Results 71 to 80 of about 7,003 (228)

Combinatorial effects of eliminating HS epimerase and O-sulfotransferases for neural migration. [PDF]

, 2014
(A) Removal of HS 3- and 6-O-sulfotransferases enhances the defects in HS epimerase mutants. C. elegans with genetic deletion in either hst-3.1 or hst-6 or in combination of both have wild type HSN migration.
Tarja K. Kinnunen (602998)
core   +1 more source

Structural and chemical profiling of the human cytosolic sulfotransferases.

PLoS Biology, 2007
The human cytosolic sulfotransfases (hSULTs) comprise a family of 12 phase II enzymes involved in the metabolism of drugs and hormones, the bioactivation of carcinogens, and the detoxification of xenobiotics.
Abdellah Allali-Hassani, Patricia W Pan, Ludmila Dombrovski, Rafael Najmanovich, Wolfram Tempel, Aiping Dong, Peter Loppnau, Fernando Martin, Janet Thornton, Aled M Edwards, Alexey Bochkarev, Alexander N Plotnikov, Masoud Vedadi, Cheryl H Arrowsmith   +13 more
doaj   +1 more source

3-O-sulfated heparan sulfate recognized by the antibody HS4C3 contributes [corrected] to the differentiation of mouse embryonic stem cells via fas signaling.

PLoS ONE, 2012
Maintenance of self-renewal and pluripotency in mouse embryonic stem cells (mESCs) is regulated by the balance between several extrinsic signaling pathways.
Kazumi Hirano, Norihiko Sasaki, Tomomi Ichimiya, Taichi Miura, Toin H Van Kuppevelt, Shoko Nishihara   +5 more
doaj   +1 more source

Heparan sulfate and glycomimetics: Advances in synthesis and biological applications for post‐stroke neurorepair

Neuroprotection, EarlyView.
ECM, extracellular matrix; BDNF, brain‐derived neuroptrophic factor; FGF, fibroblast growth factor; VEGF, vascular endothelial growth factor. Abstract Heparan sulfate, a structurally diverse glycosaminoglycan that is abundant in the central nervous system (CNS), orchestrates essential processes fundamental to neural plasticity, neurorepair, and ...
Mozammel H. Bhuiyan, Madeleine J. Smith, Simon F. R. Hinkley, Andrew N. Clarkson   +3 more
wiley   +1 more source

Human sulfotransferases and their role in chemical metabolism [PDF]

, 2005
Sulfonation is an important reaction in the metabolism of numerous xenobiotics, drugs, and endogenous compounds. A supergene family of enzymes called sulfotransferases (SULTs) catalyze this reaction. In most cases, the addition of a sulfonate moiety to a
McManus, M. E., Windmill, KF, Martin, Jennifer L., Windmill, Kelly F., Amanda Barnett, Nadine Hempel, Gamage, N., Martin, J. L., Windmill, K. F., Hempel, N., Gamage, N, Gamage, Niranjali, Niranjali Gamage, Hempel, Nadine, Duggleby, RG, Barnett, A, Duggleby, R. G., Kelly F. Windmill, Barnett, A., McManus, Michael E., Duggleby, Ronald G., Hempel, N, Jennifer L. Martin, Barnett, Amanda, Michael E. McManus, McManus, ME, Ronald G. Duggleby, Martin, JL   +27 more
core   +1 more source

The molecular basis for the broad substrate specificity of human sulfotransferase 1A1. [PDF]

PLoS ONE, 2011
Cytosolic sulfotransferases (SULTs) are mammalian enzymes that detoxify a wide variety of chemicals through the addition of a sulfate group. Despite extensive research, the molecular basis for the broad specificity of SULTs is still not understood. Here,
Ilana Berger, Chen Guttman, Dotan Amar, Raz Zarivach, Amir Aharoni   +4 more
doaj   +1 more source

The International Guideline for the Definition, Classification, Diagnosis and Management of Urticaria

Allergy, EarlyView.
ABSTRACT This update and revision of the international guideline for urticaria was developed in accordance with the methods recommended by Cochrane and the Grading of Recommendations Assessment, Development and Evaluation (GRADE) working group. It is an initiative of the Global Allergy and Asthma Excellence Network (GA2LEN) and its Urticaria and ...
T. Zuberbier, Z. Abdul Hameed Ansari, A. H. Abdul Latiff, M. M. Abuzakouk, M. S. Agcaoili‐De Jesus, R. C. Agondi, M. Al‐Ahmad, A. A. Alangari, H. Alhameli, C. D. Alonso Bello, S. Alshareef, S. Al‐Tamemi, S. Altrichter, H. Al Wahshi, S. Aquilina, M. Araújo, R. Arnaout, R. Asero, B. Ballmer‐Weber, C. Bangert, A. Bauer, M. Ben‐Shoshan, J. A. Bernstein, C. Bindslev‐Jensen, M. Bizjak, I. Boccon‐Gibod, H. Bonnekoh, L. Bouillet, K. Brockow, Z. Brzoza, M. Bulatović Ćalasan, A. Bulkhi, T. Buttgereit, A. Bygum, T. Caballero, O. Calderon, R. Campos, M. Cancian, E. Carne, M. A. Castor, I. Cerecedo, T. Çetinarslan, I. Cherrez‐Ojeda, N. Chkhikvadze, H. J. Chong‐Neto, K. Choo, G. Christoff, C.‐Y. Chu, K. Ciupka, N. Conlon, C. Costa, T. Craig, P. Criado, I. Danilycheva, R. Darlenski, E. De Arruda Chaves, L. de Montjoye, M. S. Doutre, A. Du‐Thanh, D. Ebo, S. Elkhalifa, S. Elmariah, T. El‐Shanawany, L. F. Ensina, R. Ertaş, R. Fachini Jardim Criado, M. Ferrer, S. Ferrucci, J. S. Fok, D. Fomina, L. Fonacier, G. Fouda, I. Francescantonio, A. Fukunaga, C. A. Galvan Calle, E. Garcia, K. Gáspár, A. Gelincik, S. Geng, K. Godse, M. Gonçalo, M. Gotua, C. Grattan, M. Grosber, G. Guidos Fogelbach, M. Guilarte, R. Guillod, E. Hamelmann, J. Hawkes, K. Hayama, R. Heuer, M. Hide, W. Hoetzenecker, N. Inomata, H.‐R. Kang, A. Kaplan, A. Kapp, M. Karam, A. Kasperska‐Zajac, C. H. Katelaris, A. Kessel, M. Khoshkhui, B. Kim, T. Kinaciyan, E. Kocatürk, M. Kolacinska‐Flont, P. Kolkhir, G. N. Konstantinou, M. Kosnik, D. Krasowska, K. Kulthanan, M. S. Kumaran, I. Kuprys‐Lipinska, M. Labrador, J. I. Larco, D. Larenas‐Linnemann, E. Latysheva, E. Lazaridou, P. H. Li, H. Lima, U. Lippert, M. Magerl, M. Makris, J. Alves Marcelino, A. V. Marzano, I. Medina, R. Meshkova, D. Micallef, R. Mohammed Ali, C. G. Mortz, M. Munoz, H. N. G. Oude Elberink, A. Nakonechna, I. Nasr, A. Nast, E. Netchiporouk, E. Nettis, S. Nieto, I. Ogueta Canales, T.‐L. Okas, R. L. Orfali, E. Özkaya, C. Parisi, A. Pennitz, R. Pawankar, M. P. Pereira, J. Peter, E. Petkova, P. D. Pigatto, I. Podder, T. Popov, G. Porebski, P. Pyatilova, G. D. Ramon, H. A. Ratti Sisa, M. Recto, K. Ress, K. Ridge, M. Riedl, C. Ritchie, N. Rosario Filho, I. Rosmaninho, M. Rudenko, M. Rukhadze, K. Rutkowski, V. Sabato, U. M. Sahiner, S. Saini, F. Saleh Al Sabbagh, A. Salman, F. Salvo, J. Sanchez, A. Santucci, S. Schliemann, P. Schmid‐Grendelmeier, B. E. Sekerel, F. Serpa, F. Sheikh, J. Sheikh, H. Shendi, F. Siebenhaar, M. Sonomjamts, A. Soria, B. Sousa Pinto, M. Staevska, P. Staubach, M. Stephan, K. Stevanovic, L. Stingeni, M. Stobiecki, Ö. Su Küçük, G. Sussman, A. Szegedi, S. Takahagi, A. Tanaka, N. Teovska Mitrevska, S. F. Thomsen, E. Toubi, F. Tsatsou, M. Turk, Z. Vadasz, A. Valerieva, S. Valle, M. v. Doorn, B. Veleiro Perez, C. E. Vera Ayala, C. Vestergaard, R. J. Vieira, C. W. Maruta, B. Wedi, R. N. Werner, E. W. Y. Yap, P. Xepapadaki, Y. Xiang, Y.‐M. Ye, P. Yong, G. Yosipovitch, A. Z. J. Zalewska‐Janowska, C. Zeyen, Z. Zhao, M. Metz, A. M. Giménez‐Arnau   +221 more
wiley   +1 more source

Expression of chondroitin sulfotransferases in the injured spinal cord [PDF]

, 2004
We demonstrated that chondroitinase ABC infused into the graft-host interface resolved the glial scar and improved prospects of axonal regeneration into the distal host spinal cord.
Chau, CH, Liu, J, Shum, DKY, Chan, YS
core  

Sulfotransferases: Genetics and role in toxicology. [PDF]

, 2000
The mammalian xenobiotic-metabolizing sulfotransferases are cytosolic enzymes, which form a gene superfamily (SULT). Ten distinct human SULT forms are known. Two SULT forms represent splice variants, the other forms are encoded by separate genes.
Pabel, U., Falany, C.N., Teubner, W., Coughtrie, M.W., Glatt, H., Engelke, C.E., Jones, A.L., Andrae, U., Meinl, W.   +8 more
core   +1 more source

The Emerging Roles of Heparan Sulfate 3-O-Sulfotransferases in Cancer

Frontiers in Oncology, 2019
Alteration in the expression of heparan sulfate (HS)-modifying enzymes has been frequently observed in cancer. Consequently, dysregulation of the HS biosynthetic machinery results in dramatic changes in the HS structure, thereby impacting a range of ...
Agnès Denys, Fabrice Allain
doaj   +1 more source