Nature Methods 6, 789 (2009). doi:10.1038/nmeth1109-789

Author: Michael Eisenstein

A new in vivo imaging strategy produces detailed maps of tumor microvasculature and lymphatic vessels without injected labels.

Nature Methods 6, 790 (2009). doi:10.1038/nmeth1109-790a

Author: Natalie de Souza

By monitoring the size-dependence of particle distribution in the lamellipodium, fluid flow in moving cells can be measured.

Nature Methods 6, 790 (2009). doi:10.1038/nmeth1109-790b

Author: Nicole Rusk

With a modified polymerase and optimized oligonucleotide chemistry, Helicos' single-molecule sequencer takes on RNA.

Nature Methods 6, 792 (2009). doi:10.1038/nmeth1109-792

Author: Allison Doerr

Researchers use atomic force microscopy to image the chemical structure of the small molecule pentacene, with atomic resolution.

Nature Methods 6, 794 (2009). doi:10.1038/nmeth1109-794

Author: Michael Eisenstein

Certain yeast previously assumed to lack RNA interference machinery instead have alternative enzyme variants, which can in turn be transplanted to truly deficient species.

Nature Methods 6, 805 (2009). doi:10.1038/nmeth.1393

Authors: Tongxiang Lin, Rajesh Ambasudhan, Xu Yuan, Wenlin Li, Simon Hilcove, Ramzey Abujarour, Xiangyi Lin, Heung Sik Hahm, Ergeng Hao, Alberto Hayek & Sheng Ding

The slow kinetics and low efficiency of reprogramming methods to generate human induced pluripotent stem cells (iPSCs) impose major limitations on their utility in biomedical applications. Here we describe a chemical approach that dramatically improves (200-fold) the efficiency of iPSC generation from human fibroblasts, within seven days of treatment. This will provide a basis for developing safer, more efficient, nonviral methods for reprogramming human somatic cells.

Nature Methods 6, 809 (2009). doi:10.1038/nmeth.1392

Authors: Jonas Nilsson, Ulla Rüetschi, Adnan Halim, Camilla Hesse, Elisabet Carlsohn, Gunnar Brinkmalm & Göran Larson

We present a method to enrich for glycoproteins from proteomic samples. Sialylated glycoproteins were selectively periodate-oxidized, captured on hydrazide beads, trypsinized and released by acid hydrolysis of sialic acid glycosidic bonds. Mass spectrometric fragment analysis allowed identification of glycan structures, and additional fragmentation of deglycosylated ions yielded peptide sequence information, which allowed glycan attachment site and protein identification. We identified 36 N-linked and 44 O-linked glycosylation sites on glycoproteins from human cerebrospinal fluid.

Nature Methods 6, 813 (2009). doi:10.1038/nmeth.1389

Authors: Po Hien Ear & Stephen W Michnick

Clonal selection strategies are central tools in molecular biology. We developed a general strategy to dissect protein functions through positive and negative clonal selection for protein-protein interactions, based on a protein-fragment complementation assay using Saccharomyces cerevisiae cytosine deaminase as a reporter. We applied this method to mutational or chemical disruption of protein-protein interactions in yeast and to dissection of the functions of an allosterically activated transcription factor, Swi6.

Nature Methods 6, 817 (2009). doi:10.1038/nmeth.1390

Authors: Martin Beck, Johan A Malmström, Vinzenz Lange, Alexander Schmidt, Eric W Deutsch & Ruedi Aebersold

Nature Methods 6, 825 (2009). doi:10.1038/nmeth.1379

Authors: Yang Wang, Cheom-Gil Cheong, Traci M Tanaka Hall & Zefeng Wang

Nature Methods 6, 831 (2009). doi:10.1038/nmeth.1380

Authors: Taejin L Min, Patrick J Mears, Lon M Chubiz, Christopher V Rao, Ido Golding & Yann R Chemla

Nature Methods 6, 837 (2009). doi:10.1038/nmeth.1391

Authors: Marieke Simonis, Petra Klous, Irene Homminga, Robert-Jan Galjaard, Erik-Jan Rijkers, Frank Grosveld, Jules P P Meijerink & Wouter de Laat

Nature Methods 6, 843 (2009). doi:10.1038/nmeth.1394

Authors: Matija Dreze, Benoit Charloteaux, Stuart Milstein, Pierre-Olivier Vidalain, Muhammed A Yildirim, Quan Zhong, Nenad Svrzikapa, Viviana Romero, Géraldine Laloux, Robert Brasseur, Jean Vandenhaute, Mike Boxem, Michael E Cusick, David E Hill & Marc Vidal

Nature Methods 6, 851 (2009). doi:10.1038/nmeth1109-851

Author: Alan Dove

Antibodies, the molecular workhorses of protein research, have traditionally been one of the most difficult reagents to procure. Using innovative new technologies, though, a burgeoning antibody production industry is turning these molecules into commodities.