Results 91 to 100 of about 147,841 (291)
Altered Function of the DnaJ Family Cochaperone DNJ-17 Modulates Locomotor Circuit Activity in a Caenorhabditis elegans Seizure Model. [PDF]
The highly conserved cochaperone DnaJ/Hsp40 family proteins are known to interact with molecular chaperone Hsp70, and can regulate many cellular processes including protein folding, translocation, and degradation.
Jin, Yishi, Takayanagi-Kiya, Seika
core +2 more sources
Targeting Lactate and Lactylation in Cancer Metabolism and Immunotherapy
Lactate, once deemed a metabolic waste, emerges as a central regulator of cancer progression. This review elucidates how lactate and its epigenetic derivative, protein lactylation, orchestrate tumor metabolism, immune suppression, and therapeutic resistance.
Jiajing Gong +5 more
wiley +1 more source
Chaperone driven polymer translocation through Nanopore: spatial distribution and binding energy
Chaperones are binding proteins which work as a driving force to bias the biopolymer translocation by binding to it near the pore and preventing its backsliding. Chaperones may have different spatial distribution. Recently we show the importance of their
Abdolvahab, Rouhollah Haji
core +1 more source
The SseC translocon component in Salmonella enterica serovar Typhimurium is chaperoned by SscA [PDF]
Background: Salmonella enterica is a causative agent of foodborne gastroenteritis and the systemic disease known as typhoid fever. This bacterium uses two type three secretion systems (T3SSs) to translocate protein effectors into host cells to manipulate
Allison, Sarah E +4 more
core +1 more source
The butterfly unfolded wing in an open form structure of botulinum neurotoxin type A (BoNT/A) at physiological‐state was confirmed at 2.85 Å resolution by cryo‐electron microscopy (cryo‐EM). Structure‐guided protein engineering significantly enhanced the receptor‐binding affinity, therapeutic efficacy, and safety of the engineered toxin variants ...
Wenrui Wang +16 more
wiley +1 more source
The Chaperonopathies - Diseases with Defective Molecular Chaperones
In the mid 1950's the Nobel Prize Laureate Christian B. Anfinsen from his research on the folding of ribonuclease A, began to concentrate on the problem of the relationship between structure and function in enzymes.
Giovanni Li Volti
doaj +1 more source
Wrapping the alpha-crystallin domain fold in a chaperone assembly [PDF]
Small heat shock proteins (sHsps) are oligomers that perform a protective function by binding denatured proteins. Although ubiquitous, they are of variable sequence except for a C-terminal similar to 90-residue "alpha-crystallin domain".
Basha +57 more
core +1 more source
ABSTRACT Triple‐negative breast cancer (TNBC) exhibits addiction to chronic endoplasmic reticulum (ER) stress, which sustains an aggressive metastatic phenotype through activation of the unfolded protein response (UPR). Here, we identify a previously unrecognized “ER‐stress addiction” axis in which the Hippo pathway effector TEAD4 directly ...
Yini Shang +9 more
wiley +1 more source
Metallochaperones regulate intracellular copper levels. [PDF]
Copper (Cu) is an important enzyme co-factor that is also extremely toxic at high intracellular concentrations, making active efflux mechanisms essential for preventing Cu accumulation. Here, we have investigated the mechanistic role of metallochaperones
Adams, Michael +9 more
core +1 more source
In the present study, we have demonstrated that the NUP85‐USP47‐ASK1 signaling pathway may have regulated the progression of liver fibrosis through modulating ERS. Additionally, we have developed a CREKA‐coupled liposome to target delivery of MV, a pharmacological inhibitor of NUP85, to activated HSCs, thereby attenuating liver fibrosis. ABSTRACT Liver
Dashuai Yang +11 more
wiley +1 more source

