Results 111 to 120 of about 29,175 (219)

A novel homozygous mutation of the AIRE gene in an APECED patient from Pakistan: case report and review of the literature [PDF]

, 2018
Autoimmune-poly-endocrinopathy-candidiasis-ectodermal-dystrophy syndrome (APECED) is a rare monogenic recessive disorder caused by mutations in the autoimmune regulator (AIRE) gene.
Bellacchio, Emanuele, Betterle, Corrado, Dhamo, Rudina, Fierabracci, Alessandra, Frasca, Federica, Pellegrino, Marsha   +5 more
core   +2 more sources

Prenylcysteine Oxidase 1 Deficiency Protects the Cardiac Muscle Cell Line HL‐1 Against Ischaemic/Hypoxic Stress

The FASEB Journal, Volume 40, Issue 8, 30 April 2026.
Ischaemic/hypoxic stress leads to heart remodeling and dysfunction. PCYOX1 promotes cardiomyocyte survival during injury, reducing the generation of reactive oxygen species. PCYOX1 deficiency regulates key proteins to preserve cardiomyocyte structure and function such as creatine kinase.
Cristina Banfi, Lisa Brocca, Alice Bascucci, Giulia Giusy Papaianni, Alice Mallia, Sonia Eligini   +5 more
wiley   +1 more source

Structural basis of nuclear import of flap endonuclease 1 (FEN1) [PDF]

, 2012
Flap endonuclease 1 (FEN1) is a member of the nuclease family and is structurally conserved from bacteriophages to humans. This protein is involved in multiple DNA-processing pathways, including Okazaki fragment maturation, stalled replication-fork ...
Agnes A. S. Takeda, Andrea C. de Barros, Bertinato, Boštjan Kobe, Catimel, Chelsky, Chen, Chiung-Wen Chang, Colledge, Conti, Cutress, Dingwall, Efthymiadis, Emsley, Fontes, Fontes, Fontes, Görlich, Hodel, Hosfield, Hu, Hwang, Hübner, Knudsen, Kobe, Koike, Koike, Kosugi, Kosugi, Laskowski, Lott, Marcos R. M. Fontes, Marfori, Mase, Miyamoto, Murshudov, Otwinowski, Qiu, Rexach, Sakurai, Studier, Takeda, Teh, Tsutakawa, Wallace, Yang, Zheng   +46 more
core   +2 more sources

Karyopherins regulate nuclear pore complex barrier and transport function [PDF]

, 2017
Nucleocytoplasmic transport is sustained by karyopherins (Kaps) and a Ran guanosine triphosphate (RanGTP) gradient that imports nuclear localization signal (NLS)–specific cargoes (NLS-cargoes) into the nucleus.
Adam, Allen, Bayliss, Bednenko, Ben-Efraim, Binlu Huang, Bischoff, Catimel, Chaillan-Huntington, Chantal Rencurel, Chook, Christie, Cingolani, Cingolani, Conti, Delphin, Eibauer, Eisele, Falces, Floer, Forwood, Forwood, Frey, Fukuhara, Grünwald, Görlich, Görlich, Görlich, Görlich, Hahn, Halder, Hough, Isgro, Kapinos, Kau, Kimura, Kopito, Kubitscheck, Kutay, Kutay, Larisa E. Kapinos, Lee, Lee, Lim, Lim, Lolodi, Lonhienne, Lowe, Lyman, Makise, Milles, Moroianu, Moroianu, Nigg, Ogawa, Paradise, Popken, Pumroy, Pyhtila, Rexach, Ribbeck, Riddick, Roderick Y.H. Lim, Rout, Sakiyama, Schoch, Stewart, Strawn, Sun, Tauchert, Timney, Tokunaga, Tu, von Appen, Vovk, Wagner, Weis, Yamada, Yang, Yang, Yoshimura, Zachariae   +81 more
core   +1 more source

Putting things in place for fertilization: discovering roles for importin proteins in cell fate and spermatogenesis

Asian Journal of Andrology, 2015
Importin proteins were originally characterized for their central role in protein transport through the nuclear pores, the only intracellular entry to the nucleus.
Kate L. Loveland, Andrew T. Major, Romaly Butler, Julia C. Young, David A. Jans, Yoichi Miyamoto   +5 more
doaj   +1 more source

Ciliary entry of the kinesin-2 motor KIF17 is regulated by importin-beta2 and RanGTP [PDF]

, 2010
The biogenesis, maintenance, and function of primary cilia are controlled through intraflagellar transport (IFT) driven by two kinesin-2 family members, the heterotrimeric KIF3A/KIF3B/KAP complex and the homodimeric KIF17 motor1,2.
Dishinger, John F, Fan, Shuling, Hammond, Jennetta W, Hurd, Toby W, Jenkins, Paul M, Kee, Hooi Lynn, Margolis, Ben, Martens, Jeffrey R, Truong, Yen Nhu-Thi, Verhey, Kristen J   +9 more
core   +2 more sources

Nuclear importin α and its physiological importance

Communicative & Integrative Biology, 2012
Importin α is recognized as a classical nuclear localization signal (cNLS) receptor which mediates nucleocytoplasmic transport. However, it rapidly accumulates in the nucleus in response to cellular stresses, including oxidative stress, causing a blockade of the classical nuclear import pathway. We set out to determine whether importin α performs roles
Miyamoto, Yoichi, Loveland, Kate L., Yoneda, Yoshihiro   +2 more
openaire   +2 more sources

Novel localization of formin mDia2: importin β-mediated delivery to and retention at the cytoplasmic side of the nuclear envelope

Biology Open, 2015
The formin family proteins are important regulators of actin polymerization that are involved in many cellular processes. However, little is known about their specific cellular localizations.
Xiaowei Shao, Keiko Kawauchi, G. V. Shivashankar, Alexander D. Bershadsky   +3 more
doaj   +1 more source

Importin α-importin β complex mediated nuclear translocation of insulin-like growth factor binding protein-5

Endocrine Journal, 2017
Insulin-like growth factor-binding protein (IGFBP)-5 is a secreted protein that binds to IGFs and modulates IGF actions, as well as regulates cell proliferation, migration, and apoptosis independent of IGF. Proper cellular localization is critical for the effective function of most signaling molecules.
Min, Sun, Juan, Long, Yuxin, Yi, Wei, Xia   +3 more
openaire   +3 more sources

The adapter importin‐α provides flexible control of nuclear import at the expense of efficiency

Molecular Systems Biology, 2007
Although there exists a large family of nuclear transport receptors (Karyopherins), the majority of known import cargoes use an adapter protein, Importin‐α (Impα), which links the cargo to a karyopherin, Importin‐β (Impβ). The reason for the existence of
Greg Riddick, Ian G Macara
doaj   +1 more source