pp. 83-116. by Arthur L. Horwich, Wayne A. Fenton posted to review chaperonin by quanwang on 2009-10-25 07:29:45 as
	Characterization of Archaeal Group II Chaperonin-ADP-Metal Fluoride Complexes: IMPLICATIONS THAT GROUP II CHAPERONINS OPERATE AS A "TWO-STROKE ENGINE" [My Copy] J. Biol. Chem., Vol. 280, No. 48. (2 December 2005), pp. 40375-40383. by Ryo Iizuka, Takao Yoshida, Noriyuki Ishii, et al.Tamotsu Zako, Kazunobu Takahashi, Kosuke Maki, Tomonao Inobe, Kunihiro Kuwajima, Masafumi Yohda posted to chaperonin aluminum-fluoride allostery adp by yanjiang on 2009-08-26 00:51:18 as
	Conformational rearrangements of an archaeal chaperonin upon ATPase cycling [My Copy] Current Biology, Vol. 10, No. 7. (01 April 2000), pp. 405-408. by Irina Gutsche, Jörg Holzinger, Manfred Rößle, Hermann Heumann, Wolfgang Baumeister, Roland P. May posted to cryo-em conformation chaperonin atpase by yanjiang on 2009-08-25 05:03:54 as
	The 'sequential allosteric ring' mechanism in the eukaryotic chaperonin-assisted folding of actin and tubulin. [My Copy] The EMBO journal, Vol. 20, No. 15. (1 August 2001), pp. 4065-4075. by O. Llorca, J. Martín-Benito, J. Grantham, et al.M. Ritco-Vonsovici, K. R. Willison, J. L. Carrascosa, J. M. Valpuesta posted to tric chaperonin allostery by yanjiang on 2009-08-25 04:57:49 as
	Structural Stability of Covalently Linked GroES Heptamer: Advantages in the Formation of Oligomeric Structure [My Copy] Journal of Molecular Biology, Vol. 367, No. 4. (06 April 2007), pp. 1171-1185. by Isao Sakane, Kunihiro Hongo, Fumihiro Motojima, Shigeto Murayama, Tomohiro Mizobata, Yasushi Kawata posted to chaperonin by omc11 on 2009-08-13 12:59:01 as
	Allosteric regulation of chaperonins [My Copy] Current Opinion in Structural Biology, Vol. 15, No. 6. (December 2005), pp. 646-651. by A. Horovitz, K. Willison posted to chaperonin by omc11 on 2009-07-30 10:56:40 as
	Chaperone machines in action. [My Copy] Current opinion in structural biology, Vol. 18, No. 1. (February 2008), pp. 35-42. by Helen R. Saibil posted to chaperones chaperonin gartmann by bratwurst on 2009-06-23 14:45:13 as along with 1 person guhjy
	Two families of chaperonin: physiology and mechanism. [My Copy] Annu Rev Cell Dev Biol, Vol. 23 (2007), pp. 115-145. by A. L. Horwich, W. A. Fenton, E. Chapman, G. W. Farr posted to chaperonin gartmann by bratwurst on 2009-06-19 11:26:00 as along with 2 people and 1 group thegoose2 tharris C. elegans / WormBase
	Functional consequences of single:double ring transitions in chaperonins: life in the cold [My Copy] Molecular Microbiology, Vol. 53, No. 1. (2004), pp. 167-182. by Manuel Ferrer, Heinrich Lünsdorf, Tatyana N. Chernikova, Michail Yakimov, Kenneth N. Timmis, Peter N. Golyshin posted to chaperonin by omc11 on 2009-04-20 16:28:31 as
	Brassica napus plastid and mitochondrial chaperonin-60 proteins contain multiple distinct polypeptides. [My Copy] Plant physiology, Vol. 105, No. 1. (May 1994), pp. 233-241. by L. P. Cloney, D. R. Bekkaoui, G. L. Feist, W. S. Lane, S. M. Hemmingsen posted to chaperonin plant by omc11 on 2009-04-20 15:56:48 as
	cDNA sequence and overexpression of chloroplast chaperonin 21 from Arabidopsis thaliana [My Copy] Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, Vol. 1429, No. 2. (11 January 1999), pp. 512-515. by T. Hirohashi, K. Nishio, M. Nakai posted to chaperonin plant by omc11 on 2009-04-17 14:33:41 as
	Purification and characterization of chaperonin 60 and heat-shock protein 70 from chromoplasts of Narcissus pseudonarcissus. [My Copy] Plant physiology, Vol. 111, No. 3. (July 1996), pp. 931-939. by M. Bonk, M. Tadros, J. Vandekerckhove, S. Al-Babili, P. Beyer posted to chaperonin plant by omc11 on 2009-04-17 14:27:06 as
	Chaperonin complex with a newly folded protein encapsulated in the folding chamber. [My Copy] Nature, Vol. 457, No. 7225. (1 January 2009), pp. 107-110. by D. K. Clare, P. J. Bakkes, H. van Heerikhuizen, S. M. van der Vies, H. R. Saibil posted to chaperonin em experiment protein structure by cactus on 2009-01-19 08:22:09 as along with 2 people and 1 group noraziz jmrivort Supramolecular
	A Histidine-rich and Cysteine-rich Metal-binding Domain at the C Terminus of Heat Shock Protein A from Helicobacter pylori: IMPLICATION FOR NICKEL HOMEOSTASIS AND BISMUTH SUSCEPTIBILITY [My Copy] J. Biol. Chem., Vol. 283, No. 22. (30 May 2008), pp. 15142-15151. by Shujian Cun, Hongyan Li, Ruiguang Ge, Marie C. Lin, Hongzhe Sun posted to bismuth chaperonin cpn10 cysteine-rich domain groes helicobacter histidine-rich hsp10 hspa metal-binding nickel pylori by csjonline on 2008-12-20 09:08:23 as
	Conserved residues modulate copper release in human copper chaperone Atox1 [My Copy] Proceedings of the National Academy of Sciences, Vol. 105, No. 32. (2008), pp. 11158-11163. by Faiza Hussain, John S. Olson, Pernilla Wittung-Stafshede posted to atox1 chaperonin cui domain metal-binding by csjonline on 2008-12-20 08:35:45 as along with 1 person vzaraysk
	Chaperonin chamber accelerates protein folding through passive action of preventing aggregation [My Copy] Proceedings of the National Academy of Sciences, Vol. 105, No. 45. (11 November 2008), pp. 17351-17355. by Adrian C. Apetri, Arthur L. Horwich posted to chaperonin experiment folding protein by cactus on 2008-12-18 06:09:46 as
	Dual Function of Protein Confinement in Chaperonin-Assisted Protein Folding [My Copy] Cell, Vol. 107, No. 2. (October 2001), pp. 223-233. by A. Brinker posted to chaperonin experiment folding protein by cactus on 2008-12-18 06:06:17 as
	High resolution surface structure of E. coli GroES oligomer by atomic force microscopy [My Copy] FEBS Letters, Vol. 381, No. 1-2. (26 February 1996), pp. 161-164. by Jianxun Mou, D. M. Czajkowsky, Sitong Sheng, Rouya Ho, Zhifeng Shao posted to chaperonin groes by csjonline on 2008-12-17 11:09:29 as along with 1 person hsekiguc
	A chaperonin from a thermophilic bacterium, Thermus thermophilus, that controls refoldings of several thermophilic enzymes [My Copy] J. Biol. Chem., Vol. 266, No. 33. (25 November 1991), pp. 22411-22418. by H. Taguchi, J. Konishi, N. Ishii, M. Yoshida posted to chaperonin tthgroel by rph on 2008-12-17 01:05:01 as
	Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL [My Copy] Proceedings of the National Academy of Sciences of the United States of America, Vol. 94, No. 4. (18 February 1997), pp. 1080-1085. by Matthew s Goldberg, Jing Zhang, Stacey Sondek, Robert C. . Matthews, Robert o Fox, Arthur l Horwich posted to chaperonin exchange groel hdhfr by rph on 2008-12-16 01:17:23 as
	A structural model for GroEL-polypeptide recognition. [My Copy] Proceedings of the National Academy of Sciences of the United States of America, Vol. 94, No. 8. (15 April 1997), pp. 3571-3575. by A. M. Buckle, R. Zahn, A. R. Fersht posted to chaperonin groel by rph on 2008-12-16 01:13:51 as along with 1 person Ema
	Determination of Regions in the Dihydrofolate Reductase Structure That Interact with the Molecular Chaperonin GroEL† [My Copy] Biochemistry, Vol. 35, No. 18. (1 January 1996), pp. 5893-5901. by Clay A. Clark, Eric Hugo, Carl Frieden posted to chaperonin dhfr groel by rph on 2008-12-12 19:30:50 as
	Nanopore–Protein Interactions Dramatically Alter Stability and Yield of the Native State in Restricted Spaces [My Copy] Journal of Molecular Biology, Vol. 357, No. 2. (24 March 2006), pp. 632-643. by M. Cheung, D. Thirumalai posted to chaperonin coarse-grained confinement md simulation by cactus on 2008-10-07 08:39:21 as
	Variant tricarboxylic acid cycle in Mycobacterium tuberculosis : Identification of α-ketoglutarate decarboxylase [My Copy] Proceedings of the National Academy of Sciences of the United States of America, Vol. 102, No. 30. (26 July 2005), pp. 10670-10675. by Jing Tian, Ruslana Bryk, Manabu Itoh, Makoto Suematsu, Carl Nathan posted to acyl beta2 chaperonin eno1 pou by emissrto on 2008-09-03 17:03:28 as
	The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex [My Copy] Nature, Vol. 388, No. 6644. (1997), pp. 741-750. by Zhaohui Xu, Arthur L. Horwich, Paul B. Sigler posted to chaperonin structure by rph on 2008-08-10 20:16:38 as
	The Crystal Structure of a GroEL/Peptide Complex: Plasticity as a Basis for Substrate Diversity [My Copy] Cell, Vol. 99, No. 7. (23 December 1999), pp. 757-768. by Lingling Chen, Paul B. Sigler posted to chaperonin by rph on 2008-08-10 08:24:03 as
	CHAPERONIN-MEDIATED PROTEIN FOLDING [My Copy] Annual Review of Biophysics and Biomolecular Structure, Vol. 30, No. 1. (2001), pp. 245-269. by D. Thirumalai, George H. Lorimer posted to chaperonin folding review by rph on 2008-06-18 23:01:24 as
	Protein Folding in the Cell: The Role of Molecular Chaperones Hsp70 and Hsp60 [My Copy] Annual Review of Biophysics and Biomolecular Structure, Vol. 21, No. 1. (1992), pp. 293-322. by F. U. Hartl, J. Martin, W. Neupert posted to chaperonin folding review by rph on 2008-06-17 00:32:00 as
	A Thermophilic Mini-chaperonin Contains a Conserved Polypeptide-binding Surface: Combined Crystallographic and NMR Studies of the GroEL Apical Domain with Implications for Substrate Interactions, [My Copy] Journal of Molecular Biology, Vol. 306, No. 3. (23 February 2001), pp. 513-525. by Qing-Xin Hua, Irina S. Dementieva, Martin A. Walsh, Klaas Hallenga, Michael A. Weiss, Andrzej Joachimiak posted to chaperonin structure triple-resonance tthgroel by rph on 2008-06-15 02:38:52 as
	From the Cover: Direct NMR observation of a substrate protein bound to the chaperonin GroEL [My Copy] Proceedings of the National Academy of Sciences, Vol. 102, No. 36. (6 September 2005), pp. 12748-12753. by Reto Horst, Eric B. Bertelsen, Jocelyne Fiaux, Gerhard Wider, Arthur L. Horwich, Kurt Wuthrich posted to biggies chaperonin ms-14 relaxation by rph on 2008-06-12 03:39:34 as
	Rattling the cage: computational models of chaperonin-mediated protein folding [My Copy] Current Opinion in Structural Biology In Theory and simulation / Macromolecular assemblages, Vol. 18, No. 2. (April 2008), pp. 163-169. by Jeremy England, Del Lucent, Vijay Pande posted to chaperonin groel re review simulation by cactus on 2008-05-26 05:26:12 as
	Probing Dynamics and Conformational Change of the GroEL-GroES Complex by 13C NMR Spectroscopy [My Copy] The Journal of Biochemistry, Vol. 140, No. 4. (October 2006), pp. 591-598. by Nishida, Noritaka, Motojima, et al. Fumihiro, Idota, Mayu, Fujikawa, Hiroshi, Yoshida, Masasuke, Shimada, Ichio, Kato, Koichi posted to 13c biggies chaperonin dynamics groel by rph on 2008-05-22 18:50:57 as
	GroEL stimulates protein folding through forced unfolding [My Copy] Nature Structural & Molecular Biology, Vol. 15, No. 3. (02 March 2008), pp. 303-311. by Zong Lin, Damian Madan, Hays S. Rye posted to chaperonin experiment fret groel unfolding by cactus on 2008-04-02 10:22:14 as along with 3 people aalibes zwang hsekiguc
	Coupling between allosteric transitions in GroEL and assisted folding of a substrate protein [My Copy] PNAS, Vol. 104, No. 21. (22 May 2007), pp. 8803-8808. by George Stan, George H. Lorimer, D. Thirumalai, Bernard R. Brooks posted to chaperonin folding groel theory by rph on 2008-03-28 01:10:01 as along with 1 person cactus
	Structural rearrangements of the two domains of Azotobacter vinelandii rhodanese upon sulfane sulfur release: essential molecular dynamics, 15N NMR relaxation and deuterium exchange on the uniformly labeled protein [My Copy] International Journal of Biological Macromolecules, Vol. 33, No. 4-5. (December 2003), pp. 193-201. by Daniel O. Cicero, Sonia Melino, Maria Orsale, et al.Giuseppe Brancato, Andrea Amadei, Fabio Forlani, Silvia Pagani, Maurizio Paci posted to chaperonin nmr by rph on 2008-03-20 20:10:42 as
	NMR analysis of a 900K GroEL GroES complex. [My Copy] Nature, Vol. 418, No. 6894. (11 July 2002), pp. 207-211. by J. Fiaux, E. B. Bertelsen, A. L. Horwich, K. Wüthrich posted to chaperonin groel nmr by rph on 2008-03-20 18:59:30 as along with 3 people apaydin dgront MeganBarnett
	Crystal structure of the native chaperonin complex from Thermus thermophilus revealed unexpected asymmetry at the cis-cavity. [My Copy] Structure (Camb), Vol. 12, No. 8. (August 2004), pp. 1471-1480. by T. Shimamura, A. Koike-Takeshita, K. Yokoyama, et al.R. Masui, N. Murai, M. Yoshida, H. Taguchi, S. Iwata posted to chaperonin protein structure tthgroel by rph on 2008-03-19 04:16:46 as along with 1 person and 2 groups jwm Radiation_Damage Stressosome
	Solution NMR Techniques for Large Molecular and Supramolecular Structures [My Copy] J. Am. Chem. Soc., Vol. 124, No. 41. (16 October 2002), pp. 12144-12153. by R. Riek, J. Fiaux, E. B. Bertelsen, A. L. Horwich, K. Wuthrich posted to chaperonin groel methods ms-14 nmr by rph on 2008-03-14 21:23:39 as
	Managing the solvent water polarization to obtain improved NMR spectra of large molecular structures. [My Copy] J Biomol NMR, Vol. 32, No. 1. (May 2005), pp. 61-70. by S. Hiller, G. Wider, T. Etezady-Esfarjani, R. Horst, K. Wüthrich posted to chaperonin groel nmr paramagnetic by rph on 2008-03-11 00:05:37 as
	Topologies of a substrate protein bound to the chaperonin GroEL. [My Copy] Mol Cell, Vol. 26, No. 3. (11 May 2007), pp. 415-426. by N. Elad, G. W. Farr, D. K. Clare, E. V. Orlova, A. L. Horwich, H. R. Saibil posted to chaperonin groel by rph on 2008-03-10 17:37:57 as
	Mechanisms of protein folding. [My Copy] Curr Opin Struct Biol, Vol. 11, No. 1. (February 2001), pp. 70-82. by V. Grantcharova, E. J. Alm, D. Baker, A. L. Horwich posted to chaperonin folding protein by rph on 2008-03-07 18:49:18 as along with 3 people and 2 groups ana Einat leemary4 structural_bioinformatics Bioinformatics
	Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker. [My Copy] Mol Cell, Vol. 26, No. 1. (13 April 2007), pp. 27-39. by J. F. Swain, G. Dinler, R. Sivendran, D. L. Montgomery, M. Stotz, L. M. Gierasch posted to chaperonin folding by rph on 2008-02-28 22:19:07 as
	Folding trajectories of human dihydrofolate reductase inside the GroEL GroES chaperonin cavity and free in solution [My Copy] Proceedings of the National Academy of Sciences, Vol. 104, No. 52. (26 December 2007), pp. 20788-20792. by Reto Horst, Wayne A. Fenton, Walter S. Englander, Kurt Wuthrich, Arthur L. Horwich posted to chaperonin folding groel by rph on 2008-02-27 23:36:36 as along with 1 person cactus
	Tumorigenic Mutations in VHL Disrupt Folding In Vivo by Interfering with Chaperonin Binding [My Copy] Molecular Cell, Vol. 12, No. 5. (November 2003), pp. 1213-1224. by Douglas E. Feldman, Christoph Spiess, Daniel E. Howard, Judith Frydman posted to chaperonin tric tumor vhl by wduim on 2007-09-27 22:09:00 as
	Ordered nanoparticle arrays formed on engineered chaperonin protein templates [My Copy] Nat Mater, Vol. 1, No. 4. (December 2002), pp. 247-252. by Andrew R. Mcmillan, Chad D. Paavola, Jeanie Howard, Suzanne L. Chan, Nestor J. Zaluzec, Jonathan D. Trent posted to chaperonin dot quantum by wduim on 2007-08-07 20:07:03 as
	Identification of the TRiC/CCT Substrate Binding Sites Uncovers the Function of Subunit Diversity in Eukaryotic Chaperonins [My Copy] Molecular Cell, Vol. 24, No. 1. (6 October 2006), pp. 25-37. by Christoph Spiess, Erik J. Miller, Amie J. Mcclellan, Judith Frydman posted to chaperone chaperonin folding protein by erkjm76 on 2007-07-21 01:19:37 as
	$My PDF yifrach_95_nested.pdf$ Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL. [My Copy] Biochemistry, Vol. 34, No. 16. (25 April 1995), pp. 5303-5308. by O. Yifrach, A. Horovitz posted to chaperonin atpase by yanjiang to the group moernerlab on 2007-07-11 05:58:05 as along with 1 person anns39
	Structural Features of the GroEL-GroES Nano-Cage Required for Rapid Folding of Encapsulated Protein [My Copy] Cell, Vol. 125, No. 5. (2 June 2006), pp. 903-914. by Yun-Chi Tang, Hung-Chun Chang, Annette Roeben, et al.Dirk Wischnewski, Nadine Wischnewski, Michael J. Kerner, Ulrich F. Hartl, Manajit Hayer-Hartl posted to chaperonin cited clip confinement experiment groel by cactus on 2007-05-16 11:53:59 as along with 1 person rph

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groel	16
folding	10
experiment	7
protein	6
atpase	4
nmr	4
review	4
structure	4
allostery	3
confinement	3
plant	3
tthgroel	3
biggies	2
domain	2
gartmann	2
groes	2
md	2
metal-binding	2
ms-14	2
simulation	2
tric	2
13c	1
acyl	1
adp	1
aluminum-fluoride	1
atox1	1
beta2	1
bismuth	1
cct-gamma	1
chaperone	1
chaperones	1
cited	1
clip	1
coarse-grained	1
conformation	1
cooperativity	1
cpn10	1
cryo-em	1
cui	1
cysteine-rich	1
dhfr	1
dot	1
dynamics	1
em	1
eno1	1
exchange	1
fret	1
hdhfr	1
helicobacter	1
histidine-rich	1
hsp10	1
hspa	1
methods	1
nickel	1
no-tectal-neuron	1
paramagnetic	1
pou	1
pylori	1
quantum	1
re	1
relaxation	1
retina	1
retinotectal	1
theory	1
thermosome	1
triple-resonance	1
tumor	1
unfolding	1
vhl	1
wd_repeat	1
zebrafish	1

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