28 research outputs found
Where do firms manage earnings?
Despite decades of research on how, why, and when companies manage earnings, there is a paucity of evidence about the geographic location of earnings management within multinational firms. In this study, we examine where companies manage earnings using a sample of 2,067 U.S. multinational firms from 1994 to 2009. We predict and find that firms with extensive foreign operations in weak rule of law countries have more foreign earnings management than companies with subsidiaries in locations where the rule of law is strong. We also find some evidence that profitable firms with extensive tax haven subsidiaries manage earnings more than other firms and that the earnings management is concentrated in foreign income. Apart from these results, we find that most earnings management takes place in domestic income, not foreign income.Arthur Andersen (Firm) (Arthur Andersen Faculty Fund
Trust within Brazilian new economy organizations: an empirical investigation of gender effects benchmarked on Brazilian old economy organizations
NIST Interlaboratory Study on Glycosylation Analysis of Monoclonal Antibodies: Comparison of Results from Diverse Analytical Methods
Glycosylation is a topic of intense current interest in the
development of biopharmaceuticals because it is related
to drug safety and efficacy. This work describes results of
an interlaboratory study on the glycosylation of the Primary
Sample (PS) of NISTmAb, a monoclonal antibody
reference material. Seventy-six laboratories from industry,
university, research, government, and hospital sectors
in Europe, North America, Asia, and Australia submit-
Avenue, Silver Spring, Maryland 20993; 22Glycoscience Research Laboratory, Genos, Borongajska cesta 83h, 10 000 Zagreb, Croatia;
23Faculty of Pharmacy and Biochemistry, University of Zagreb, A. KovacË icÂŽ a 1, 10 000 Zagreb, Croatia; 24Department of Chemistry, Georgia
State University, 100 Piedmont Avenue, Atlanta, Georgia 30303; 25glyXera GmbH, Brenneckestrasse 20 * ZENIT / 39120 Magdeburg, Germany;
26Health Products and Foods Branch, Health Canada, AL 2201E, 251 Sir Frederick Banting Driveway, Ottawa, Ontario, K1A 0K9 Canada;
27Graduate School of Advanced Sciences of Matter, Hiroshima University, 1-3-1 Kagamiyama Higashi-Hiroshima 739â8530 Japan; 28ImmunoGen,
830 Winter Street, Waltham, Massachusetts 02451; 29Department of Medical Physiology, Jagiellonian University Medical College,
ul. Michalowskiego 12, 31â126 Krakow, Poland; 30Department of Pathology, Johns Hopkins University, 400 N. Broadway Street Baltimore,
Maryland 21287; 31Mass Spec Core Facility, KBI Biopharma, 1101 Hamlin Road Durham, North Carolina 27704; 32Division of Mass
Spectrometry, Korea Basic Science Institute, 162 YeonGuDanji-Ro, Ochang-eup, Cheongwon-gu, Cheongju Chungbuk, 363â883 Korea
(South); 33Advanced Therapy Products Research Division, Korea National Institute of Food and Drug Safety, 187 Osongsaengmyeong 2-ro
Osong-eup, Heungdeok-gu, Cheongju-si, Chungcheongbuk-do, 363â700, Korea (South); 34Center for Proteomics and Metabolomics, Leiden
University Medical Center, P.O. Box 9600, 2300 RC Leiden, The Netherlands; 35Ludger Limited, Culham Science Centre, Abingdon,
Oxfordshire, OX14 3EB, United Kingdom; 36Biomolecular Discovery and Design Research Centre and ARC Centre of Excellence for Nanoscale
BioPhotonics (CNBP), Macquarie University, North Ryde, Australia; 37Proteomics, Central European Institute for Technology, Masaryk
University, Kamenice 5, A26, 625 00 BRNO, Czech Republic; 38Max Planck Institute for Dynamics of Complex Technical Systems, Sandtorstrasse
1, 39106 Magdeburg, Germany; 39Department of Biomolecular Sciences, Max Planck Institute of Colloids and Interfaces, 14424
Potsdam, Germany; 40AstraZeneca, Granta Park, Cambridgeshire, CB21 6GH United Kingdom; 41Merck, 2015 Galloping Hill Rd, Kenilworth,
New Jersey 07033; 42Analytical R&D, MilliporeSigma, 2909 Laclede Ave. St. Louis, Missouri 63103; 43MS Bioworks, LLC, 3950 Varsity Drive
Ann Arbor, Michigan 48108; 44MSD, Molenstraat 110, 5342 CC Oss, The Netherlands; 45Exploratory Research Center on Life and Living
Systems (ExCELLS), National Institutes of Natural Sciences, 5â1 Higashiyama, Myodaiji, Okazaki 444â8787 Japan; 46Graduate School of
Pharmaceutical Sciences, Nagoya City University, 3â1 Tanabe-dori, Mizuhoku, Nagoya 467â8603 Japan; 47Medical & Biological Laboratories
Co., Ltd, 2-22-8 Chikusa, Chikusa-ku, Nagoya 464â0858 Japan; 48National Institute for Biological Standards and Control, Blanche Lane, South
Mimms, Potters Bar, Hertfordshire EN6 3QG United Kingdom; 49Division of Biological Chemistry & Biologicals, National Institute of Health
Sciences, 1-18-1 Kamiyoga, Setagaya-ku, Tokyo 158â8501 Japan; 50New England Biolabs, Inc., 240 County Road, Ipswich, Massachusetts
01938; 51New York University, 100 Washington Square East New York City, New York 10003; 52Target Discovery Institute, Nuffield Department
of Medicine, University of Oxford, Roosevelt Drive, Oxford, OX3 7FZ, United Kingdom; 53GlycoScience Group, The National Institute for
Bioprocessing Research and Training, Fosters Avenue, Mount Merrion, Blackrock, Co. Dublin, Ireland; 54Department of Chemistry, North
Carolina State University, 2620 Yarborough Drive Raleigh, North Carolina 27695; 55Pantheon, 201 College Road East Princeton, New Jersey
08540; 56Pfizer Inc., 1 Burtt Road Andover, Massachusetts 01810; 57Proteodynamics, ZI La Varenne 20â22 rue Henri et Gilberte Goudier 63200
RIOM, France; 58ProZyme, Inc., 3832 Bay Center Place Hayward, California 94545; 59Koichi Tanaka Mass Spectrometry Research Laboratory,
Shimadzu Corporation, 1 Nishinokyo Kuwabara-cho Nakagyo-ku, Kyoto, 604 8511 Japan; 60Childrenâs GMP LLC, St. Jude Childrenâs
Research Hospital, 262 Danny Thomas Place Memphis, Tennessee 38105; 61Sumitomo Bakelite Co., Ltd., 1â5 Muromati 1-Chome, Nishiku,
Kobe, 651â2241 Japan; 62Synthon Biopharmaceuticals, Microweg 22 P.O. Box 7071, 6503 GN Nijmegen, The Netherlands; 63Takeda
Pharmaceuticals International Co., 40 Landsdowne Street Cambridge, Massachusetts 02139; 64Department of Chemistry and Biochemistry,
Texas Tech University, 2500 Broadway, Lubbock, Texas 79409; 65Thermo Fisher Scientific, 1214 Oakmead Parkway Sunnyvale, California
94085; 66United States Pharmacopeia India Pvt. Ltd. IKP Knowledge Park, Genome Valley, Shamirpet, Turkapally Village, Medchal District,
Hyderabad 500 101 Telangana, India; 67Alberta Glycomics Centre, University of Alberta, Edmonton, Alberta T6G 2G2 Canada; 68Department
of Chemistry, University of Alberta, Edmonton, Alberta T6G 2G2 Canada; 69Department of Chemistry, University of California, One Shields Ave,
Davis, California 95616; 70HorvaÂŽ th Csaba Memorial Laboratory for Bioseparation Sciences, Research Center for Molecular Medicine, Doctoral
School of Molecular Medicine, Faculty of Medicine, University of Debrecen, Debrecen, Egyetem ter 1, Hungary; 71Translational Glycomics
Research Group, Research Institute of Biomolecular and Chemical Engineering, University of Pannonia, Veszprem, Egyetem ut 10, Hungary;
72Delaware Biotechnology Institute, University of Delaware, 15 Innovation Way Newark, Delaware 19711; 73Proteomics Core Facility, University
of Gothenburg, Medicinaregatan 1G SE 41390 Gothenburg, Sweden; 74Department of Medical Biochemistry and Cell Biology, University of
Gothenburg, Institute of Biomedicine, Sahlgrenska Academy, Medicinaregatan 9A, Box 440, 405 30, Gothenburg, Sweden; 75Department of
Clinical Chemistry and Transfusion Medicine, Sahlgrenska Academy at the University of Gothenburg, Bruna Straket 16, 41345 Gothenburg,
Sweden; 76Department of Chemistry, University of Hamburg, Martin Luther King Pl. 6 20146 Hamburg, Germany; 77Department of Chemistry,
University of Manitoba, 144 Dysart Road, Winnipeg, Manitoba, Canada R3T 2N2; 78Laboratory of Mass Spectrometry of Interactions and
Systems, University of Strasbourg, UMR Unistra-CNRS 7140, France; 79Natural and Medical Sciences Institute, University of Tuš bingen,
Markwiesenstrae 55, 72770 Reutlingen, Germany; 80Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical
Sciences, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands; 81Division of Bioanalytical Chemistry, Amsterdam Institute for
Molecules, Medicines and Systems, Vrije Universiteit Amsterdam, de Boelelaan 1085, 1081 HV Amsterdam, The Netherlands; 82Department
of Chemistry, Waters Corporation, 34 Maple Street Milford, Massachusetts 01757; 83Zoetis, 333 Portage St. Kalamazoo, Michigan 49007
Authorâs ChoiceâFinal version open access under the terms of the Creative Commons CC-BY license.
Received July 24, 2019, and in revised form, August 26, 2019
Published, MCP Papers in Press, October 7, 2019, DOI 10.1074/mcp.RA119.001677
ER: NISTmAb Glycosylation Interlaboratory Study
12 Molecular & Cellular Proteomics 19.1
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ted a total of 103 reports on glycan distributions. The
principal objective of this study was to report and compare
results for the full range of analytical methods presently
used in the glycosylation analysis of mAbs. Therefore,
participation was unrestricted, with laboratories
choosing their own measurement techniques. Protein glycosylation
was determined in various ways, including at
the level of intact mAb, protein fragments, glycopeptides,
or released glycans, using a wide variety of methods for
derivatization, separation, identification, and quantification.
Consequently, the diversity of results was enormous,
with the number of glycan compositions identified by
each laboratory ranging from 4 to 48. In total, one hundred
sixteen glycan compositions were reported, of which 57
compositions could be assigned consensus abundance
values. These consensus medians provide communityderived
values for NISTmAb PS. Agreement with the consensus
medians did not depend on the specific method or
laboratory type. The study provides a view of the current
state-of-the-art for biologic glycosylation measurement
and suggests a clear need for harmonization of glycosylation
analysis methods. Molecular & Cellular Proteomics
19: 11â30, 2020. DOI: 10.1074/mcp.RA119.001677.L
Qualitative and Quantitative Assessment on the Use of Magnetic Nanoparticles for Glycopeptide Enrichment
Glycoproteomics
represent the field of study of the dynamic changes
occurring among glycoconjugates within the cellular compartments.
Changes in glycosylation have been linked to various diseases, including
metastatic carcinomas in which the 9 carbon sialic acid moiety has
been shown to play a prominent role. The common method used to study
these aberrant changes most often includes a mass spectrometer at
some stage in the workflow. However, serum samples contain many proteins
which inhibit the analysis of these glycosylation changes, and ergo,
enrichment steps are employed as a measure to help alleviate this
ailment. Routinely, this is accomplished using lectins, either alone
or in combination, to retrieve proteins with specific sugar linkages
within the serum sample. This methodology, although known to be very
specific, requires many washing steps, making it a cumbersome addition
to a high throughput workflow. Presented here is an alternative protocol
using custom-made amine functionalized magnetic nanoparticles (MNP)
which are nearly 4Ă smaller than those used before for similar
purposes. The developed protocol is based on both hydrophilic interaction
and weak anion exchange principles, allowing it to target glycopeptides
but, more specifically, those which contain sialylation. For quantification
purposes, tandem mass tags from Thermo Scientific were utilized to
compare the enrichment efficiencies between the magnetic nanoparticle
method and a commercially available glycopeptide enrichment kit offered
through EMD Millipore. The MNP method is fast (âŒ10 min) and
simple and can quantitatively and qualitatively enrich sialylated
glycopeptides more than the commercially available kit
Fluid management, intra-abdominal hypertension and the abdominal compartment syndrome : a narrative review
Ten to fifteen year reassessment of the performance characteristics of the Starr-Edwards Model 6120 mitral valve prosthesis
Fluid Management, Intra-Abdominal Hypertension and the Abdominal Compartment Syndrome: A Narrative Review
BACKGROUND: General pathophysiological mechanisms regarding associations between fluid administration and intra-abdominal hypertension (IAH) are evident, but specific effects of type, amount, and timing of fluids are less clear. OBJECTIVES: This review aims to summarize current knowledge on associations between fluid administration and intra-abdominal pressure (IAP) and fluid management in patients at risk of intra-abdominal hypertension and abdominal compartment syndrome (ACS). METHODS: We performed a structured literature search from 1950 until May 2021 to identify evidence of associations between fluid management and intra-abdominal pressure not limited to any specific study or patient population. Findings were summarized based on the following information: general concepts of fluid management, physiology of fluid movement in patients with intra-abdominal hypertension, and data on associations between fluid administration and IAH. RESULTS: We identified three randomized controlled trials (RCTs), 38 prospective observational studies, 29 retrospective studies, 18 case reports in adults, two observational studies and 10 case reports in children, and three animal studies that addressed associations between fluid administration and IAH. Associations between fluid resuscitation and IAH were confirmed in most studies. Fluid resuscitation contributes to the development of IAH. However, patients with IAH receive more fluids to manage the effect of IAH on other organ systems, thereby causing a vicious cycle. Timing and approach to de-resuscitation are of utmost importance, but clear indicators to guide this decision-making process are lacking. In selected cases, only surgical decompression of the abdomen can stop deterioration and prevent further morbidity and mortality. CONCLUSIONS: Current evidence confirms an association between fluid resuscitation and secondary IAH, but optimal fluid management strategies for patients with IAH remain controversial