Advances in Experimental Medicine and Biology Journal Impact Factor & Information

Publisher: Kluwer

Journal description

Current impact factor: 1.96

Impact Factor Rankings

2015 Impact Factor Available summer 2016
2014 Impact Factor 1.958
2012 Impact Factor 1.825
2011 Impact Factor 1.093
2010 Impact Factor 1.379
2009 Impact Factor 2.02
2008 Impact Factor 0.663
2007 Impact Factor 0.663
2006 Impact Factor 0.646
2005 Impact Factor 0.635
2004 Impact Factor 0.642
2000 Impact Factor 0.513
1999 Impact Factor 0.446
1998 Impact Factor 0.36

Impact factor over time

Impact factor

Additional details

5-year impact 1.70
Cited half-life 6.30
Immediacy index 0.59
Eigenfactor 0.03
Article influence 0.56
Website Advances in Experimental Medicine & Biology website
Other titles Advances in experimental medicine and biology, Experimental medicine and biology
ISSN 0065-2598
OCLC 1461189
Material type Series
Document type Journal / Magazine / Newspaper

Publisher details


  • Pre-print
    • Author can archive a pre-print version
  • Post-print
    • Author can archive a post-print version
  • Conditions
    • Authors own final version can be archived
    • Publisher's protected PDF can be used for a fee
    • Published source must be acknowledged
    • Must link to publisher version
    • Articles in some journals can be made Open Access on payment of additional charge
    • 'Kluwer' is an imprint of 'Springer Verlag (Germany)'
  • Classification
    ​ green

Publications in this journal

  • Advances in Experimental Medicine and Biology 01/2016; DOI:10.1007/978-3-319-17121-0_24
  • Advances in Experimental Medicine and Biology 01/2016;
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    ABSTRACT: King Hussein Cancer (KHCC) is a specialized cancer center that treats both adult and pediatric cancer patients from Jordan and the neighboring countries. KHCC is acknowledged as a leader in cancer treatment in the Middle East and its vision is to maintain its leading position in cancer therapy and research. Hence, KHCC embarked on establishing the first ISO compliant cancer biobank (KHCCBIO) in Jordan.Currently, there are very few biobanks in the Middle East, hence, KHCC wanted to change this situation by establishing an ISO-compliant cancer biobank which would incorporate all current international guidelines and best-in class practices under an approved quality management system for the benefit of researchers in Jordan, its neighboring countries, and throughout the world. The established biobank would follow the highest ethical standards in collecting, processing, storing and distributing high-quality, clinically annotated biospecimens.The strategy used in establishing KHCCBIO was based on taking advantage of international networking and collaboration. This in essence led to knowledge transfer between well established organizations, institutions and individuals from Europe and Jordan, in existing technological innovation and internationally recognized quality standards. KHCC efforts were facilitated by a grant from the European Union under the seventh frame work program.Future aims of KHCCBIO are to develop KHCC's research infrastructure, increase its scope and visibility and improve its competitiveness throughout the biomedical science arena. Moreover, KHCCBIO is aiming to establish a platform for future knowledge transfer and collaborative research; develop partnerships between European and Middle Eastern organizations.
    Advances in Experimental Medicine and Biology 10/2015; 864:141.
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    ABSTRACT: The scientific community's major conceptual notion of structural biology has recently shifted in emphasis from the classical structure-function paradigm due to the emergence of intrinsically disordered proteins (IDPs). As opposed to their folded cousins, these proteins are defined by the lack of a stable 3D fold and a high degree of inherent structural heterogeneity that is closely tied to their function. Due to their flexible nature, solution techniques such as small-angle X-ray scattering (SAXS), nuclear magnetic resonance (NMR) spectroscopy and fluorescence resonance energy transfer (FRET) are particularly well-suited for characterizing their biophysical properties. Computationally derived structural ensembles based on such experimental measurements provide models of the conformational sampling displayed by these proteins, and they may offer valuable insights into the functional consequences of inherent flexibility. The Protein Ensemble Database ( is the first openly accessible, manually curated online resource storing the ensemble models, protocols used during the calculation procedure, and underlying primary experimental data derived from SAXS and/or NMR measurements. By making this previously inaccessible data freely available to researchers, this novel resource is expected to promote the development of more advanced modelling methodologies, facilitate the design of standardized calculation protocols, and consequently lead to a better understanding of how function arises from the disordered state.
    Advances in Experimental Medicine and Biology 09/2015; 870:335-349. DOI:10.1007/978-3-319-20164-1_11
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    ABSTRACT: Intrinsically disordered proteins (IDPs) perform their function despite their lack of well-defined tertiary structure. Residual structure has been observed in IDPs, commonly described as transient/dynamic or expressed in terms of fractional populations. In order to understand how the protein primary sequence dictates the dynamic and structural properties of IDPs and in general to understand how IDPs function, atomic-level descriptions are needed. Nuclear magnetic resonance spectroscopy provides information about local and long-range structure in IDPs at amino acid specific resolution and can be used in combination with ensemble descriptions to represent the dynamic nature of IDPs. In this chapter we describe sample-and-select approaches for ensemble modelling of local structural propensities in IDPs with specific emphasis on validation of these ensembles.
    Advances in Experimental Medicine and Biology 09/2015; 870:123-147. DOI:10.1007/978-3-319-20164-1_4
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    ABSTRACT: Beta amyloid protein (Aβ) is one of the intrinsically disordered proteins associated with neurodegenerative diseases like Parkinson's, prion disease and Alzheimer's disease (AD) in particular. Although the direct involvement of Aβ peptides in AD is well documented and their aggregative ability is closely related to their neurotoxicity, the precise mechanism of the neurotoxic effects of Aβ peptides remains unclear. There is still a significant gap between the site-specific structural information and the complex structural diversity of Aβ amyloids. The description of the structural polymorphisms of Aβ amyloids can provide valuable information of the molecular basis of AD onset-progress and is essential for comprehension of the Aβ aggregation pathways, in particular its structural evolution. In this review we tried to illustrate the emerging trend of defining several human neurodegenerative disorders as syndromes of protein folding and oligomerization through the example of AD.
    Advances in Experimental Medicine and Biology 09/2015; 870:401-421. DOI:10.1007/978-3-319-20164-1_14
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    ABSTRACT: From the 1970s to the present, regions of missing electron density in protein structures determined by X-ray diffraction and the characterization of the functions of these regions have suggested that not all protein regions depend on prior 3D structure to carry out function. Motivated by these observations, in early 1996 we began to use bioinformatics approaches to study these intrinsically disordered proteins (IDPs) and IDP regions. At just about the same time, several laboratory groups began to study a collection of IDPs and IDP regions using nuclear magnetic resonance. The temporal overlap of the bioinformatics and NMR studies played a significant role in the development of our understanding of IDPs. Here the goal is to recount some of this history and to project from this experience possible directions for future work.
    Advances in Experimental Medicine and Biology 09/2015; 870:1-34. DOI:10.1007/978-3-319-20164-1_1
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    ABSTRACT: In this review we summarize available data showing the abundance of structural disorder within the nucleoprotein (N) and phosphoprotein (P) from three paramyxoviruses, namely the measles (MeV), Nipah (NiV) and Hendra (HeV) viruses. We provide a detailed description of the molecular mechanisms that govern the disorder-to-order transition that the intrinsically disordered C-terminal domain (NTAIL) of their N proteins undergoes upon binding to the C-terminal X domain (XD) of the homologous P proteins. We also show that a significant flexibility persists within NTAIL-XD complexes, which therefore provide illustrative examples of "fuzziness". The functional implications of structural disorder for viral transcription and replication are discussed in light of the ability of disordered regions to establish a complex molecular partnership and to confer a considerable reach to the elements of the replicative machinery.
    Advances in Experimental Medicine and Biology 09/2015; 870:351-381. DOI:10.1007/978-3-319-20164-1_12
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    ABSTRACT: Small-angle X-ray scattering (SAXS) is a powerful structural method allowing one to study the structure, folding state and flexibility of native particles and complexes in solution and to rapidly analyze structural changes in response to variations in external conditions. New high brilliance sources and novel data analysis methods significantly enhanced resolution and reliability of structural models provided by the technique. Automation of the SAXS experiment, data processing and interpretation make solution SAXS a streamline tool for large scale structural studies in molecular biology. The method provides low resolution macromolecular shapes ab initio and is readily combined with other structural and biochemical techniques in integrative studies. Very importantly, SAXS is sensitive to macromolecular flexibility being one of the few structural techniques applicable to flexible systems and intrinsically disordered proteins (IDPs). A major recent development is the use of SAXS to study particle dynamics in solution by ensemble approaches, which allow one to quantitatively characterize flexible systems. Of special interest is the joint use of SAXS with solution NMR, given that both methods yield highly complementary structural information, in particular, for IDPs. In this chapter, we present the basics of SAXS and also consider protocols of the experiment and data analysis for different scenarios depending on the type of the studied object. These include ab initio shape reconstruction, validation of available high resolution structures and rigid body modelling for folded macromolecules and also characterisation of flexible proteins with the ensemble methods. The methods are illustrated by examples of recent applications and further perspectives of the integrative use of SAXS with NMR in the studies of IDPs are discussed.
    Advances in Experimental Medicine and Biology 09/2015; 870:261-289. DOI:10.1007/978-3-319-20164-1_8
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    ABSTRACT: Thanks to recent improvements in NMR instrumentation, pulse sequence design, and sample preparation, a panoply of new NMR tools has become available for atomic resolution characterization of intrinsically disordered proteins (IDPs) that are optimized for the particular chemical and spectroscopic properties of these molecules. A wide range of NMR observables can now be measured on increasingly complex IDPs that report on their structural and dynamic properties in isolation, as part of a larger complex, or even inside an entire living cell. Herein we present basic NMR concepts, as well as optimised tools available for the study of IDPs in solution. In particular, the following sections are discussed hereafter: a short introduction to NMR spectroscopy and instrumentation (Sect. 3.1), the effect of order and disorder on NMR observables (Sect. 3.2), particular challenges and bottlenecks for NMR studies of IDPs (Sect. 3.3), 2D HN and CON NMR experiments: the fingerprint of an IDP (Sect. 3.4), tools for overcoming major bottlenecks of IDP NMR studies (Sect. 3.5), (13)C detected experiments (Sect. 3.6), from 2D to 3D: from simple snapshots to site-resolved characterization of IDPs (Sect. 3.7), sequential NMR assignment: 3D experiments (Sect. 3.8), high-dimensional NMR experiments (nD, with n > 3) (Sect. 3.9) and conclusions and perspectives (Sect. 3.10).
    Advances in Experimental Medicine and Biology 09/2015; 870:49-122. DOI:10.1007/978-3-319-20164-1_3
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    ABSTRACT: Intrinsically disordered proteins (IDPs) are characterized by substantial conformational flexibility and thus not amenable to conventional structural biology techniques. Given their inherent structural flexibility NMR spectroscopy offers unique opportunities for structural and dynamic studies of IDPs. The past two decades have witnessed significant development of NMR spectroscopy that couples advances in spin physics and chemistry with a broad range of applications. This chapter will summarize key advances in NMR methodology. Despite the availability of efficient (multi-dimensional) NMR experiments for signal assignment of IDPs it is discussed that NMR of larger and more complex IDPs demands spectral simplification strategies capitalizing on specific isotope-labeling strategies. Prototypical applications of isotope labeling-strategies are described. Since IDP-ligand association and dissociation processes frequently occur on time scales that are amenable to NMR spectroscopy we describe in detail the application of CPMG relaxation dispersion techniques to studies of IDP protein binding. Finally, we demonstrate that the complementary usage of NMR and EPR data provide a more comprehensive picture about the conformational states of IDPs and can be employed to analyze the conformational ensembles of IDPs.
    Advances in Experimental Medicine and Biology 09/2015; 870:149-185. DOI:10.1007/978-3-319-20164-1_5
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    ABSTRACT: Intrinsically disordered proteins (IDPs) and hybrid proteins possessing ordered domains and intrinsically disordered protein regions (IDPRs) are highly abundant in various proteomes. They are different from ordered proteins at many levels, and an unambiguous representation of an IDP structure is a difficult task. In fact, IDPs show an extremely wide diversity in their structural properties, being able to attain extended conformations (random coil-like) or to remain globally collapsed (molten globule-like). Disorder can differently affect different parts of a protein, with some regions being more ordered than others. IDPs and IDPRs exist as dynamic ensembles, resembling "protein-clouds". IDP structures are best presented as conformational ensembles that contain highly dynamic structures interconverting on a number of timescales. The determination of a unique high-resolution structure is not possible for an isolated IDP, and a detailed structural and dynamic characterization of IDPs cannot typically be provided by a single tool. Therefore, accurate descriptions of IDPs/IDPRs rely on a multiparametric approach that includes a host of biophysical methods that can provide information on the overall compactness of IDPs and their conformational stability, shape, residual secondary structure, transient long-range contacts, regions of restricted or enhanced mobility, etc. The goal of this chapter is to provide a brief overview of some of the components of this multiparametric approach.
    Advances in Experimental Medicine and Biology 09/2015; 870:215-260. DOI:10.1007/978-3-319-20164-1_7
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    ABSTRACT: Although the proteins in all the current major classes considered to be druggable are folded in their native states, intrinsically disordered proteins (IDPs) are becoming attractive candidates for therapeutic intervention by small drug-like molecules. IDPs are challenging targets because they exist as ensembles of structures, thereby making them unsuitable for standard rational drug design approaches, which require the knowledge of the three-dimensional structure of the proteins to be drugged. As we review in this chapter, several different small molecule strategies are currently under investigation to target IDPs, including: (i) to stabilise IDPs in their natively disordered states, (ii) to inhibit interactions with ordered or disordered protein partners, and (iii) to induce allosteric inhibition. In this context, biophysical techniques, including in particular nuclear magnetic resonance (NMR) spectroscopy and small-angle X-ray scattering (SAXS) coupled with molecular dynamics simulations and chemoinformatics approaches, are increasingly used to characterize the structural ensembles of IDPs and the specific interactions that they make with their binding partners. By analysing the results of recent studies, we describe the main structural features that may render IDPs druggable, and describe techniques that can be used for drug discovery programs focused on IDPs.
    Advances in Experimental Medicine and Biology 09/2015; 870:383-400. DOI:10.1007/978-3-319-20164-1_13
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    ABSTRACT: Investigating the activity and structure of cellular biochemical machinery at atomic resolution has been a point of paramount significance for understanding health and disease over the decades. The underlying molecular mechanisms are primarily studied in vitro. Nuclear magnetic resonance (NMR) is a technique that allows to look into cells and study proteins and other constituents, thanks to careful experimental design and technological advances (spectrometer sensitivity and pulse sequence design). Here we outline current applications of the technique and propose a realistic future for the field.
    Advances in Experimental Medicine and Biology 09/2015; 870:319-334. DOI:10.1007/978-3-319-20164-1_10
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    ABSTRACT: The growing recognition of the several roles that intrinsically disordered proteins play in biology places an increasing importance on protein sample availability to allow the characterization of their structural and dynamic properties. The sample preparation is therefore the limiting step to allow any biophysical method being able to characterize the properties of an intrinsically disordered protein and to clarify the links between these properties and the associated biological functions.An increasing array of tools has been recruited to help prepare and characterize the structural and dynamic properties of disordered proteins. This chapter describes their sample preparation, covering the most common drawbacks/barriers usually found working in the laboratory bench. We want this chapter to be the bedside book of any scientist interested in preparing intrinsically disordered protein samples for further biophysical analysis.
    Advances in Experimental Medicine and Biology 09/2015; 870:187-213. DOI:10.1007/978-3-319-20164-1_6
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    ABSTRACT: Intrinsically disordered proteins (IDPs) are involved in a wide range of essential biological processes, including in particular signalling and regulation. We are only beginning, however, to develop a detailed knowledge of the structure and dynamics of these proteins. It is becoming increasingly clear that, as IDPs populate highly heterogeneous states, they should be described in terms of conformational ensembles rather than as individual structures, as is instead most often the case for the native states of globular proteins. Within this context, in this chapter we describe the conceptual tools and methodological aspects associated with the description of the structure and dynamics of IDPs in terms of conformational ensembles. A major emphasis is given to methods in which molecular simulations are used in combination with experimental nuclear magnetic resonance (NMR) measurements, as they are emerging as a powerful route to achieve an accurate determination of the conformational properties of IDPs.
    Advances in Experimental Medicine and Biology 09/2015; 870:35-48. DOI:10.1007/978-3-319-20164-1_2
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    ABSTRACT: One of the great challenges of mechanistic ion-channel biology is to obtain structural information from well-defined functional states. In the case of neurotransmitter-gated ion channels, the open-channel conformation is particularly elusive owing to its transient nature and brief mean lifetime. In this Chapter, we show how the analysis of single-channel currents recorded from mutants engineered to contain single ionizable side chains in the transmembrane region can provide specific information about the open-channel conformation without any interference from the closed or desensitized conformations. The method takes advantage of the fact that the alternate binding and unbinding of protons to and from an ionizable side chain causes the charge of the protein to fluctuate by 1 unit. We show that, in mutant muscle acetylcholine nicotinic receptors (AChRs), this fluctuating charge affects the rate of ion conduction in such a way that individual proton-transfer events can be identified in a most straightforward manner. From the extent to which the single-channel current amplitude is reduced every time a proton binds, we can learn about the proximity of the engineered side chain to the lumen of the pore. And from the kinetics of proton binding and unbinding, we can calculate the side-chain's affinity for protons (pK a), and hence, we can learn about the electrostatic properties of the microenvironment around the introduced ionizable group. The application of this method to systematically mutated AChRs allowed us to identify unambiguously the stripes of the M1, M2 and M3 transmembrane α-helices that face the pore's lumen in the open-channel conformation in the context of a native membrane.
    Advances in Experimental Medicine and Biology 09/2015; 869:5-23. DOI:10.1007/978-1-4939-2845-3_2
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    ABSTRACT: Nature has incorporated small photochromic molecules, colloquially termed 'photoswitches', in photoreceptor proteins to sense optical cues in phototaxis and vision. While Nature's ability to employ light-responsive functionalities has long been recognized, it was not until recently that scientists designed, synthesized and applied synthetic photochromes to manipulate many of which open rapidly and locally in their native cell types, biological processes with the temporal and spatial resolution of light. Ion channels in particular have come to the forefront of proteins that can be put under the designer control of synthetic photochromes. Photochromic ion channel controllers are comprised of three classes, photochromic soluble ligands (PCLs), photochromic tethered ligands (PTLs) and photochromic crosslinkers (PXs), and in each class ion channel functionality is controlled through reversible changes in photochrome structure. By acting as light-dependent ion channel agonists, antagonist or modulators, photochromic controllers effectively converted a wide range of ion channels, including voltage-gated ion channels, 'leak channels', tri-, tetra- and pentameric ligand-gated ion channels, and temperature-sensitive ion channels, into man-made photoreceptors. Control by photochromes can be reversible, unlike in the case of 'caged' compounds, and non-invasive with high spatial precision, unlike pharmacology and electrical manipulation. Here, we introduce design principles of emerging photochromic molecules that act on ion channels and discuss the impact that these molecules are beginning to have on ion channel biophysics and neuronal physiology.
    Advances in Experimental Medicine and Biology 09/2015; 869:101-17. DOI:10.1007/978-1-4939-2845-3_6