نتایج جستجو برای: heat shock protein 60 kda

تعداد نتایج: 1748885  

2003
J. A. Lockwood

In vivo protein expression in the abdominal viscera of C. v. slmorensis was examined from aduh flies that were cold shocked for various lengths of time at O, 10, or 15°C and labelled at 25°C with 35S-methionine at 0, 2, 4 and 6 hr during the recovery period. In vitro labelling showed that seven unique proteins (23, 40, 43, 48, 60, 70 and 92 kDa) were produced in C. v. sonorensis exposed to low ...

2017
Yuki Miyamoto Tomohiro Torii Kazuko Kawahara Nanami Hasegawa Akito Tanoue Yoichi Seki Takako Morimoto Megumi Funakoshi-Tago Hiroomi Tamura Keiichi Homma Masahiro Yamamoto Junji Yamauchi

Hypomyelinating leukodystrophy (HLD) is genetic demyelinating or dysmyelinating disease and is associated with at least 13 responsible genes. The mutations seem likely cause the functional deficiency of their gene products. HLD4- and HLD5-associated HSPD1 and FAM126A mutations affect biochemical properties of the gene products (Miyamoto et al. (2015,2014) [[1], [2]]). Herein we provide the data...

Journal: :FEMS microbiology letters 1991
P Hindersson N Høiby J Bangsborg

A 2.7 kb DNA fragment encoding the 60 kDa common antigen (CA) and a 13 kDa protein of Legionella micdadei was sequenced. Two open reading frames of 57,677 and 10,456 Da were identified, corresponding to the heat shock proteins GroEL and GroES, respectively. Typical -35, -10, and Shine-Dalgarno heat shock expression signals were identified upstream of the L. micdadei groEL gene. Further upstream...

Journal: :Infection and immunity 1990
P S Hoffman L Houston C A Butler

A 60-kilodalton (kDa) immunodominant antigen of Legionella pneumophila is a heat shock protein (HSP) of the GroEL class of HSPs. The gene (htpB) coding the 60-kDa protein was localized to a 3.2-kilobase DNA fragment of L. pneumophila cloned into pUC19 (pSH16) (P. S. Hoffman, C. A. Butler, and F. D. Quinn, Infect. Immun. 57:1731-1739, 1989). The nucleotide sequence of the DNA fragment cloned int...

Journal: :The Journal of comparative neurology 1998
R A Sheller M E Smyers R M Grossfeld M L Ballinger G D Bittner

To characterize heat-shock proteins (HSPs) of the 70-kDa family in the crayfish medial giant axon (MGA), we analyzed axoplasmic proteins separately from proteins of the glial sheath. Several different molecular weight isoforms of constitutive HSP 70s that were detected on immunoblots were approximately 1-3% of the total protein in the axoplasm of MGAs. To investigate inducible HSPs, MGAs were h...

Journal: :FEMS microbiology letters 1998
L M Mutharia J Klinck H Yamaguchi M Davey

Vibrio anguillarum strains expressed increased amounts of a novel 60-kDa protein when cells were grown at physiologically elevated temperatures. The relative amounts of the 60-kDa protein were unaltered by changes in osmolarity or ionic concentration of the growth medium in cells grown at optimal growth temperatures. The N-terminal amino acid sequence analysis of the V. anguillarum 60-kDa prote...

2001
J. Welch

We describe the biochemical characterization and purification of the small 28,000-dalton heat shock protein (28-kDa protein) of mammalian cells. Metabolic pulse labeling of heat shock-treated cells with either [3H]leucine or HaS2P04 and analysis of the labeled proteins by two-dimensional gel electrophoresis revealed increased levels of three 28-kDa proteins differing only in their relative isoe...

Journal: :Arthritis Research & Therapy 2009
Yvonne Vercoulen Nienke H van Teijlingen Ismé M de Kleer Sylvia Kamphuis Salvatore Albani Berent J Prakken

Juvenile idiopathic arthritis (JIA) is a disease characterized by chronic joint inflammation, caused by a deregulated immune response. In patients with JIA, heat shock proteins (HSPs) are highly expressed in the synovial lining tissues of inflamed joints. HSPs are endogenous proteins that are expressed upon cellular stress and are able to modulate immune responses. In this review, we concentrat...

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