Results 71 to 80 of about 21,272 (221)

Proteomic signatures of equine dental tooth tissues in ageing and disease

Equine Veterinary Journal, Volume 58, Issue 6, Page 1552-1569, November 2026.
Abstract Background Ageing and dental disease in horses lead to structural and functional deterioration of dental tissues, yet their molecular signatures remain poorly characterised. Understanding how these processes alter the protein composition of enamel, dentin, cementum and pulp is essential for improving equine oral health and identifying ...
Anders Jensen, Danae Emilie Zambouli, Iris Gringel, Zoe Nugent, Kazuhiro Yamamoto, Lee Cooper, Andrew J. Peffers, Guido Rocchigiani, Mandy J. Peffers   +8 more
wiley   +1 more source

Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin. [PDF]

, 1998
We describe the discovery of a heterohexameric chaperone protein, prefoldin, based on its ability to capture unfolded actin. Prefoldin binds specifically to cytosolic chaperonin (c-cpn) and transfers target proteins to it. Deletion of the gene encoding a
Lewis, Sally A, LEWIS, SA, Klein, Hannah L, ROMMELAERE, H, KLEIN, HL, Vandekerckhove, Joël, COWAN, NJ, VAINBERG, IE, Rommelaere, Heidi, Vainberg, Irina E, Cowan, Nicholas J, Ampe, Christophe   +11 more
core   +1 more source

The Cpn10(1) co-chaperonin of A. thaliana functions only as a hetero-oligomer with Cpn20. [PDF]

PLoS ONE, 2014
The A. thaliana genome encodes five co-chaperonin homologs, three of which are destined to the chloroplast. Two of the proteins, Cpn10(2) and Cpn20, form functional homo-oligomers in vitro.
Anna Vitlin Gruber, Gal Zizelski, Abdussalam Azem, Celeste Weiss   +3 more
doaj   +1 more source

PolyG Fibrils Coalesce Into Nuclear Ribbons That Engage Proteostasis Machinery in Neuronal Intranuclear Inclusion Disease

Advanced Science, Volume 13, Issue 56, 9 October 2026.
In NIID, expanded NOTCH2NLC repeats give rise to nuclear polyG inclusions. Tracer‐guided in situ cryo‐electron tomography enables cross‐scale structural analysis from mouse brain to native neuronal nuclei, revealing dense‐core/peripheral‐halo inclusions built from compact polyG ribbons.
Hui Dong, Yongcheng Pan, Zhiyao Tang, Yuxuan Yao, Guicong Zhang, Junpu Wang, Haonan Xiao, Yun Tian, Beisha Tang, Dan Li, Qiang Guo, Ruijun Tian, Qiong Liu, Cong Liu   +13 more
wiley   +1 more source

Ordered biological nanostructures formed from chaperonin polypeptides [PDF]

, 2010
The following application relates to nanotemplates, nanostructures, nanoarrays and nanodevices formed from wild-type and mutated chaperonin polypeptides, methods of producing such compositions, methods of using such compositions and particular chaperonin
Trent, Jonathan D., Paavola, Chad D., McMillan, R. Andrew, Kagawa, Hiromi   +3 more
core  

Streamlining Diagnosis of Bardet–Biedl Syndrome: New Diagnostic Algorithm With Updated Criteria

American Journal of Medical Genetics Part A, Volume 200, Issue 10, Page 2181-2198, October 2026.
ABSTRACT Considerable advances have been made in our understanding of Bardet–Biedl syndrome (BBS), particularly in its core clinical features and molecular genetics, warranting an update to the existing diagnostic criteria framework. Using a rigorous, evidence‐based, and consensus‐driven process, a multidisciplinary group of international experts and ...
Jeremy J. Pomeroy, Jesse Richards, Brooke R. Sweeney, Seema Kumar, Katie E. Queen, Joshua Zaritsky, Carl H. Cramer, Elias I. Traboulsi, Brittni A. Scruggs, Erica E. Davis, Ekaterina Keifer, Emma McGibbon, Timothy Ogden, Bendert De Graaf, Tonia Hymers, Elizabeth Forsythe, Philip Beales   +16 more
wiley   +1 more source

Facilitated release of substrate protein from prefoldin by chaperonin [PDF]

, 2005
Prefoldin is a chaperone that captures a protein-folding intermediate and transfers it to the group II chaperonin for correct folding. However, kinetics of interactions between prefoldin and substrate proteins have not been investigated.
Masafumi Yohda, Taro Ueno, Tadakuma, Hisashi, Tamotsu Zako, Okochi, Mina, Yohda, Masafumi, Ryo Iizuka, Mina Okochi, Zako, Tamotsu, Ueno, Taro, Takashi Funatsu, Iizuka, Ryo, Nomura, Tomoko, Funatsu, Takashi, Tomoko Nomura, Hisashi Tadakuma   +15 more
core   +1 more source

Bardet–Biedl Syndrome Presenting With Acute Kidney Injury Revealing Previously Undiagnosed Advanced Chronic Kidney Disease in a Young Adult: A Case Report

Clinical Case Reports, Volume 14, Issue 10, October 2026.
ABSTRACT Bardet–Biedl syndrome (BBS) is an autosomal recessive disorder characterized by obesity, rod‐cone dystrophy, polydactyly, developmental delay, renal dysfunction, and genitourinary abnormalities. We report the case of a 27‐year‐old female with previously undiagnosed BBS who presented with acute kidney injury precipitated by acute ...
Aqeel Abbas, Nouman Amjad, Amna Faheem Mufti, Muhammad Waqas, Minahil Iqbal, Hamza Ali, Amir Habib, Yahya Samadi, Muhammad Usman Haider   +8 more
wiley   +1 more source

Ordered Nanostructures Made Using Chaperonin Polypeptides [PDF]

, 2004
A recently invented method of fabricating periodic or otherwise ordered nanostructures involves the use of chaperonin polypeptides. The method is intended to serve as a potentially superior and less expensive alternative to conventional lithographic ...
Paavola, Chad, Mogul, Rakesh, McMillan, Robert, Trent, Jonathan, Kagawa, Hiromi   +4 more
core  

Inhibition of chaperonin ATPase activity by various co-chaperonins.

, 2012
Steady-state ATPase activity was measured for each chaperonin. The T.O.N values (1/min) were 3.27±0.32, 0.83±0.14, 0.91±0.1 and 0.79±0.08 for GroEL, mHsp60, E321K and R264K/E358K, respectively. The percentage of ATPase inhibition by each co-chaperonin is
Galit Levy-Rimler (115146), Shahar Nisemblat (104049), Celeste Weiss (104056), Amir Pri-Or (115148), Peter A. Lund (115152), Peter Bross (115155), Abdussalam Azem (17943), Avital Parnas (104053), Tsaffrir Zor (115150)   +8 more
core   +1 more source