Results 41 to 50 of about 753,077 (248)

Trehalose improves cell proliferation and dehydration tolerance of human HaCaT cells [PDF]

Archives of Biological Sciences, 2015
Trehalose is a disaccharide molecule that serves as a natural osmotic regulator in halophilic microorganisms and plants but not in mammals. We observed that human HaCaT cells supplied with trehalose improved cell proliferation and extended ...
Lee Kyung Eun, Moon Doo Hwan, Kang Sang Gu   +2 more
doaj   +1 more source

Human plasma kininogens are identical with α-cysteine proteinase inhibitors Evidence from immunological, enzymological and sequence data [PDF]

, 1985
Human high- and low-Mr kininogens were shown to be potent inhibitors of cysteine proteinases such as cathepsin L and papain (Ki = 17–48 pM). A strong immunological cross-reaction between the kininogens and low-Mr α-cysteine proteinase inhibitor from ...
Lottspeich, Friedrich, Joze Brzin, Kotnik, Matjaz, Werner Machleidt, Matjaz Kotnik, Friedrich Lottspeich, Ritonja, Anka, Werner Müller-Esterl, Vito Turk, Hans Fritz, Kellermann, Josef, Machleidt, Werner, Müller-Esterl, Werner, Brzin, Joze, Josef Kellermann, Fritz, Hans, Turk, Vito, Anka Ritonja   +17 more
core   +1 more source

Autophagy and mitophagy in pancreatic β‐cell homeostasis and their involvement in diabetes pathophysiology

FEBS Letters, EarlyView.
This review focuses on the role of autophagy and mitophagy in maintaining pancreatic β‐cell function and homeostasis. We discuss how genetic defects affecting these pathways contribute to the development of type 1, type 2, monogenic, and gestational diabetes. We further explore their potential as therapeutic targets. Created in BioRender.
Yunkyeong Lee, Mingming Tong, Anna L. Gloyn   +2 more
wiley   +1 more source

LCTX-F2, a Novel Potentiator of Coagulation Factors From the Spider Venom of Lycosa singoriensis

Frontiers in Pharmacology, 2020
Spider venoms contain many functional proteins/peptides such as proteinases, serine/cysteine proteinase inhibitors, insecticidal toxins, and ion channel toxins.
Pengpeng Li, Zhongzhe Zhang, Qiong Liao, Er Meng, James Mwangi, Ren Lai, Mingqiang Rong   +6 more
doaj   +1 more source

Toll-like receptor 4 and Syk kinase shape dendritic cell-induced immune activation to major house dust mite allergens

Frontiers in Medicine, 2023
BackgroundHouse dust mite (HDM) is a major cause of respiratory allergic diseases. Dendritic cells (DCs) play a central role in orchestrating adaptive allergic immune responses. However, it remains unclear how DCs become activated by HDM.
Stefanie Busold, Stefanie Busold, Jaap H. Akkerdaas, Jaap H. Akkerdaas, Esther M. Zijlstra-Willems, Esther M. Zijlstra-Willems, Kees van der Graaf, Sander W. Tas, Sander W. Tas, Sander W. Tas, Esther C. de Jong, Esther C. de Jong, Ronald van Ree, Ronald van Ree, Ronald van Ree, Teunis B. H. Geijtenbeek, Teunis B. H. Geijtenbeek   +16 more
doaj   +1 more source

Translophagy—A potential link between autophagy impairment and translational errors

FEBS Letters, EarlyView.
Neurodegenerative diseases are characterised by the accumulation of abnormal proteins and protein aggregates, but their origin often remains unknown. We propose that selective autophagy removes damaged protein‐making machinery, preventing errors during protein synthesis.
Mykola V. Korolchuk, Gailing Ma, Robin Antrobus, Diego Manni, Marco Trevisan‐Herraz, Mustafa Khwaja, Max Brown, Gavin D. Richardson, Masaaki Komatsu, Daniel Erskine, Viktor I. Korolchuk, Tetsushi Kataura   +11 more
wiley   +1 more source

Pictolysin-III, a Hemorrhagic Type-III Metalloproteinase Isolated from Bothrops pictus (Serpentes: Viperidae) Venom, Reduces Mitochondrial Respiration and Induces Cytokine Secretion in Epithelial and Stromal Cell Lines

Pharmaceutics, 2023
From the venom of the Bothrops pictus snake, an endemic species from Peru, we recently have described toxins that inhibited platelet aggregation and cancer cell migration.
Dan E. Vivas-Ruiz, Paola Rosas, Alex Proleón, Daniel Torrejón, Fanny Lazo, Ana Belén Tenorio-Ricca, Francisco Guajardo, Cristopher Almarza, Víctor Andrades, Jessica Astorga, Daniel Oropesa, Jorge Toledo, María Jesús Vera, Jorge Martínez, Ramiro Araya-Maturana, Karen Dubois-Camacho, Marcela A. Hermoso, Valéria G. Alvarenga, Eladio Flores Sanchez, Armando Yarlequé, Luciana Souza Oliveira, Félix A. Urra   +21 more
doaj   +1 more source

The Shewanella oneidensis Fic enzyme SoFic targets the switch‐I region of EF‐Tu for AMPylation

FEBS Letters, EarlyView.
Fic enzymes mediate diverse post‐translational modifications across all domains of life, including AMPylation. Prokaryotic EF‐Tu can be AMPylated and deAMPylated by the conserved Fic enzyme SoFic. Structural and biochemical approaches were used to characterize the effect of AMPylation on EF‐Tu, SoFic's enzymatic activities, and the enzyme‐target ...
Svenja Runge, Vivian Pogenberg, Alexander Baumgart, Bente Siebels, Hartmut Schlüter, Michael Hecht‐Bucher, Aymelt Itzen   +6 more
wiley   +1 more source

SPINK7 Recognizes Fungi and Initiates Hemocyte-Mediated Immune Defense Against Fungal Infections

Frontiers in Immunology, 2021
Serine protease inhibitors of Kazal-type (SPINKs) were widely identified in vertebrates and invertebrates, and played regulatory roles in digestion, coagulation, and fibrinolysis.
Zhaoming Dong, Zhaoming Dong, Zhaoming Dong, Lingna An, Lingna An, Lingna An, Mengyao Lu, Mengyao Lu, Mengyao Lu, Muya Tang, Muya Tang, Muya Tang, Haiqin Chen, Haiqin Chen, Haiqin Chen, Xuan Huang, Xuan Huang, Xuan Huang, Yong Hou, Yong Hou, Yong Hou, Guanwang Shen, Guanwang Shen, Guanwang Shen, Xiaolu Zhang, Xiaolu Zhang, Xiaolu Zhang, Yan Zhang, Yan Zhang, Yan Zhang, Qingyou Xia, Qingyou Xia, Qingyou Xia, Ping Zhao, Ping Zhao, Ping Zhao   +35 more
doaj   +1 more source

An inflammatory role for the mammalian carboxypeptidase inhibitor latexin: Relationship to cystatins and the tumor suppressor TIG1 [PDF]

, 2005
Latexin, the only known mammalian carboxypeptidase inhibitor, has no detectable sequence similarity with plant and parasite inhibitors, but it is related to a human putative tumor suppressor protein, TIG1.
Listwan, P., Flanagan, Jack U., Flanagan, JU, Martin, Jennifer L, Listwan, P, Wells, Christine A, Kobe, Bostjan, Hume, DA, Cowieson, Nathan, Martin, Jennifer L., Hume, D A, Ravasi, T., Listwan, Pawel, Kellie, S, Kobe, B., Martin, Jennifer Louise, Cowieson, N. P., Martin, J. L., Huber, T, Huber, Thomas, Aagaard, A, Kobe, B, Flanagan, J. U., Ravasi, Timothy, Aagaard, A., A. Wells, Christine, Wells, C. A., Wells, Christine A., Aagaard, Anna, Wells, Christine, Flanagan, Jack U, Cowieson, N, Kellie, S., Huber, T. L., Hume, David A, Hume, D. A., Kellie, Stuart, Ravasi, T, Hume, David A., Wells, CA, Martin, JL   +40 more
core   +1 more source