Results 101 to 110 of about 788,026 (349)

Supplementary Figure 2 from L1 Cell Adhesion Molecule Promotes Tumorigenicity and Metastatic Potential in Non–Small Cell Lung Cancer [PDF]

, 2023
Josephine Hai, Chang‐Qi Zhu, Bizhan Bandarchi, Yuhui Wang, Roya Navab, Frances A. Shepherd, Igor Jurišica, Ming‐Sound Tsao   +7 more
openalex   +1 more source

LDAcoop: Integrating non‐linear population dynamics into the analysis of clonogenic growth in vitro

Molecular Oncology, EarlyView.
Limiting dilution assays (LDAs) quantify clonogenic growth by seeding serial dilutions of cells and scoring wells for colony formation. The fraction of negative wells is plotted against cells seeded and analyzed using the non‐linear modeling of LDAcoop.
Nikko Brix, Daniel Samaga, Katharina Gehr, Benedek Dankó, Mohamed Schumann, Guido Drexler, Ahmed Alnatsha, Georg Beyer, Ujjwal Mahajan, Martin Selmansberger, Julia Mayerle, Claus Belka, Horst Zitzelsberger, Kirsten Lauber   +13 more
wiley   +1 more source

Notch-Mediated Cell Adhesion

Biology, 2016
Notch family members are generally recognized as signaling molecules that control various cellular responses in metazoan organisms. Early fly studies and our mammalian studies demonstrated that Notch family members are also cell adhesion molecules ...
Akihiko Murata, Shin-Ichi Hayashi
doaj   +1 more source

Plecstatin inhibits hepatocellular carcinoma tumorigenesis and invasion through cytolinker plectin

Molecular Oncology, EarlyView.
The ruthenium‐based metallodrug plecstatin exerts its anticancer effect in hepatocellular carcinoma (HCC) primarily through selective targeting of plectin. By disrupting plectin‐mediated cytoskeletal organization, plecstatin inhibits anchorage‐dependent growth, cell polarization, and tumor cell dissemination.
Zuzana Outla, Jan Kosla, Magdalena Prechova, Lukas Frick, Patricia Bortel, Yasmin Borutzki, Andrea Bileck, Christopher Gerner, Samuel M. Meier‐Menches, Selma Osmanagic‐Myers, Martin Gregor   +10 more
wiley   +1 more source

Carcinoembryonic Antigen Gene Family [PDF]

, 1991
The carcinoembryonic antigen (CEA) gene family belongs to the immunoglobulin supergene family and can be divided into two main subgroups based on sequence comparisons.
Accili, Ahnen, Anderson, Arakawa, Arakawa, Audette, Aurivillius, Barnett, Barnett, Barnett, Barnett, Barnett, Barthels, Beatty, Beauchemin, Beauchemin, Beauchemin, Beidler, Benchimol, Berling, Berling, Bhattacharya-Chatterjee, Biggin, Bischof, Bischoff-Delaloye, Bohn, Bordes, Borjigin, Boucher, Boucher, Buchegger, Buchegger, Burtin, Börmer, Capecchi, Chakrabarty, Chakrabarty, Chan, Chan, Chandrasekaran, Chou, Chou, Chu, Cordon, Cournoyer, Cross, Cunningham, DeRobertis, Dustin, Edelman, Edwards, Egan, Fantini, Feizi, Fiebig, Freyer, Fritsch, Fritsche, Fritz Grunert, Gold, Gold, Goldenberg, Goldenberg, Greiner, Greiner, Grosveld, Grunert, Grunert, Guadagni, Hager, Hammarström, Haniford, Hansson, Hardman, Hass, Hefta, Hefta, Hefta, Hemperly, Higashide, Hinoda, Hinoda, Hinoda, Hostetter, Huang, Huitric, Hwang, Inazawa, Jean, John A. Thompson, Jones, Kamarck, Kasuga, Khan, Khan, Khan, Knapp, Kobata, Kodelja, Kolbinger, Kudo, Kupchik, Kuroki, Kuroki, Kuroki, Kuroki, Kuroki, Kuroki, Kuroki, Kurroki, Lai, Leon, Leslie, Leusch, Lewis, Lin, Lin, Lin, Lisanti, Losman, Mach, Margolis, Margolis, Martin, Matsuoka, McDonald, McLenachan, Monden, Mount, Nagata, Neumaier, Neumaier, Neumaier, Nichols, Niemann, Niemann, Niles, Novak-Hofer, Ocklind, Odin, Ogilvie, Oikawa, Oikawa, Oikawa, Oikawa, Oikawa, Paxton, Perkins, Perrotti, Pignatelli, Proudfoot, Ravetch, Ravetch, Rebstock, Rees-Jones, Rojas, Rooney, Rosen, Rosen, Rudert, Rudert, Ruoslahti, Sack, Salzer, Sato, Saunders, Schmid, Schonk, Schrewe, Schrewe, Schwarz, Schwarz, Sell, Sewell, Sharkey, Shively, Siepen, Slightom, Smale, Soeller, Staunton, Staunton, Streydio, Streydio, Streydio, Svenberg, Svenberg, Takami, Takeichi, Takeichi, Tatarinov, Tawaragi, Terry, Thomas, Thomas, Thompson, Thompson, Thompson, Thompson, Thompson, Tingström, Toribara, Toribara, Toth, Toth, Tran, Tsao, Tsujisaki, Tsujisaki, Tuan, Turbide, Van der Schoot, Van der Schoot, Von Kleist, Von Kleist, Von Kleist, Von Kleist, Vorličková, Wallner, Watanabe, Watanabe, Watt, Willcocks, Willcocks, Williams, Williams, Williams, Wolfgang Zimmermann, Yamaguchi, Yarden, Zheng, Zhou, Zimmermann, Zimmermann, Zimmermann, Zoubir, Öbrink   +236 more
core   +1 more source

Therapeutic strategies for MMAE‐resistant bladder cancer through DPP4 inhibition

Molecular Oncology, EarlyView.
We established monomethyl auristatin E (MMAE)‐resistant bladder cancer (BC) cell lines by exposure to progressively increasing concentrations of MMAE in vitro. RNA sequencing showed DPP4 expression was increased in MMAE‐resistant BC cells. Both si‐DPP4 and the DPP4 inhibitor sitagliptin suppressed the viability of MMAE‐resistant BC cells.
Gang Li, Shuichi Tatarano, Hirofumi Yoshino, Saeki Saito, Mitsuhiko Tominaga, Junya Arima, Ikumi Fukuda, Takashi Sakaguchi, Ryosuke Matsushita, Yasutoshi Yamada, Hideki Enokida   +10 more
wiley   +1 more source

Use of a recombinant pseudorabies virus to analyze motor cortical reorganization after unilateral facial denervation [PDF]

, 2005
A unilateral facial nerve injury (n7x) was found to influence the transcallosal spread of the attenuated strain of pseudorabies virus (PRV Bartha) from the affected (left) primary motor cortex (MI) to the contralateral MI of rats.
Boda, Krisztina, Boldogkői, Zsolt, Farkas, Tamás, Horváth, Szatmár, Janka, Zoltán, Kis, Zsolt, Pankotai, Eszter, Prandovszky, Emese, Toldi, József   +8 more
core   +1 more source

Peroxidasin enables melanoma immune escape by inhibiting natural killer cell cytotoxicity

Molecular Oncology, EarlyView.
Peroxidasin (PXDN) is secreted by melanoma cells and binds the NK cell receptor NKG2D, thereby suppressing NK cell activation and cytotoxicity. PXDN depletion restores NKG2D signaling and enables effective NK cell–mediated melanoma killing. These findings identify PXDN as a previously unrecognized immune evasion factor and a potential target to improve
Hsu‐Min Sung, David Bickel, Lena C. M. Krause, Daria Ezeriņa, Christian Ickes, Julian Wojtachnia, Christine S. Gibhardt, Magdalena Shumanska, Khadija Wahni, Andrea Paluschkiwitz, Julia Malo Pueyo, Ekaterina Baranova, Wim Vranken, Hedwig Stanisz, Ioana Stejerean‐Todoran, Michael P. Schön, Joris Messens, Ivan Bogeski   +17 more
wiley   +1 more source

Solving the binding problem: cellular adhesive molecules and their control of the cortical quantum entangled network [PDF]

, 2003
Quantum entanglement is shown to be the only acceptable physical solution to the binding problem. The biological basis of interneuronal entanglement is described in the frames of the beta-neurexin-neuroligin model developed by Georgiev (2002) and is ...
Georgiev, Danko
core  

Effects of oxidized low density lipoprotein, lipid mediators and statins on vascular cell interactions [PDF]

, 1999
The integrin heterodimer CD11b/CD18 (alpha M beta 2, Mac-1, CR3) expressed on monocytes or polymorphonuclear leukocytes (PMN) is a receptor for iC3b, fibrinogen, heparin, and for intercellular adhesion molecule (ICAM)-1 on endothelium, crucially ...
Amatruda TT, Bednar MM, Bellosta S, Buttrum SM, Buyon JP, Calara F, Calderon TM, Diacovo TG, Giroux LM, Jukema JW, Kim JA, Kimura M, Laufs U, Laws KH, Lehr H-A, Marcus AJ, Notabartolo A, Olstrowsky L, Pons F, Ruf A, Smalley DM, Stragliotto E, Sugiyama S, Weber C, Weber C, Weber C, Yeagle PL, Yeo EL, Yue TL   +28 more
core   +1 more source