Mads Grønborg
Johns Hopkins University
19 Papers
505 Citations
Mads Grønborg is an academic researcher from Johns Hopkins University. The author has contributed to research in topics: Biology & Proteomics. The author has an hindex of 12, co-authored 16 publications. Previous affiliations of Mads Grønborg include Max Planck Society & University of Southern Denmark.
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Papers
Development of Human Protein Reference Database as an Initial Platform for Approaching Systems Biology in Humans
Suraj Peri,Suraj Peri,J. Daniel Navarro,J. Daniel Navarro,Ramars Amanchy,Troels Z. Kristiansen,Troels Z. Kristiansen,Chandra Kiran Jonnalagadda,Vineeth Surendranath,Vidya Niranjan,Babylakshmi Muthusamy,Tejal K. Gandhi,Mads Grønborg,Mads Grønborg,Nieves Ibarrola,Nandan P. Deshpande,K. Shanker,H N Shivashankar,B. P. Rashmi,M A Ramya,Zhixing Zhao,K N Chandrika,N. Padma,H. C. Harsha,A.J. Yatish,M.P. Kavitha,Minal Menezes,Dipanwita Roy Choudhury,Shubha Suresh,Neelanjana Ghosh,R. Saravana,Sreenath Chandran,Subhalakshmi Krishna,Mary Joy,Sanjeev K. Anand,V. Madavan,Ansamma Joseph,Guang W. Wong,William P. Schiemann,Stefan N. Constantinescu,Lily Jun Shen Huang,Roya Khosravi-Far,Hanno Steen,Muneesh Tewari,Saghi Ghaffari,Gerard C. Blobe,Chi V. Dang,Joe G.N. Garcia,Jonathan Pevsner,Ole N. Jensen,Peter Roepstorff,Krishna S. Deshpande,Arul M. Chinnaiyan,Ada Hamosh,Aravinda Chakravarti,Akhilesh Pandey +55 more
TL;DR: The Human Protein Reference Database (HPRD) as mentioned in this paper is an object database that integrates a wealth of information relevant to the function of human proteins in health and disease, including protein-protein interactions, posttranslational modifications, enzyme/substrate relationships, disease associations, tissue expression, and subcellular localization.
Analysis of protein phosphorylation using mass spectrometry: deciphering the phosphoproteome.
TL;DR: Several methods for enrichment of phosphorylated proteins and peptides are outlined and various options for their identification and quantitation are discussed with special emphasis on mass spectrometry-based techniques.
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Biomarker Discovery from Pancreatic Cancer Secretome Using a Differential Proteomic Approach
Mads Grønborg,Mads Grønborg,Troels Zaccharias Glahn Kristiansen,Troels Zaccharias Glahn Kristiansen,Akiko Iwahori,Rubens Chang,Raghunath Reddy,Norihiro Sato,Henrik Molina,Henrik Molina,Ole N. Jensen,Ralph H. Hruban,Michael C. Goggins,Anirban Maitra,Akilesh Pandey +14 more
TL;DR: Stable isotope labeling with amino acids in cell culture (SILAC) method is demonstrated to compare the secreted proteins (secretome) from pancreatic cancer-derived cells with that from non-neoplastic pancreatic ductal cells, confirming the validity of this approach.
531
A Mass Spectrometry-based Proteomic Approach for Identification of Serine/Threonine-phosphorylated Proteins by Enrichment with Phospho-specific Antibodies Identification of a Novel Protein, Frigg, as a Protein Kinase A Substrate
Mads Grønborg,Troels Z. Kristiansen,Allan Stensballe,Jens S. Andersen,Osamu Ohara,Matthias Mann,Ole N. Jensen,Akhilesh Pandey +7 more
TL;DR: Several antibodies are described that recognize phosphoserine/phosphothreonine-containing proteins by Western blotting and can be used to enrich for proteins phosphorylated on serine/threonine residues by immunoprecipitation, as well.
414
Sequential phosphorylation of CCAAT enhancer-binding protein β by MAPK and glycogen synthase kinase 3β is required for adipogenesis
Qi Qun Tang,Mads Grønborg,Haiyan Huang,Haiyan Huang,Jae Woo Kim,Tamara C. Otto,Akhilesh Pandey,M. Daniel Lane +7 more
TL;DR: Ex vivo and in vitro experiments with C/EBPβ show that phosphorylation of Thr-188 by mitogen-activating protein kinase “primes” C/eBPβ for subsequent phosphorylated on Ser-184 and Thr-179 by glycogen synthase kinase 3β, acquisition of DNA-binding function, and transactivation of the C/ EBPα and PPARγ genes appear necessary to allow mitotic clonal expansion.
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