Results 51 to 60 of about 30,138 (217)

Profiling Heparan Sulfate Proteoglycans in Ovarian Carcinoma [PDF]

The Scientific World JOURNAL, 2005
: heparan sulfate, proteoglycans, syndecan, glypican, perlecan, ovarian carcinoma, angiogenesis, prognostic factors Heparan sulfate proteoglycans (HSPGs) are ubiquitously expressed cell surface and extracellular matrix (ECM) molecules consisting of a core protein covalently attached to the structurally complex glycosaminoglycan, heparan sulfate (HS ...
Clamp, Andrew R., Jayson, Gordon C.
openaire   +4 more sources

Lipolysis of very low density lipoproteins by heparan sulfate proteoglycan-bound lipoprotein lipase

Journal of Lipid Research, 1997
An in vitro assay to study lipolysis of very low density lipoproteins (VLDL) by heparan sulfate proteoglycan (HSPG-bound lipoprotein lipase (LPL) was developed.
F H de Man, F de Beer, A van der Laarse, A H Smelt, L M Havekes   +4 more
doaj   +1 more source

Heparan sulfates and heparan sulfate proteoglycans in hematopoiesis

Blood
Abstract From signaling mediators in stem cells to markers of differentiation and lineage commitment to facilitators for the entry of viruses, such as HIV-1, cell surface heparan sulfate (HS) glycans with distinct modification patterns play important roles in hematopoietic biology.
Richard T. Piszczatowski, Hannes E. Bülow, Ulrich Steidl   +2 more
openaire   +2 more sources

Isolation and Characterization of Heparan Sulfate from Human Lung Tissues

Molecules, 2021
Glycosaminoglycans are a class of linear, highly negatively charged, O-linked polysaccharides that are involved in many (patho)physiological processes.
Rupert Derler, Nikola Kitic, Tanja Gerlza, Andreas J. Kungl   +3 more
doaj   +1 more source

An Expanded Toolbox for Versatile Chemical Editing of Adeno‐Associated Virus

Angewandte Chemie, EarlyView.
We describe technology to introduce diverse non‐natural chemical functionalities site‐specifically into the capsid of adeno‐associated virus through genetic code expansion, and using them to engineer this leading vector for human gene therapy for enhanced tissue specificity and reduced immunogenicity Abstract Site‐specific incorporation of noncanonical
Quan Pham, Jake Glicksman, Boyang Han, David Koo, Conor Loynd, Soumya Jyoti Singha Roy, Abhishek Chatterjee   +6 more
wiley   +2 more sources

The multifaceted roles of perlecan in fibrosis [PDF]

, 2018
Perlecan, or heparan sulfate proteoglycan 2 (HSPG2), is a ubiquitous heparan sulfate proteoglycan that has major roles in tissue and organ development and wound healing by orchestrating the binding and signaling of mitogens and morphogens to cells in a ...
Al-Ahmad, Andersson-Sjoland, Andersson-Sjoland, Arthur, Ashikari-Hada, Asplund, Aviezer, Barkefors, Barros, Behrens, Beller, Bengtsson, Bingley, Bishop, Bittencourt, Bix, Bix, Borkham-Kamphorst, Bremnes, Burgess, Cailhier, Cassiman, Celie, Ceol, Chakravarti, Chen, Chilosi, Chuang, Chuang, Cohen, Conde-Knape, Conte, Costell, Di Sario, Dos Santos, Duffield, Ebefors, Edgar, Esko, Evanko, Farach-Carson, Farach-Carson, Fengying Tang, Fernandez, Forsberg, Friedman, Friedman, Fujii, Gallai, Garl, Ge, Gellersen, Giros, Gohring, Gonzalez, Gonzalez, Goyal, Gressner, Gubbiotti, Guo, Hajari Case, Hallgren, Hammond, Hashimoto, Haubst, Hayashi, Hayward, Hedin, Hedin, Hering, Hilberg, Hisatomi, Ichimaru, Ikeguchi, Iozzo, Iozzo, Iozzo, Iredale, James G.W. Smith, James Melrose, Jelena Rnjak-Kovacina, John M. Whitelock, Jung, Kahari, Kaji, Kennett, Kinsella, Knox, Knox, Knox, Knox, Kotaru, Kovalszky, Koyama, Krimmer, Kunjathoor, Kvist, Laplante, Laplante, Leask, Leask, Leask, Lee, Lee, Lee, Lekkerkerker, Levy, Liang, Lord, Lord, Lord, Lord, Lundkvist, Mak, Mak, Mak, Malmstrom, Marra, Martinez-Hernandez, Martinez-Hernandez, Marx, Marzoll, Masola, Matsui, Matsuo, Megan S. Lord, Melrose, Melrose, Menzel, Mitra, Mollmark, Mongiat, Mongiat, Moon, Murphy, Musso, Nagy, Nakamura, Nakayama, Narita, Nguyen, Nihlberg, Nilsson, Ogawa, Ohkawara, Ozaki, Paka, Patel, Pillarisetti, Pinzani, Poluri, Pozzi, Raines, Raj, Rauch, Raymond, Rees, Rienstra, Rnjak-Kovacina, Rojkind, Rolls, Rosenzweig, Roskams, Ross, Sahin, Sakai, Salem, Sato, Schaefer, Schafer, Segev, Sharma, Shimizu-Hirota, Singh, Sofroniew, Sweeney, Tang, Tang, Tannock, Tao, Teh, Teimouri, Theret, Thomas, Thyberg, Timpl, Tomasek, Tran, Tran, Tran-Lundmark, Tátrai, Uchimura, Vanheule, Venkatesan, Venkatesan, Wang, Weiser, Weiser, Westergren-Thorsson, Westergren-Thorsson, Westergren-Thorsson, Whitelock, Whitelock, Whitelock, Whitelock, Willis, Wollin, Wollin, Woodall, Xu, Yamamoto, Yang, Yaoi, Yue, Yung, Yung, Zeisberg, Zeisberg   +217 more
core   +1 more source

Microbial Subversion of Heparan Sulfate Proteoglycans

Molecules and Cells, 2008
The interactions between the host and microbial pathogen largely dictate the onset, progression, and outcome of infectious diseases. Pathogens subvert host components to promote their pathogenesis and, among these, cell surface heparan sulfate proteoglycans are exploited by many pathogens for their initial attachment and subsequent cellular entry.
Ye, Chen, Martin, Götte, Jian, Liu, Pyong Woo, Park   +3 more
openaire   +2 more sources

Endothelial glycocalyx degradation during sepsis: Causes and consequences

Matrix Biology Plus, 2021
The glycocalyx is a ubiquitous structure found on endothelial cells that extends into the vascular lumen. It is enriched in proteoglycans, which are proteins attached to the glycosaminoglycans heparan sulfate, chondroitin sulfate, dermatan sulfate ...
Ryan C. Sullivan, Matthew D. Rockstrom, Eric P. Schmidt, Joseph A. Hippensteel   +3 more
doaj   +1 more source

Syndecan-4 knockout leads to reduced extracellular transglutaminase-2 and protects against tubulointerstitial fibrosis [PDF]

, 2013
Transglutaminase type 2 (TG2) is an extracellular matrix crosslinking enzyme with a pivotal role in kidney fibrosis. The interaction of TG2 with the heparan sulfate proteoglycan syndecan-4 (Sdc4) regulates the cell surface trafficking, localization, and ...
Burhan, I, Funck, M, Huang, L, Johnson, TS, Scarpellini, A, Schroeder, N, Verderio, EAM   +6 more
core   +1 more source

Dammarenediol II enhances etoposide‐induced apoptosis by targeting O‐GlcNAc transferase and Akt/GSK3β/mTOR signaling in liver cancer

Molecular Oncology, EarlyView.
Etoposide induces DNA damage, activating p53‐dependent apoptosis via caspase‐3/7, which cleaves PARP1. Dammarenediol II enhances this apoptotic pathway by suppressing O‐GlcNAc transferase activity, further decreasing O‐GlcNAcylation. The reduction in O‐GlcNAc levels boosts p53‐driven apoptosis and influences the Akt/GSK3β/mTOR signaling pathway ...
Jaehoon Lee, Byung‐Cheol Han, Gi‐Bang Koo, Jihye Park, Mijin Kwon, Young Bin Park, Jae‐Mun Choi, Seung‐Ho Lee, Sangho Roh   +8 more
wiley   +1 more source