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Journal articles on the topic 'ShK'

Author: Grafiati
Published: 4 June 2021
Last updated: 18 February 2022

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1

Crow, James Mitchell. "Venomous drugs: ShK." New Scientist 214, no. 2863 (May 2012): 37. http://dx.doi.org/10.1016/s0262-4079(12)61175-0.

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2

Pennington, M. "ShK-186 from discovery to clinical development." Toxicon 75 (December 2013): 211. http://dx.doi.org/10.1016/j.toxicon.2013.08.020.

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3

Diez-Martín, Fernando, Cristina Fraile, David Uribelarrea, Policarpo Sánchez-Yustos, Manuel Domínguez-Rodrigo, Javier Duque, Isabel Díaz, et al. "SHK Extension: a new archaeological window in the SHK fluvial landscape of Middle Bed II (Olduvai Gorge, Tanzania)." Boreas 46, no. 4 (April 13, 2017): 831–59. http://dx.doi.org/10.1111/bor.12246.

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4

Velazhahan, Rethinasamy, Shima Nasser Hamed Al-Mamari, Abdullah Mohammed Al-Sadi, Issa Hashil Al-Mahmooli, and S. P. Sathish Babu. "In vitro antagonistic potential, plant growth-promoting activity and indole-3-acetic acid producing trait of bacterial isolates from spent mushroom substrate of Agaricus bisporus." Journal of Agricultural and Marine Sciences [JAMS] 25, no. 2 (September 20, 2020): 22. http://dx.doi.org/10.24200/jams.vol25iss2pp22-29.

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Spent mushroom substrate (SMS) is widely used as fertilizer and to control plant diseases. The microorganisms surviving in SMS play a crucial role in plant growth promotion and biocontrol properties of SMS. In this study, an effort was made to isolate and characterize the bacterial species present in the SMS of Agaricus bisporus and to study their antagonistic potential, plant growth-promoting ability and indole-3-acetic acid (IAA) producing trait. Six different bacterial isolates exhibiting morphological variabilities were obtained from the SMS by serial dilution technique. On the basis of 16S rRNA gene sequences, these isolates were identified as Staphylococcus epidermidis (Sh1 and Sh3), S. aureus (Sh2), Bacillus albus (Sh4), Delftia lacustris (Sh6) and Comamonas aquatica (Sh7). These bacterial strains were assayed for their antagonism against Pythium aphanidermatum, a phytopathogenic oomycete. The results of in vitro dual culture assay revealed that all the 6 bacterial isolates showed low levels of suppression of P. aphanidermatum and recorded less than 5 mm inhibition zone. Among the bacterial isolates, S. epidermidis Sh3 recorded the maximum inhibition zone of 4.2 mm. Plant growth promotion test using roll paper towel method revealed that C. aquatica Sh7, B. albus Sh4, D. lacustris Sh6 and S. epidermidis Sh3 caused a significant increase in seedling vigour of cucumber compared to control. The seeds treated with the bacterial isolate C. aquatica Sh7 showed the maximum seedling vigor. Assessment of in vitro production of IAA by the bacterial isolates revealed that the bacterial isolates highly varied (ranging from 0.28 to 9.25 mg L-1) in their potential for production of IAA. The maximum amount of IAA was produced by C. aquatica Sh7 (9.25 mg L-1), while the minimum was produced by S. epidermidis Sh1 (0.28 mg L-1).
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Li, Huachao, Yueming Chen, Jiahao Zhang, Xiangcui Chen, Zheng Li, Bing Liu, and Luyong Zhang. "Shikonin Attenuates Acetaminophen-Induced Hepatotoxicity by Upregulation of Nrf2 through Akt/GSK3β Signaling." Molecules 24, no. 1 (December 29, 2018): 110. http://dx.doi.org/10.3390/molecules24010110.

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Acetaminophen (APAP) overdose-induced acute liver damage is mostly due to overwhelmingly increased oxidative stress. Nuclear factor-erythroid 2-related factor2 (Nrf2) plays an important role in alleviating APAP hepatic toxicity. Shikonin (SHK) enhances Nrf2 in multiple lines of normal cells. Nevertheless, whether SHK protects against APAP-induced liver toxicity remains undefined. This study found SHK defended APAP-induced liver toxicity, as well as reversed the levels of serum alanine/aspartate aminotransferases (ALT/AST), liver myeloperoxidase (MPO) activity, and reactive oxygen species (ROS), while it enhanced the liver glutathione (GSH) level in APAP-treated mice. SHK rescued the cell viability and GSH depletion, but neutralized oxidative stress in APAP-treated human normal liver L-02 cells. Mechanically, SHK increased Nrf2 expression in the exposure of APAP at the protein level but not at the mRNA level. Inhibition of Nrf2 blocked the SHK effect in APAP-treated hepatocytes. Furthermore, SHK improved Nrf2 stability through stimulating PI3K/Akt pathway, thus inhibiting GSK-3β. In vivo studies confirmed the close correlation of liver protection of SHK against APAP and Akt/GSK-3β/Nrf2 pathway. In conclusion, this study reveals that SHK prevents APAP hepatotoxicity by upregulation of Nrf2 via PI3K/Akt/GSK-3β pathway. Therefore, SHK may be a promising candidate against APAP-induced liver injury.
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6

Ma, Shu-Xin, Li-Bo Tang, Zhi-Hang Chen, Min-Li Wei, Zi-Juan Tang, Yue-Hui Zheng, Guo Zong, and Jia Li. "Effects of shikonin on the development of ovarian follicles and female germline stem cells." Journal of International Medical Research 49, no. 7 (July 2021): 030006052110294. http://dx.doi.org/10.1177/03000605211029461.

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Objective To investigate the effects and potential mechanism of action of shikonin (SHK) on the development of ovarian follicles and female germline stem cells (FGSCs). Methods Female Kunming adult mice were administered SHK (0, 20 and 50 mg/kg) by oral gavage. Cultures of FGSCs were treated with SHK 32 μmol/l for 24 h. The ovarian index in mouse ovaries was calculated. Numbers of primordial, primary and atretic follicles were counted. Germline stem cell markers and apoptosis were examined. Levels of glutathione (GSH), superoxide dismutase (SOD) and reactive oxygen species (ROS) were measured. Results Both doses of SHK significantly decreased the ovarian index, the numbers of primordial follicles, primary follicles and antral follicles in mice. SHK significantly increased the numbers of atretic follicles and atretic corpora lutea. SHK promoted apoptosis in vivo and in vitro. SHK significantly decreased the levels of the germline stem cell markers. SHK significantly lowered GSH levels and the activity of SOD in the peripheral blood from mice, whereas SHK significantly elevated cellular ROS content in FGSCs. Conclusions These current results suggested that follicular development and FGSCs were suppressed by SHK through the induction of apoptosis and oxidative stress might be involved in this pathological process.
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7

Kalman, Katalin, Michael W. Pennington, Mark D. Lanigan, Angela Nguyen, Heiko Rauer, Vladimir Mahnir, Kathy Paschetto, et al. "ShK-Dap22, a Potent Kv1.3-specific Immunosuppressive Polypeptide." Journal of Biological Chemistry 273, no. 49 (December 4, 1998): 32697–707. http://dx.doi.org/10.1074/jbc.273.49.32697.

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8

Pasquadibiscesceglie, Andrea, Manuela Cervelli, Jonathan Reinoso Sanchez, Paolo Mariottini, Marco Oliverio, Marco Gerdol, and Maria Vittoria Modica. "ShK-like toxins from the vampire snail Colubraria reticulata." Toxicon 149 (July 2018): 100–101. http://dx.doi.org/10.1016/j.toxicon.2018.02.018.

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9

Wada, Naoko, Yawara Kawano, Shiho Fujiwara, Yoshitaka Kikukawa, Yutaka Okuno, Hiroaki Mitsuya, and Hiroyuki Hata. "A Small Molecule, Shikonin, Dually Functions As a Proteasome Inhibitor and a Necroptosis Inducer In Multiple Myeloma Cells." Blood 122, no. 21 (November 15, 2013): 3172. http://dx.doi.org/10.1182/blood.v122.21.3172.3172.

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Abstract Background Despite of recent advances in therapeutic strategy for multiple myeloma (MM), MM still remains incurable and novel therapeutic approach is urgently needed. We have previously demonstrated that a natural small molecule, shikonin (SHK), induced both apoptosis and necroptosis (programmed necrosis) in MM cells. In this study, we attempted to elucidate biological mechanisms of SHK in inducing apoptosis and necroptosis. Methods Six MM cell lines, KMS-12-PE, RPMI 8226, U266, KMM1, KMS-11 and a bortezomib-resistant MM cell line, KMS-11/BTZ (obtained from Kyowa Hakko Kirin Co. Ltd.), were utilized. Inhibitors of pan-caspase and necroptosis, ZVAD-fmk and Nec-1 (necrostatin-1), were employed to distinguish apoptosis and necroptosis, respectively. Cell death was analyzed using the trypan blue dye exclusion method (WST-8 assay) and flow cytometry analysis using AnnexinV/PI staining. Morphological examinations of cells were performed with May Giemza staining. Caspases, RIP1, ubiquitinated proteins, and heat shock proteins were analyzed with western blot. Knockdown of RIP1, an essential molecule for necroptosis, was performed using siRNA. ER stress was assessed by detecting activated XBP-1, which was analyzed by digestion of PCR products with ApaLI. Because the ApaLI site in XBP-1 mRNA is spliced out upon activation, the activated XBP-1 shows one large band after ApaLI digestion, while inactivated XBP-1 shows two ApaI-digested bands. Thapsigargin, sarcoplasmic/endoplasmic reticulum Ca2+ ATPase (SERCA) inhibitor, was used as an ER stress inducer. Results By screening natural compounds libraries (provided by Institute of Natural Medicine, Toyama University, Japan), we found that SHK, a natural compound derived from the root of Lithospermum erythrorhizon, induced cell death in MM cells. Apoptosis was induced at a relatively low concentration (2.5∼5 µM) and was inhibited by a caspase-inhibitor, while necroptosis was promptly induced at higher concentrations (10∼ 20 µM) within 5 hours and was completely inhibited by Nec-1. Morphological analysis showed that SHK at low concentrations induced typical apoptotic changes, such as fragmented nucleus, while SHK at higher concentrations induced necrotic morphology, such as translucent cytoplasm and swelling of cell membranes. By contrast, SHK did not induce apoptosis or necrptosis in peripheral blood mononuclear cells from healthy donors at low concentrations. SHK activated caspase-8 and -3 at low concentrations but did not at higher concentrations. RIP1, an essential molecule for necroptosis, was cleaved after treatment with SHK at low concentrations, which leads to the inhibition of necroptosis, while it was not cleaved and remained active at higher concentrations, suggesting that SHK dynamically regulates the cleavage of RIP-1. At low concentrations, shikonin induced an accumulation of ubiquitinated proteins and activated XBP-1, suggesting SHK may have a property of proteasome inhibitor eventually inducing endoplasmic reticulum stress. Finally, SHK at low concentration killed bortezomib resistant cells with lower IC50 comparing to that of the parental cells (0.91 vs 1.56 µM, respectively). Conclusions We here report, for the first time, that SHK induces apoptosis and necroptosis in MM cells at low and high concentrations, respectively, by regulating proteasome function and RIP-1 cleavage. Given the fact that SHK efficiently induces cell death in bortezomib-resistant cell line, SHK may act as a novel proteasome inhibitor for bortezomib-resistant myeloma cells. Moreover, SHK at higher concentrations, which induces nectoptosis, should be an attractive future therapeutic option potentially to eradicate MM cells. Disclosures: No relevant conflicts of interest to declare.
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10

Sachkova, Maria Y., Morani Landau, Joachim M. Surm, Jason Macrander, Shir A. Singer, Adam M. Reitzel, and Yehu Moran. "Toxin-like neuropeptides in the sea anemoneNematostellaunravel recruitment from the nervous system to venom." Proceedings of the National Academy of Sciences 117, no. 44 (October 15, 2020): 27481–92. http://dx.doi.org/10.1073/pnas.2011120117.

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The sea anemoneNematostella vectensis(Anthozoa, Cnidaria) is a powerful model for characterizing the evolution of genes functioning in venom and nervous systems. Although venom has evolved independently numerous times in animals, the evolutionary origin of many toxins remains unknown. In this work, we pinpoint an ancestral gene giving rise to a new toxin and functionally characterize both genes in the same species. Thus, we report a case of protein recruitment from the cnidarian nervous to venom system. The ShK-like1 peptide has a ShKT cysteine motif, is lethal for fish larvae and packaged into nematocysts, the cnidarian venom-producing stinging capsules. Thus, ShK-like1 is a toxic venom component. Its paralog, ShK-like2, is a neuropeptide localized to neurons and is involved in development. Both peptides exhibit similarities in their functional activities: They provoke contraction inNematostellapolyps and are toxic to fish. Because ShK-like2 but not ShK-like1 is conserved throughout sea anemone phylogeny, we conclude that the two paralogs originated due to aNematostella-specific duplication of a ShK-like2 ancestor, a neuropeptide-encoding gene, followed by diversification and partial functional specialization. ShK-like2 is represented by two gene isoforms controlled by alternative promoters conferring regulatory flexibility throughout development. Additionally, we characterized the expression patterns of four other peptides with structural similarities to studied venom components and revealed their unexpected neuronal localization. Thus, we employed genomics, transcriptomics, and functional approaches to reveal one venom component, five neuropeptides with two different cysteine motifs, and an evolutionary pathway from nervous to venom system in Cnidaria.
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11

Chang, Shih Chieh, Saumya Bajaj, and K. George Chandy. "ShK toxin: history, structure and therapeutic applications for autoimmune diseases." WikiJournal of Science 1, no. 1 (June 1, 2018): 3. http://dx.doi.org/10.15347/wjs/2018.003.

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12

Lanigan, Mark D., Michael W. Pennington, Yann Lefievre, Heiko Rauer, and Raymond S. Norton. "Designed Peptide Analogues of the Potassium Channel Blocker ShK Toxin†." Biochemistry 40, no. 51 (December 2001): 15528–37. http://dx.doi.org/10.1021/bi011300b.

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13

Karaduta, Oleg, and Loutfouz Zaman. "Shk-9: A new tool in approach of glycoprotein annotation." SoftwareX 7 (January 2018): 302–3. http://dx.doi.org/10.1016/j.softx.2018.08.004.

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14

Kem, William R., Gautam Sanyal, Robert W. Williams, and Michael W. Pennington. "Secondary structure of ShK toxin, a potassium-channel-blocking peptide." Letters in Peptide Science 3, no. 2 (May 1996): 69–72. http://dx.doi.org/10.1007/bf00126735.

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15

Dang, Bobo, Sandeep Chhabra, Michael W. Pennington, Raymond S. Norton, and Stephen B. H. Kent. "Reinvestigation of the biological activity of d-allo-ShK protein." Journal of Biological Chemistry 292, no. 30 (June 8, 2017): 12599–605. http://dx.doi.org/10.1074/jbc.m117.793943.

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16

Nemolochnov, A. G., S. N. Levichev, I. M. Galimov, and N. A. Zubachev. "Results of Laboratory Tests on Shk-150 Composite Sheet Piles." Power Technology and Engineering 53, no. 5 (January 2020): 549–52. http://dx.doi.org/10.1007/s10749-020-01114-0.

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17

Upadhyay, Sanjeev K., Kristin Eckel-Mahan, MohammedReza Mirbolooki, Indra W. Tjong, Jogeshwar Mukharjee, Shawn P. Iadonato, Paolo Sassoni-Corsi, Ping H. Wang, and K. George Chandy. "Anti-Obesity Effect of Shk-186, a K+ Channel Blocker." Biophysical Journal 102, no. 3 (January 2012): 658a. http://dx.doi.org/10.1016/j.bpj.2011.11.3585.

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18

Karamercan, Mehmet Akif, Scott L. Weiss, Jose Paul Perales Villarroel, Yuxia Guan, Evan Werlin, Ronald Figueredo, Lance B. Becker, and Carrie Sims. "Can Peripheral Blood Mononuclear Cells Be Used as a Proxy for Mitochondrial Dysfunction in Vital Organs During Hemorrhagic Shock and Resuscitation?" Shock 40, no. 6 (December 2013): 476–84. http://dx.doi.org/10.1097/shk.0000000000000026.

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19

Bergt, Stefan, Nana-Maria Wagner, Manja Heidrich, Antje Butschkau, Gabriele E. F. Nöldge-Schomburg, Brigitte Vollmar, and Jan P. Roesner. "Hydrocortisone Reduces the Beneficial Effects of Toll-Like Receptor 2 Deficiency on Survival in a Mouse Model of Polymicrobial Sepsis." Shock 40, no. 5 (November 2013): 414–19. http://dx.doi.org/10.1097/shk.0000000000000029.

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Huang, Pei-Ming, Tzu-Hsin Lin, Pi-Ru Tsai, and Wen-Je Ko. "Intrapleural Steroid Instillation for Multiple Organ Failure With Acute Respiratory Distress Syndrome." Shock 40, no. 5 (November 2013): 392–97. http://dx.doi.org/10.1097/shk.0000000000000031.

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Rump, Katharina, Peter Brendt, Ulrich H. Frey, Simon Thomas Schäfer, Winfried Siffert, Jürgen Peters, and Michael Adamzik. "Aquaporin 1 and 5 Expression Evoked by the β2 Adrenoreceptor Agonist Terbutaline and Lipopolysaccharide in Mice and in the Human Monocytic Cell Line THP-1 Is Differentially Regulated." Shock 40, no. 5 (November 2013): 430–36. http://dx.doi.org/10.1097/shk.0000000000000035.

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Liu, Liangming, Kunlun Tian, Mingying Xue, Yu Zhu, Dan Lan, Xiaoyong Peng, Yue Wu, and Tao Li. "Small Doses of Arginine Vasopressin in Combination With Norepinephrine “Buy” Time for Definitive Treatment for Uncontrolled Hemorrhagic Shock in Rats." Shock 40, no. 5 (November 2013): 398–406. http://dx.doi.org/10.1097/shk.0000000000000036.

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23

Yang, Sung H., Matt Gangidine, Timothy A. Pritts, Michael D. Goodman, and Alex B. Lentsch. "Interleukin 6 Mediates Neuroinflammation and Motor Coordination Deficits After Mild Traumatic Brain Injury and Brief Hypoxia in Mice." Shock 40, no. 6 (December 2013): 471–75. http://dx.doi.org/10.1097/shk.0000000000000037.

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Junger, Wolfgang G., Shawn G. Rhind, Sandro B. Rizoli, Joseph Cuschieri, Andrew J. Baker, Pang N. Shek, David B. Hoyt, and Eileen M. Bulger. "Prehospital Hypertonic Saline Resuscitation Attenuates the Activation and Promotes Apoptosis of Neutrophils in Patients With Severe Traumatic Brain Injury." Shock 40, no. 5 (November 2013): 366–74. http://dx.doi.org/10.1097/shk.0000000000000038.

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Kusadasi, Nuray, and A. B. Johan Groeneveld. "A Perspective on Mesenchymal Stromal Cell Transplantation in the Treatment of Sepsis." Shock 40, no. 5 (November 2013): 352–57. http://dx.doi.org/10.1097/shk.0000000000000039.

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Clemens, Mark G. "What’s New in Shock? October 2013." Shock 40, no. 4 (October 2013): 237–38. http://dx.doi.org/10.1097/shk.0000000000000040.

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Kimmoun, Antoine, Elsa Dubois, Pierre Perez, Annick Barbaud, and Bruno Levy. "Shock State." Shock 40, no. 5 (November 2013): 387–91. http://dx.doi.org/10.1097/shk.0000000000000041.

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Bohannon, Julia K., Antonio Hernandez, Perenlei Enkhbaatar, William L. Adams, and Edward R. Sherwood. "The Immunobiology of Toll-Like Receptor 4 Agonists." Shock 40, no. 6 (December 2013): 451–62. http://dx.doi.org/10.1097/shk.0000000000000042.

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Schofield, Zoe Victoria, Trent Martin Woodruff, Reena Halai, Mike Chia-Lun Wu, and Matthew Allister Cooper. "Neutrophils—A Key Component of Ischemia-Reperfusion Injury." Shock 40, no. 6 (December 2013): 463–70. http://dx.doi.org/10.1097/shk.0000000000000044.

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&NA;. "Superoxide Production in the Vasculature of Lipopolysaccharide-Treated Rats and Pigs." Shock 40, no. 4 (October 2013): 347. http://dx.doi.org/10.1097/shk.0000000000000045.

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Vanwijngaerden, Yoo-Mee, Lies Langouche, Sarah Derde, Christopher Liddle, Sally Coulter, Greet van den Berghe, and Dieter Mesotten. "Impact of Parenteral Nutrition Versus Fasting on Hepatic Bile Acid Production and Transport in a Rabbit Model of Prolonged Critical Illness." Shock 41, no. 1 (January 2014): 48–54. http://dx.doi.org/10.1097/shk.0000000000000046.

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Glassberg, Elon, Roy Nadler, Sami Gendler, Amir Abramovich, Philip C. Spinella, Robert T. Gerhardt, John B. Holcomb, and Yitshak Kreiss. "Freeze-Dried Plasma at the Point of Injury." Shock 40, no. 6 (December 2013): 444–50. http://dx.doi.org/10.1097/shk.0000000000000047.

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DeLano, Frank A., and Geert W. Schmid-Schönbein. "Pancreatic Digestive Enzyme Blockade in the Small Intestine Prevents Insulin Resistance in Hemorrhagic Shock." Shock 41, no. 1 (January 2014): 55–61. http://dx.doi.org/10.1097/shk.0000000000000048.

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Ristagno, Giuseppe, Francesca Fumagalli, Ilaria Russo, Simona Tantillo, Davide Danilo Zani, Valentina Locatelli, Marcella De Maglie, et al. "Postresuscitation Treatment With Argon Improves Early Neurological Recovery in a Porcine Model of Cardiac Arrest." Shock 41, no. 1 (January 2014): 72–78. http://dx.doi.org/10.1097/shk.0000000000000049.

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Valdés-Ferrer, Sergio I., Mauricio Rosas-Ballina, Peder S. Olofsson, Ben Lu, Meghan E. Dancho, JianHua Li, Huan Yang, Valentin A. Pavlov, Sangeeta S. Chavan, and Kevin J. Tracey. "High-Mobility Group Box 1 Mediates Persistent Splenocyte Priming in Sepsis Survivors." Shock 40, no. 6 (December 2013): 492–95. http://dx.doi.org/10.1097/shk.0000000000000050.

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Hobson, Michael J., Paul W. Hake, Michael O’Connor, Christine Schulte, Victoria Moore, Jeanne M. James, Giovanna Piraino, and Basilia Zingarelli. "Conditional Deletion of Cardiomyocyte Peroxisome Proliferator-Activated Receptor γ Enhances Myocardial Ischemia-Reperfusion Injury in Mice." Shock 41, no. 1 (January 2014): 40–47. http://dx.doi.org/10.1097/shk.0000000000000051.

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Gomez, Hernando, Can Ince, Daniel De Backer, Peter Pickkers, Didier Payen, John Hotchkiss, and John A. Kellum. "A Unified Theory of Sepsis-Induced Acute Kidney Injury." Shock 41, no. 1 (January 2014): 3–11. http://dx.doi.org/10.1097/shk.0000000000000052.

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Guillory, Ashley, and Celeste C. Finnerty. "What’s New in Shock? November 2013." Shock 40, no. 5 (November 2013): 349–51. http://dx.doi.org/10.1097/shk.0000000000000053.

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Descamps, Vincent. "Diagnosis of DRESS (Drug Reaction With Eosinophilia and Systemic Symptoms) in the Intensive Care Unit." Shock 40, no. 5 (November 2013): 437–38. http://dx.doi.org/10.1097/shk.0000000000000054.

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Bauzá, Gustavo, Rituparna Moitra, and Daniel Remick. "Adenosine Receptor Antagonists Effect on Plasma-Enhanced Killing." Shock 41, no. 1 (January 2014): 62–66. http://dx.doi.org/10.1097/shk.0000000000000055.

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Shimizu, Tomoharu, Toru Obata, Hiromichi Sonoda, Hiroya Akabori, Tohru Miyake, Hiroshi Yamamoto, Takahisa Tabata, Yutaka Eguchi, and Tohru Tani. "Diagnostic Potential of Endotoxin Scattering Photometry for Sepsis and Septic Shock." Shock 40, no. 6 (December 2013): 504–11. http://dx.doi.org/10.1097/shk.0000000000000056.

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Kochanek, Patrick M., and Travis C. Jackson. "Will the Next Breakthrough for Neuroprotection After Cardiac Arrest Come Out of Thin Air?" Shock 41, no. 1 (January 2014): 85–86. http://dx.doi.org/10.1097/shk.0000000000000057.

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Hall, Kelly E., Claire R. Sharp, Cynthia R. Adams, and Gregory Beilman. "A Novel Trauma Model." Shock 41, no. 1 (January 2014): 25–32. http://dx.doi.org/10.1097/shk.0000000000000058.

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Spinella, Philip C., and Geir Strandenes. "The Trauma Hemostasis and Oxygenation Research Network’s Remote Damage Control Resuscitation Symposium." Shock 41 (May 2014): 1–2. http://dx.doi.org/10.1097/shk.0000000000000059.

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Favory, Raphaël, Julien Poissy, Isabelle Alves, Mary-Jane Guerry, Malcolm Lemyze, Erika Parmentier-Decrucq, Thibault Duburcq, and Daniel Mathieu. "Activated Protein C Improves Macrovascular and Microvascular Reactivity in Human Severe Sepsis and Septic Shock." Shock 40, no. 6 (December 2013): 512–18. http://dx.doi.org/10.1097/shk.0000000000000060.

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Lusczek, Elizabeth R., Daniel R. Lexcen, Nancy E. Witowski, Charles Determan, Kristine E. Mulier, and Greg Beilman. "Prolonged Induced Hypothermia in Hemorrhagic Shock Is Associated With Decreased Muscle Metabolism." Shock 41, no. 1 (January 2014): 79–84. http://dx.doi.org/10.1097/shk.0000000000000061.

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de Haan, Jacco J., Eva Pastille, Florian Wirsdörfer, Tim Lubbers, Jan-Willem M. Greve, Yang Zhang, Wim A. Buurman, and Stefanie B. Flohé. "Lipid-Rich Enteral Nutrition Improves the Defense Against an Opportunistic Infection During Polymicrobial Sepsis." Shock 41, no. 2 (February 2014): 109–14. http://dx.doi.org/10.1097/shk.0000000000000062.

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48

Kamisoglu, Kubra, Kirsten E. Sleight, Steve E. Calvano, Susette M. Coyle, Siobhan A. Corbett, and Ioannis P. Androulakis. "Temporal Metabolic Profiling of Plasma During Endotoxemia in Humans." Shock 40, no. 6 (December 2013): 519–26. http://dx.doi.org/10.1097/shk.0000000000000063.

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Kim, Won Young, Jong Hun Jun, Jin Won Huh, Sang Bum Hong, Chae-Man Lim, and Younsuck Koh. "Radial to Femoral Arterial Blood Pressure Differences in Septic Shock Patients Receiving High-Dose Norepinephrine Therapy." Shock 40, no. 6 (December 2013): 527–31. http://dx.doi.org/10.1097/shk.0000000000000064.

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Zaky, Ahmed, Steven Deem, Karim Bendjelid, and Miriam M. Treggiari. "Characterization of Cardiac Dysfunction in Sepsis." Shock 41, no. 1 (January 2014): 12–24. http://dx.doi.org/10.1097/shk.0000000000000065.

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