Results 181 to 190 of about 11,541 (227)

Identification of genetic variations linked to buparvaquone resistance in Theileria annulata infecting dairy cattle in India. [PDF]

PLoS One
Musale P, Khilari A, Gade R, Dhanikachalam V, Jadhav S, Bajpai M, Turakani B, Joshi A, Prajapati A, Srivastava A, Swaminathan M, Joshi S, Shanmugam D.   +12 more
europepmc   +1 more source

MAKR6 integrates TMK and CAMEL/CANAR signalling for auxin canalization in Arabidopsis

Ge Z, Koczka L, Mazur E, Molnar G, Vladimirtsev D, Kassem N, Ikene SA, Fiedler L, Friml J.   +8 more
europepmc   +1 more source

FragmentScope - exploring the fragment space with learned surface representations

Elizarova E, Morozova I, Igashov I, Gampp O, Pavel Iosub DR, Schneuing A, Lau K, Ferraris D, Pojer F, Riek R, Bronstein M, Correia BE.   +11 more
europepmc   +1 more source

Evidence for sexual antagonism and antagonistic pleiotropy in the maintenance of late onset Alzheimer’s disease alleles

Morrow EH, Harper JA.
europepmc   +1 more source

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Pin1 and Alzheimer's disease

Translational Research, 2023
Alzheimer's disease (AD) is an immense and growing public health crisis. Despite over 100 years of investigation, the etiology remains elusive and therapy ineffective. Despite current gaps in knowledge, recent studies have identified dysfunction or loss-of-function of Pin1, a unique cis-trans peptidyl prolyl isomerase, as an important step in AD ...
openaire   +2 more sources

Pin1 as an anticancer drug target

Drug News & Perspectives, 2009
Pin1 specifically catalyzes the cis/trans isomerization of phospho-Ser/Thr-Pro bonds and plays an important role in many cellular events through the effects of conformational change on the function of its biological substrates, including cell division cycle 25 C (Cdc25C), c-Jun and p53.
Guoyan G, Xu, Felicia A, Etzkorn
openaire   +2 more sources

PIN1, the cell cycle and cancer

Nature Reviews Cancer, 2007
PIN1 is a peptidyl-prolyl isomerase that can alter the conformation of phosphoproteins and so affect protein function and/or stability. PIN1 regulates a number of proteins important for cell-cycle progression and, based on gain- and loss-of-function studies, is presumed to operate as a molecular timer of this important process.
Elizabeth S, Yeh, Anthony R, Means
openaire   +2 more sources

Mammalian Pin1

1997
Abstract Pinl, a human protein interacting with the mitotic NIMA kinase isolated from Aspergillus nidulans, contains a catalytic domain characteristic of the highly conserved third family of peptidyl-prolyl cis-trans isomerases that are distinct from either the cyclophilins or the FK506-binding proteins. Pinl is a widely expressed 18 kDa
K P Lu, T Hunter
openaire   +1 more source

Pin1: A New Outlook in Alzheimers Disease

Current Alzheimer Research, 2011
Neurodegenerative diseases termed Tauopathies, including Alzheimer disease, are characterized by the presence of intraneuronal neurofibrillary tangles (NFTs), composed by hyperphosphorylated protein Tau. Peptidyl-prolyl cis/trans isomerase Pin1 plays a pivotal role in the regulation of Tau phosphorylation/dephosphorylation state.
LONATI, ELENA RITA, MASSERINI, MASSIMO ERNESTO, BULBARELLI, ALESSANDRA   +2 more
openaire   +3 more sources

Pin1 and Nuclear Receptors: A New Language?

Journal of Cellular Physiology, 2013
AbstractPin1 is a unique enzyme that can isomerize specific phospho‐Ser/Thr‐Pro peptide bonds, inducing a conformational change in the target protein. Such activity represents a novel and tightly controlled signaling mechanism regulating a spectrum of protein functions during the normal physiology of the cell and in pathological conditions.
La Montagna, Raffaele, Caligiuri, Isabella, Giordano, Antonio, RIZZOLIO, Flavio   +3 more
openaire   +4 more sources